Lyophilized and sprayable silk fibroin and modified silk fibroin forms

Abstract

The disclosure relates to lyophilized or sprayable peptide compositions, e.g., lyophilized or sprayable silk fibroin derived peptide compositions.

Description

[0001]LYOPHILIZED AND SPRAYABLE SILK FIBROIN AND MODIFIED SILK FIBROIN FORMS CROSS REFERENCE TO RELATED APPLICATIONS This application claims the benefit of priority of U.S. Provisional Patent Application No.63 / 656,512 filed June 5, 2024, which is incorporated by reference herein in its entirety. FIELD The disclosure relates to peptide compositions, e.g., silk fibroin derived peptide composition. BACKGROUND Silk is a natural polymer produced by a variety of insects and spiders, and comprises a filament core protein, silk fibroin, and a glue-like coating consisting of a non-filamentous protein, sericin. SUMMARY Embodiments of the present disclosure provide a plurality of substantially solid particles comprising silk fibroin fragments, the particles being characterized by at least one of: bulk density, surface area, pore size, pore volume, aspect ratio, and / or Hausner ratio. In some embodiments, the substantially solid particles are annealed. In some embodiments, the substantially solid particles are grounded. In some embodiments, the plurality of substantially solid particles comprise a pH modifier. In some embodiments, the pH modifier is selected from sodium hydroxide and Ammonium hydroxide. In some embodiments, the pH modifier is present in the pellet in an amount ranging from about 25 ppm to about 10,000. In some embodiments, the substantially solid particles have a bulk density of less than 0.03 g / ml, less than 0.04 g / ml, less than 0.05 g / ml, less than 0.06 g / ml, less than 0.07 g / ml, less than 0.08 g / ml, less than 0.09 g / ml, less than 0.10 g / ml, less than 0.11 g / ml, less than 0.12 g / ml, less than 0.13 g / ml, less than 0.14 g / ml, less than 0.15 g / ml, less than 0.16 g / ml, less than 0.17 g / ml, less than 0.18 g / ml, less than 0.19 g / ml, less than 0.20 g / ml, less than 0.21 g / ml, less than 0.22 g / ml, less than 0.23 g / ml, less than 0.24 g / ml, or less than 0.25 g / ml, less than 0.26 g / ml, less than 0.27 g / ml, less than 0.28 g / ml, less than 0.29 g / ml, less than 0.30 g / ml, less than 0.31 g / ml, less than 0.32 g / ml, less than 0.33 g / ml, less than 0.34 g / ml, or less than 0.35 g / ml. In some DB1 / 158748174.5 1 embodiments, the substantially solid particles have an average bulk density of about 0.03 g / ml, about 0.04 g / ml, or about 0.05 g / ml, about 0.03 g / ml, about 0.04 g / ml, about 0.05 g / ml, about 0.06 g / ml, about 0.07 g / ml, about 0.08 g / ml, about 0.09 g / ml, about 0.10 g / ml, about 0.11 g / ml, about 0.12 g / ml, about 0.13 g / ml, about 0.14 g / ml, about 0.15 g / ml, about 0.16 g / ml, about 0.17 g / ml, about 0.18 g / ml, about 0.19 g / ml, about 0.20 g / ml, about 0.21 g / ml, about 0.22 g / ml, about 0.23 g / ml, about 0.24 g / ml, about 0.25 g / ml, about 0.26 g / ml, about 0.27 g / ml, about 0.28 g / ml, about 0.29 g / ml, about 0.30 g / ml, about 0.31 g / ml, about 0.32 g / ml, about 0.33 g / ml, about 0.34 g / ml, or about 0.35 g / ml. In some embodiments, the substantially solid particles have a Hausner ratio of between 1.00 and 1.11, between 1.12 and 1.18, between 1.19 and 1.25, between 1.26 and 1.34, or between 1.35 and 1.45. In some embodiments, the substantially solid particles have an average diameter of between about 3 mm and about 10 mm. In some embodiments, the substantially solid particles have an average diameter of about 1 mm, about 2 mm, about 3 mm, about 4 mm, about 5 mm, about 6 mm, about 7 mm, about 8 mm, about 9 mm, about 10 mm, about 11 mm, about 12 mm, about 13 mm, about 14 mm, about 15 mm, about 16 mm, about 17 mm, about mm, about 18 mm, about 19 mm, or about 20 mm. In some embodiments, the substantially solid particles have an aspect ratio between 1 and about 1.45. In some embodiments, the substantially solid particles have an aspect ratio of 1, about 1.10, about 1.15, about 1.20, about 1.25, about 1.30, about 1.35, about 1.40, or about 1.45. In some embodiments, the substantially solid particles have an aspect ratio of 1, about 1.10, about 1.11, about 1.12, about 1.13, about 1.14, about 1.15, about 1.16, about 1.17, about 1.18, about 1.19, about 1.20, about 1.21, about 1.22, about 1.23, about 1.24, about 1.25, about 1.26, about 1.27, about 1.28, about 1.29, about 1.30, about 1.31, about 1.32, about 1.33, about 1.34, about 1.35, about 1.36, about 1.37, about 1.38, about 1.39, about 1.40, about 1.41, about 1.42, about 1.43, about 1.44, about 1.45, about 1.46, about 1.47, about 1.48, about 1.49, or about 1.50. In some embodiments, the substantially solid particles are substantially spherical. In some embodiments, the substantially solid particles are mesoporous. In some embodiments, the substantially solid particles have a BET (Brunauer–Emmett–Teller) surface area between about 2.50 m2 / g and about 6.50 m2 / g. In some embodiments, the substantially solid particles have a BET (Brunauer–Emmett–Teller) surface area of between about 2.50 m2 / g and about 3.00 m2 / g, about 3.00 m2 / g and about 3.50 m2 / g, about 3.50 m2 / g and about 4.00 m2 / g, about 4.00 m2 / g and about 4.50 m2 / g, about 4.50 m2 / g and about DB1 / 158748174.5 2 5.00 m2 / g, about 5.00 m2 / g and about 5.50 m2 / g, about 5.50 m2 / g and about 6.00 m2 / g, or about 6.00 m2 / g and about 6.50 m2 / g. In some embodiments, the substantially solid particles have an average pore size between about 25 Å and about 500 Å. In some embodiments, the substantially solid particles have an average pore size of about 25 Å to about 30 Å, about 30 Å to about 35 Å, about 35 Å to about 40 Å, about 40 Å to about 45 Å, about 45 Å to about 50 Å, about 50 Å to about 55 Å, about 55 Å to about 60 Å, about 60 Å to about 65 Å, about 65 Å to about 70 Å, about 70 Å to about 75 Å, about 75 Å to about 80 Å, about 80 Å to about 85 Å, about 85 Å to about 90 Å, about 90 Å to about 95 Å, about 95 Å to about 100 Å, about 100 Å to about 105 Å, about 105 Å to about 110 Å, about 110 Å to about 115 Å, about 115 Å to about 120 Å, about 120 Å to about 125 Å, about 125 Å to about 130 Å, about 130 Å to about 135 Å, about 135 Å to about 140 Å, about 140 Å to about 145 Å, or about 145 Å to about 150 Å. In some embodiments, a substantially solid silk fibroin particle comprises a plurality of radially orientated microchannels. In some embodiments, the substantially solid silk fibroin particle comprises an emulsifier, a surfactant, a buffering agent, an amino acid, or a sugar. In some embodiments, the substantially solid silk fibroin particle comprises a polysaccharide, a polysorbate, a glycoside, PBS, arginine, trehalose, glucose, or sucrose. In some embodiments, the substantially solid silk fibroin particle comprises a surfactant selected from sucrose ester, cetearyl glucoside, caprylyl / capryl glucoside, sucrose laurate, sucrose palmitate, sucrose stearate, sucrose cocoate, sorbitan monostearate, and combinations thereof. In some embodiments, the substantially solid silk fibroin particle comprises an additional protein or peptide, a C12-C24 fatty alcohol, a glycolipid, or a lipid. In some embodiments, the substantially solid silk fibroin particle comprises a protein, a peptide, a sugar surfactant, a biosurfactant, a lipid, or a combination. In some embodiments, the substantially solid silk fibroin particle comprises a sugar fatty acid ester, a sugar fatty acid monoester, a sugar fatty diester, a sugar fatty triester, or a sugar fatty and polyester. In some embodiments, the substantially solid silk fibroin particle comprises a sucrose fatty acid ester, a sorbitan or sorbitol fatty acid ester, an alkyl glucoside, an alkyl polyglucoside, or a combination thereof. In some embodiments, the substantially solid silk fibroin particle comprises KCl, NaCl, MgCl2, CaCl2, PBS, Tris, Polysorbate 20, Polysorbate 80, Capryl Glucoside, Sucrose, Histidine, Glycine, or Arginine. In some embodiments, a stabilizer is selected from a polysaccharide, e.g., and without limitation, maltodextrins, dextran, a surfactant, e.g., and without DB1 / 158748174.5 3 limitation, polysorbate (20, 60, 80), capryl glucoside, a buffering agent, e.g., and without limitation, PBS, tris acetate, sodium phosphate, an amino acid, e.g., and without limitation, arginine, glycine, cysteine, histidine, lysine, serine, and / or a sugar, e.g., and without limitation, trehalose, glucose, sucrose, maltose, fucose. Embodiments of the present disclosure provide a silk fibroin nanoclay composite or film, comprising silk fibroin fragments and a clay, wherein the % (w / w) of clay in the composite is from about 1% to about 99%. In some embodiments, the clay is a bentonite clay. In some embodiments, the concentration of clay in the composite or film is from about 20% (w / w) to about 33% (w / w), from about 33% (w / w) to about 50% (w / w), or from about 50% (w / w) to about 67% (w / w). In some embodiments, the water vapor permeance (WVP) of the composite is inversely proportional to the concentration of clay in the composite. In some embodiments, water vapor permeance (WVP, g / m2*Pa*24h) of the composite is from about 0.20 to about 0.30, from about 0.30 to about 0.35, from about 0.35 to about 0.40, from about 0.40 to about 0.45, from about 0.45 to about 0.50, from about 0.50 to about 0.55, from about 0.55 to about 0.60, from about 0.60 to about 0.65, from about 0.65 to about 0.70, from about 0.70 to about 0.75, from about 0.75 to about 0.80, or from about 0.80 to about 0.85. Embodiments of the present disclosure provide a stabilized silk fibroin solution comprising silk fibroin fragments and a stabilizer, wherein the solution has a z-average value lower than a substantially similar silk fibroin solution comprising silk fibroin fragments but excluding the stabilizer, and / or the solution has a z-average plateau value lower than a substantially similar silk fibroin solution comprising silk fibroin fragments but excluding the stabilizer. In some embodiments, the z-average is measured after a period of time after the silk fibroin fragments and the stabilizer are co-formulated, wherein the period time ranges from 1 hour to 250 hours, from 1 hour to 350 hours, from 1 hour to 450 hours, from 1 hour to 550 hours, from 1 hour to 650 hours, or from 1 hour to 1000 hours. In some embodiments, the z-average is measured after a period of time after the silk fibroin fragments and the stabilizer are co- formulated, wherein the period time ranges from 1 minute to 10 minutes, from 1 minute to 20 minutes, from 1 minute to 30 minutes, from 1 minute to 40 minutes, from 1 minute to 50 minutes, from 1 minute to 60 minutes, from 1 minute to 70 minutes, or from 1 minute to 80 minutes. In some embodiments, the stabilizer is an emulsifier, a surfactant, a buffering agent, an amino acid, or a sugar. In some DB1 / 158748174.5 4 embodiments, the stabilizer is a polysaccharide, a polysorbate, a glycoside, PBS, arginine, trehalose, glucose, or sucrose. In some embodiments, the stabilizer is a surfactant selected from sucrose ester, cetearyl glucoside, caprylyl / capryl glucoside, sucrose laurate, sucrose palmitate, sucrose stearate, sucrose cocoate, sorbitan monostearate, and combinations thereof. In some embodiments, the stabilizer is an additional protein or peptide, a C12-C24 fatty alcohol, a glycolipid, or a lipid. In some embodiments, the stabilizer is a protein, a peptide, a sugar surfactant, a biosurfactant, a lipid, or a combination. In some embodiments, the stabilizer is a sugar fatty acid ester, a sugar fatty acid monoester, a sugar fatty diester, a sugar fatty triester, or a sugar fatty and polyester. In some embodiments, the stabilizer is a sucrose fatty acid ester, a sorbitan or sorbitol fatty acid ester, an alkyl glucoside, an alkyl polyglucoside, or a combination thereof. In some embodiments, the stabilizer is KCl, NaCl, MgCl2, CaCl2, PBS, Tris, Polysorbate 20, Polysorbate 80, Capryl Glucoside, Sucrose, Histidine, Glycine, or Arginine. In some embodiments, a stabilizer is selected from a polysaccharide, e.g., and without limitation, maltodextrins, dextran, a surfactant, e.g., and without limitation, polysorbate (20, 60, 80), capryl glucoside, a buffering agent, e.g., and without limitation, PBS, tris acetate, sodium phosphate, an amino acid, e.g., and without limitation, arginine, glycine, cysteine, histidine, lysine, serine, and / or a sugar, e.g., and without limitation, trehalose, glucose, sucrose, maltose, fucose. In some embodiments, the solution is sprayable. Embodiments of the present disclosure provide a liquid in air suspension comprising a plurality of droplets comprising the stabilized silk fibroin solution described above, wherein the droplets are sufficiently stable after being sprayed, for a period of time necessary to reach a surface. In some embodiments, the droplets or drops are sufficiently stable after being formed, for a period of time necessary to reach a surface. In some embodiments, the silk fibroin fragments in any of the embodiments of the plurality of substantially solid particles, the silk fibroin nanoclay composite or film, the stabilized silk fibroin solution, the liquid in air suspension, or the plurality of drops or droplets described herein, have a weight average molecular weight selected from between about 1 kDa and about 5 kDa, from between about 5 kDa and about 10 kDa, from between about 6 kDa and about 17 kDa, from between about 10 kDa and about 15 kDa, from between about 14 kDa and about 30 kDa, from between about 15 kDa and about 20 kDa, from between about 17 kDa and about 39 kDa, from between about 20 kDa and about 25 kDa, from between about 25 kDa and about 30 kDa, from DB1 / 158748174.5 5 between about 30 kDa and about 35 kDa, from between about 35 kDa and about 40 kDa, from between about 39 kDa and about 54 kDa, from between about 39 kDa and about 80 kDa, from between about 40 kDa and about 45 kDa, from between about 45 kDa and about 50 kDa, from between about 50 kDa and about 55 kDa, from between about 55 kDa and about 60 kDa, from between about 60 kDa and about 100 kDa, from between about 80 kDa and about 144 kDa, from between about 144 kDa and about 250 kDa, or from between about 250 kDa and about 350 kDa, and a polydispersity from 1 to about 5. In some embodiments, the polydispersity of any of the above mentioned embodiments is from 1 to about 1.5, from about 1.5 to about 2.0, from about 2.0 to about 2.5, from about 2.5 to about 3.0, from about 3.0 to about 3.5, from about 3.5 to about 4.0, from about 4.0 to about 4.5, or from about 4.5 to about 5.0. Any of the above mentioned embodiments may further comprise about 0.001% (w / w) to about 10% (w / w) sericin relative to the silk fibroin fragments. In any of the above mentioned embodiments, the silk fibroin fragments do not spontaneously or gradually gelate and do not visibly change in color or turbidity when in an aqueous solution for at least 10 days prior to being formulated into the substantially solid particles, the silk fibroin nanoclay composite or film, or the stabilized silk fibroin solution. In any of the embodiments of the plurality of substantially solid particles, the silk fibroin nanoclay composite or film, the stabilized silk fibroin solution, the liquid in air suspension, or the plurality of drops or droplets described herein, the silk fibroin fragments may comprise a plurality of amino acids selected from M, R, V, K, T, F, I, L, C, A, Q, Y, N, D, E, G, S, H, P, and W, wherein at least one of the amino acids is modified, substituted, or replaced. In any of the above mentioned embodiments, the fibroin is a fibroin heavy chain, a fibroin light chain, or a fibrohexamerin. In any of the above mentioned embodiments, the silk fibroin fragment comprises between about 2 and about 100 amino acids. In any of the above mentioned embodiments, silk fibroin fragment comprises between one and five modifications, substitutions, and / or replacements. In any of the above mentioned embodiments, a modification, substitution, and / or replacement is selected from an asparagine to aspartic acid modification, substitution, and / or replacement, a glutamine to glutamic acid modification, substitution, and / or replacement, and a methionine to methionine oxide modification, substitution, and / or replacement. In any of the above mentioned embodiments, the fibroin is a fibroin heavy chain, and wherein a modification, DB1 / 158748174.5 6 substitution, and / or replacement is at a position corresponding to any one position from 1 to 5263 of the fibroin heavy chain. In any of the above mentioned embodiments, a modification, substitution, and / or replacement is at Q58, M64, N68, N70, N77, M80, N93, M103, Q125, N132, Q139, Q275, N4191, Q5216, and / or N5262. In any of the above mentioned embodiments, the fibroin is a fibroin light chain, and wherein a modification, substitution, and / or replacement is at a position corresponding to any one position from 1 to 262 of the fibroin light chain. In any of the above mentioned embodiments, a modification, substitution, and / or replacement is at N23, Q24, N28, M69, N105, N108, N118, N136, N138, Q149, N186, N200, Q202, N204, N240, N248, and / or Q255. In any of the above mentioned embodiments, the fibroin is a fibrohexamerin (p25), and wherein a modification, substitution, and / or replacement is at a position corresponding to any one position from 1 to 220 of the fibrohexamerin (p25). In any of the above mentioned embodiments, a modification, substitution, and / or replacement is at Q62, N93, M120, N149, N172, N174, and / or N202. In any of the above mentioned embodiments, each modification, substitution, and / or replacement is independently ranging between about 1% to about 99% in the silk fibroin fragments portion of the substantially solid particles, the silk fibroin nanoclay composite or film, or the stabilized silk fibroin solution composition. In any of the above mentioned embodiments, a % modification, substitution, and / or replacement is defined as (number of peptide or protein fragments comprising a modification, substitution, and / or replacement at a specific position, divided by the total number of peptide or protein fragments which include the specific position, whether comprising a modification, substitution, and / or replacement, or not) x 100. In any of the plurality of substantially solid particles, the silk fibroin nanoclay composite or film, the stabilized silk fibroin solution, the liquid in air suspension, or the plurality of drops or droplets described herein, the silk fibroin fragments are included in one or more fractions, each fraction independently comprising a plurality of fibroin heavy chain fragments, a plurality of fibroin light chain fragments, and / or a plurality of fibrohexamerin (p25) fragments. In any of the embodiments, the silk fibroin fragments have a weight average molecular weight (Mw) selected from between about 1 kDa and about 20 kDa, from between about 20 kDa and about 40 kDa, from between about 40 kDa and about 60 kDa, from between about 60 kDa and about 80 kDa, from between about 80 kDa and about 100 kDa, from between about 100 kDa and about 120 kDa, from between about 120 kDa and about 140 kDa, or DB1 / 158748174.5 7 from between about 140 kDa and about 160 kDa, from between about 160 kDa and about 180 kDa, from between about 180 kDa and about 200 kDa, or from between about 200 kDa and about 250 kDa, and a polydispersity between 1 and about 1.7. In any of the above mentioned embodiments, the silk fibroin fragments have a weight average molecular weight (Mw) selected from between about 10 kDa and about 20 kDa, from between about 20 kDa and about 40 kDa, from between about 40 kDa and about 60 kDa, from between about 60 kDa and about 80 kDa, from between about 80 kDa and about 100 kDa, from between about 100 kDa and about 120 kDa, from between about 120 kDa and about 140 kDa, from between about 140 kDa and about 160 kDa, or from between about 160 kDa and about 180 kDa, and a polydispersity between 1 and about 1.1, or 1 and about 1.2. In any of the above mentioned embodiments, the silk fibroin fragments in a fraction have a weight average molecular weight (Mw) selected from between about 10 kDa and about 20 kDa, from between about 20 kDa and about 40 kDa, from between about 40 kDa and about 60 kDa, from between about 60 kDa and about 80 kDa, from between about 80 kDa and about 100 kDa, from between about 100 kDa and about 120 kDa, or from between about 120 kDa and about 140 kDa, and a polydispersity between 1 and about 1.1, or 1 and about 1.2. In any of the above mentioned embodiments, the silk fibroin fragments in a fraction have a weight average molecular weight (Mw) selected from between about 60 kDa and about 80 kDa, from between about 80 kDa and about 100 kDa, or from between about 100 kDa and about 120 kDa, and a polydispersity between 1 and about 1.1. In any of the above mentioned embodiments, the silk fibroin fragments in a fraction have a weight average molecular weight (Mw) selected from between about 10 kDa and about 20 kDa, from between about 20 kDa and about 40 kDa, from between about 40 kDa and about 60 kDa, from between about 60 kDa and about 80 kDa, from between about 80 kDa and about 100 kDa, or from between about 100 kDa and about 110 kDa, and a polydispersity between 1 and about 1.1, or 1 and about 1.2. In any of the above mentioned embodiments, the silk fibroin fragments in a fraction have a weight average molecular weight (Mw) selected from between about 60 kDa and about 80 kDa, from between about 80 kDa and about 100 kDa, from between about 100 kDa and about 120 kDa, or from between about 120 kDa and about 140 kDa, and a polydispersity between 1 and about 1.1. In any of the above mentioned embodiments, the silk fibroin fragments in a fraction have a weight average molecular weight (Mw) selected from between about 20 kDa and about 40 kDa, or DB1 / 158748174.5 8 from between about 40 kDa and about 60 kDa, and a polydispersity between 1 and about 1.1, or 1 and about 1.2. In any of the above mentioned embodiments, the one or more fractions are selected from AS77, AS78, AS79, AS80, and AS81. In any of the above mentioned embodiments, the one or more fractions are selected from AS82, AS83, AS84, AS85, AS86, AS87, AS88, and AS89. In any of the above mentioned embodiments, the one or more fractions are selected from AS90, AS91, AS92, AS93, and AS94. In any of the above mentioned embodiments, the one or more fractions are selected from AS95, AS96, AS97, AS98, AS99, and AS100. In any of the above mentioned embodiments, the silk fibroin fragments have a weight average molecular weight (Mw) selected from between about 40 kDa and about 60 kDa, from between about 60 kDa and about 80 kDa, from between about 80 kDa and about 100 kDa, from between about 100 kDa and about 120 kDa, from between about 120 kDa and about 140 kDa, from between about 140 kDa and about 160 kDa, from between about 160 kDa and about 180 kDa, from between about 180 kDa and about 200 kDa, or from between about 200 kDa and about 220 kDa, and a polydispersity between 1 and about 1.7. In any of the above mentioned embodiments, the silk fibroin fragments in a fraction have a weight average molecular weight (Mw) selected from between about 40 kDa and about 60 kDa, from between about 60 kDa and about 80 kDa, from between about 80 kDa and about 100 kDa, from between about 100 kDa and about 120 kDa, from between about 120 kDa and about 140 kDa, from between about 140 kDa and about 160 kDa, from between about 160 kDa and about 180 kDa, from between about 180 kDa and about 200 kDa, or from between about 200 kDa and about 210 kDa, and a polydispersity between 1 and about 1.2, or 1 and about 1.3. In any of the above mentioned embodiments, the silk fibroin fragments in a fraction have a weight average molecular weight (Mw) selected from between about 40 kDa and about 60 kDa, from between about 60 kDa and about 80 kDa, from between about 80 kDa and about 100 kDa, or from between about 100 kDa and about 110 kDa, and a polydispersity between 1 and about 1.1, or 1 and about 1.2. In any of the above mentioned embodiments, the silk fibroin fragments in a fraction have a weight average molecular weight (Mw) selected from between about 60 kDa and about 80 kDa, from between about 80 kDa and about 100 kDa, from between about 100 kDa and about 120 kDa, from between about 120 kDa and about 140 kDa, from between about 140 kDa and about 160 kDa, from between about 160 kDa and about 180 kDa, from between about 180 kDa and about 200 kDa, or from between about 200 kDa and DB1 / 158748174.5 9 about 210 kDa, and a polydispersity between 1 and about 1.2, or 1 and about 1.3. In any of the above mentioned embodiments, the one or more fractions are selected from AS101, AS102, AS103, AS104, and AS105. In any of the above mentioned embodiments, the one or more fractions are selected from AS106, AS107, AS108, AS109, AS110, and AS111. In any of the above mentioned embodiments, the silk fibroin fragments comprise one or more amino acid modifications, substitutions, or replacements of an amino acid is selected from M, R, V, K, T, F, I, L, C, A, Q, Y, N, D, E, G, S, H, P, and W. In any of the above mentioned embodiments, wherein the silk fibroin fragments comprise between about 2 and about 100 amino acids. In any of the above mentioned embodiments, a silk fibroin fragment comprise between one and five modifications, substitutions, and / or replacements. In any of the above mentioned embodiments, the fibroin is a fibroin heavy chain, and wherein a modification, substitution, and / or replacement is at a position corresponding to any one position from 1 to 5263 of the fibroin heavy chain. In any of the above mentioned embodiments, the fibroin is a fibroin light chain, and wherein a modification, substitution, and / or replacement is at a position corresponding to any one position from 1 to 262 of the fibroin light chain. In any of the above mentioned embodiments, the fibroin is a fibrohexamerin (p25) chain, and wherein a modification, substitution, and / or replacement is at a position corresponding to any one position from 1 to 220 of the fibrohexamerin (p25) chain. In any of the above mentioned embodiments, a modification, substitution, and / or replacement is selected from an asparagine to aspartic acid modification, substitution, and / or replacement, a glutamine to glutamic acid modification, substitution, and / or replacement, and a methionine to methionine oxide modification, substitution, and / or replacement. In any of the above mentioned embodiments, a modification, substitution, and / or replacement is at fibroin heavy chain position selected from Q58, M64, N68, N70, N77, M80, N93, M103, Q125, N132, Q139, Q275, N4191, Q5216, and / or N5262. In any of the above mentioned embodiments, a modification, substitution, and / or replacement is at fibroin light chain position selected from N23, Q24, N28, M69, N105, N108, N118, N136, N138, Q149, N186, N200, Q202, N204, N240, N248, and / or Q255. In any of the above mentioned embodiments, a modification, substitution, and / or replacement is at fibrohexamerin (p25) position selected from Q62, N93, M120, N149, N172, N174, and / or N202. In any of the above mentioned embodiments, each modification, substitution, and / or replacement is independently ranging in the composition between about 1% to about DB1 / 158748174.5 10 99%. In any of the above mentioned embodiments, the % modification, substitution, and / or replacement is defined as (number of peptide or protein fragments comprising a modification, substitution, and / or replacement at a specific position, divided by the total number of peptide or protein fragments which include the specific position, whether comprising a modification, substitution, and / or replacement, or not) x 100. In any of the above mentioned embodiments, molecular weight is determined by MALS. Embodiments of the present disclosure provide a pouch or a laundry pod comprising the plurality of substantially solid particles of any of the above mentioned embodiments. In some embodiments, the plurality of substantially solid particles are compressed in a multi-particulate puck. In some embodiments, the laundry pod further comprises a dissolvable enclosure comprising polyvinylalcohol (PVA) or a derivative of PVA. In some embodiments, the laundry pod further comprises an enclosure comprising one or more of nylon, polyglycolide (PGA), polylactic acid (PLA), poly(lactide-co-glycolide) (PLGA), polycaprolactone (PCL), poly(butylene succinate) (PBS), polybutylene succinate adipate, poly(p-dioxanone) (PPDO), poly(butylene adipate-co-terephthalate) (PBAT), a copolyester of terephthalic acid and lactic acid, a copolyester of terephthalic acid and glycolic acid, a copolyester of terephthalic acid and succinic acid, poly(hydroxybutyrate), poly(hydroxyvalerate), polyhydroxyhexanoate, a poly(hydroxyalkanoate) (PHA), polymethylene adipate / terephthalate. Embodiments of the present disclosure provide a method of making the plurality of substantially solid particles of any of the above mentioned embodiments, the method comprising dripping a solution comprising a plurality of the silk fibroin fragments into liquid nitrogen. In some embodiments, the method further comprises a lyophilization step. In some embodiments, the concentration of silk fibroin fragments in the solution is from about 3% (w / w) to about 50% (w / w). In some embodiments, the concentration of silk fibroin fragments in the solution is from about 6% (w / w) to about 25% (w / w). In some embodiments, the concentration of silk fibroin fragments in the solution is from about 6% (w / w) to about 20% (w / w). In some embodiments, the concentration of silk fibroin fragments in the solution is about 3% (w / w), about 4% (w / w), about 5% (w / w), about 6% (w / w), about 7% (w / w), about 8% (w / w), about 9% (w / w), about 10% (w / w), about 11% (w / w), about 12% (w / w), about 13% (w / w), about 14% (w / w), about 15% (w / w), about 16% (w / w), about 17% (w / w), about 18% DB1 / 158748174.5 11 (w / w), about 19% (w / w), about 20% (w / w), about 21% (w / w), about 22% (w / w), about 23% (w / w), about 24% (w / w), or about 25% (w / w). In some embodiments, the silk fibroin fragments comprise one or more of a molecular weight, polydispersity, and / or a modification, substitution, and / or replacement at a specific amino acid position, as defined in any one of the above mentioned embodiments. In some embodiments, the solution is stabilized as defined in any one the above mentioned embodiments. In any of the above mentioned embodiments, the particles have a reconstitution yield of more than 90%. In any of the above mentioned embodiments, the particles have a reconstitution yield in DI water of more than 90%. In some embodiments, a reconstitution rate of at least 90% is preserved after a stability testing comprising simulated ageing of a plurality of substantially solid particles described herein, the ageing comprising storage a temperature between about 40 °C and about 60 °C, for a period of time ranging from about 400 days to about 650 days. In some embodiments, the simulated age ranges from about 4 years to about 15 years. BRIEF DESCRIPTION OF THE DRAWINGS The presently disclosed embodiments will be further explained with reference to the attached drawings. The drawings shown are not necessarily to scale, with emphasis instead generally being placed upon illustrating the principles of the presently disclosed embodiments. Figure 1. Ion Exchange Fractionation Schemes for the isolation of the populations that constitute Low and Mid Skid silk / modified polypeptide compositions. Low and Mid Skid silk / modified polypeptide compositions contains silk / modified polypeptides that are negatively, positively charged, or neutral. Using Q anion exchange chromatography (A) these populations were isolated. Figure 2. Chromatogram of Low Skid silk / modified polypeptide composition loaded in a Q-Sepharose HP column (Cytiva). The flow through contains the silk / modified polypeptides that do not get captured in the column and are the depleted in negatively charged amino acids. After the column is loaded with Low or Mid Skid silk / modified polypeptide compositions and the flow through is collected, the column is washed until the UV-280 absorbance becomes less than 200 AU. The captured negatively charged silk / modified polypeptides are eluted with high salt concentration DB1 / 158748174.5 12 (1M NaCl) and constitute AS11 and AS22. The chromatography is performed in Tris- containing buffers but the flow through and the Q-elution were finally dialyzed in water. Figure 3. Analytical Size Exclusion Chromatography of Low, Mid Skid silk / modified silk compositions and their constituent AS compositions. Average molecular weight in kDa and polydispersity measurements are shown. Figures 4A- 4B. Analytical Size Exclusion Chromatography of the Low and Mid skid silk / modified peptide compositions and their components (see table 1 for more details). Fig.4A, Molecular weight of the various Activated Silk new compositions described in this study. Fig.4B, Polydispersity (PDI) of the various Activated Silk new compositions described in this study. AS24 reconstitutes the average molecular weight and polydispersity of the Low skid silk / modified peptide composition and it consists of 50% AS12 and 50% AS22 (see table 1 for details). AS6 reconstitutes the average molecular weight and polydispersity of the Mid skid silk / modified peptide composition and it consists of 50% AS1 and 50% AS11 (see table 1 for details). Figure 5. Isoelectric Focusing Electrophoresis of Low Skid silk / modified polypeptide compositions. Lanes 2, 7; Low Skid silk different amounts loaded. Lanes 3, 5, 8, 10; AS12 silk, different preparations different amounts loaded. Lanes 4, 6, 9, 11; AS22 silk, different preparations different amounts loaded. Figures 6A- 6B. Self-assembly reactions of the of the Low and Mid skid silk / modified peptide compositions and their components (see table 1 for more details). Both graphs depict the kinetic parameters of gel formation during self- assembly of silk. On graph A calculation of the three self-assembly kinetic parameters is shown, t0.5, Amax and SARF. For more details look at the text. Figures 7A- 7C. Self-assembly kinetics of the Low and Mid skid silk / modified peptide compositions and their components (see table 1 for more details). Fig.7A, the Self-assembly Rate Factor shows how fast the self-assembly reaction proceeds once it is initiated and the self-assembly nuclei are organized. Fig. 7B, Maximum Gel Yield shows how dense the silk gel is after self-assembly is complete. Fig.7C, Time required for the self-assembly reaction to produce half of the maximum gel amount. DB1 / 158748174.5 13 Figure 8. the Low and Mid skid silk / modified peptide compositions and their components (see table 1 for more details). The Self Assembly Factor reflects the average propensity of silk to self-assemble and form gels. While the above-identified drawings set forth presently disclosed embodiments, other embodiments are also contemplated, as noted in the discussion. This disclosure presents illustrative embodiments by way of representation and not limitation. Numerous other modifications and embodiments can be devised by those skilled in the art which fall within the scope and spirit of the principles of the presently disclosed embodiments. Figure 9 is a graph of Weight average molecular weight (i.e., average molecular weight average or average MW) using Size exclusion chromatography with a refractive index detector (SEC-RI) plotted as a function of time for solubilized fibroin in 9.3 M LiBr at 100 °C - 103 °C (i.e., 3 degree Celsius temperature gradient between 100 °C and 103 °C). Figure 10 is a graph of weight average molecular weight (i.e., average molecular weight average or average MW) using Size exclusion chromatography with a refractive index detector (SEC-RI) plotted as a function of time for solubilized fibroin in 9.3 M LiBr at 122 °C - 125 °C (i.e., 3 degree Celsius temperature gradient between 122 °C and 125 °C). Figure 11 is a graph illustrating percentage of amino acid modification in silk. Figures 12A-12C are graphs illustrating percentage of amino acid modifications in Low Skid Silk and Mid Skid silk. Fig.12A illustrates heavy chain modifications, Fig.12B illustrates light chain modifications, and Fig.12C illustrates fibrohexamerin modifications. N are Asparagines that become aspartic acid and Q are Glutamines that become deamidated. M corresponds to Methionies that become oxidized. The numbers after each amino acid show its position along the amino acid chain from the corresponding protein. Figures 13A- 13B are graphs illustrating percentage of amino acid modifications in Low Skid Silk and Mid Skid silk produced and lyophilized. Fig.13A illustrates heavy chain modifications and Fig.13B illustrates light chain modifications. N are Asparagines that become aspartic acid and Q are Glutamines that become deamidated. M corresponds to Methionies that become oxidized. The DB1 / 158748174.5 14 numbers after each amino acid show its position along the amino acid chain from the corresponding protein. Figures 14A- 14B are graphs illustrating percentage of amino acid modifications in Low Skid silk produced in Walpole and Medford using the Skid process with differing process parameters and variable levels. Fig.14A illustrates heavy chain modifications and Fig.14B illustrates light chain modifications. N are Asparagines that become aspartic acid and Q are Glutamines that become deamidated. M corresponds to Methionies that become oxidized. The numbers after each amino acid show its position along the amino acid chain from the corresponding protein. Figures 15A- 15D are graphs illustrating percentage of amino acid modifications in Low and Mid silk produced in Skid and Benchtop processes. N are Asparagines that become aspartic acid and Q are Glutamines that become deamidated. M corresponds to Methionies that become oxidized. The numbers after each amino acid show its position along the amino acid chain from the corresponding protein. Figure 16 is an explanation of the method used to calculate percentage ratios of modified amino acids at specific locations along the sequence of each peptide. Figure 17 illustrates an Anion exchange chromatography and size exclusion chromatography scheme of the isolation of Low Skid silk / modified peptide compositions. Low Skid silk / modified polypeptide compositions is composed of a variety of peptide populations, in a wide range of sizes and charge. Using Q- Sepharose anion exchange chromatography as a first step, and HiLoad Superdex 200 size exclusion chromatography as a second purification step, distinct populations of Low Skid silk / modified polypeptide compositions were separated. The Q-Sepharose eluate was loaded onto HiLoad Superdex 200 size exclusion chromatography, which resulted in negatively charged silk compositions / modified peptides fractionated by size. Figures 18A and 18B are chromatograms of the anion exchange chromatography and the following size exclusion chromatography of the eluate (Q- eluate) of Low Skid silk / modified polypeptide compositions. Fig.18A: Anion exchange chromatography was performed with a Q-Sepharose column (Cytiva). Low Skid silk / modified peptide compositions were separated to uncharged peptide population (flowthrough – light blue background) and eluted negatively charged silk compositions (eluate – light pink background) by anion exchange chromatography. DB1 / 158748174.5 15 Light yellow background indicates column wash with 50 mM Tris pH=8.0 before eluting the charged peptide population. Fig.18B: The negatively charged eluate was loaded onto the Superdex 200 column and was flowed through the column with 50 mM Tris, 200 mM CaCl2, pH=8.0. When the UV-280 absorbance started to increase fractions were collected to separate the Low Skid silk / modified peptide compositions by size. The relative elution volume of silk compositions AS77 and AS81 are indicated on the chromatogram. Figures 19A and 19B illustrates the Analytical Size Exclusion Chromatography of Low Skid silk / modified silk compositions and their constituent AS compositions. Fig.19A. Average molecular weight in kDa of Low Skid silk (LS) and AS77-AS81 are shown. Fig.19B. Polydispersity (PDI) measurements are shown. The numerical data is presented in Table 7. Figure 20 is a SDS polyacrylamide gel electrophoresis of Low Skid silk / modified polypeptide compositions. Lanes are indicated by fraction number, at the order of elution from the Superdex 200 column, and their respective silk composition: fraction 6 is AS77, fraction 7 is AS78, fraction 8 is AS79, fraction 9 is AS80, and fraction 10 is AS81. Figures 21A and 21B are graphs illustrating self-assembly reactions of the of the Low Skid silk / modified peptide compositions. Mid Skid Silk reaction was used as a positive control. Fig.21A. Illustrate kinetic parameters of gel formation during self- assembly of silk. Self-Assembly parameters of Mid Skid silk: Amax is 0.6780 (Abs), SARF is 8.676, T0.5 is 3.668 h, and the FSAF is 3.08 (Abs / min). Fig.21B. Is a snapshot of a later time point of the same self-assembly assay, 12 days after setting the assay. None of the tested fraction has self-assembled over time. Figures 22A and 22B illustrate the characterization of Low Skid silk compositions by Dynamic Light Scattering. Low skid silk / modified peptide compositions were diluted to a concentration of 1 mg / mL, filtered, and analyzed by the Zetasizer Pro to estimate the diameter particle size of each silk composition. Fig. 22A. Illustrates intensity diameter particle size distribution measured for silk compositions AS77, AS78, AS79, AS80, and AS81. Fig.22B. Illustrate correlogram functions of silk compositions AS77, AS78, AS79, AS80, AS81. DB1 / 158748174.5 16 Figure 23 illustrates size exclusion chromatography scheme of the isolation of Low Skid silk / modified peptide compositions. Low Skid silk / modified polypeptide compositions is composed of a variety of peptide populations, in a wide range of sizes, using HiLoad Superdex 200 size exclusion chromatography, distinct populations of Low Skid silk / modified polypeptide compositions were separated. Figure 24 is a chromatogram of Low Skid silk / modified polypeptide compositions loaded onto a Superdex 200 gel filtration column. Low Skid silk / modified peptide compositions were loaded onto the Superdex 200 column and were flowed through the column with 50 mM Tris, 200 mM CaCl2, pH=8.0. When the UV-280 absorbance started to increase fractions were collected to separate the Low Skid silk / modified peptide compositions by size. The relative elution volume of silk compositions AS82, AS86, and AS87 are indicated on the chromatogram. Figures 25A and 25B illustrate Analytical Size Exclusion Chromatography of Low Skid silk / modified silk compositions and their constituent AS compositions. Fig. 25A. Illustrates average molecular weight in kDa of Low Skid silk (LS) and AS82- AS89 are shown. Fig.25B. Polydispersity (PDI) measurements are shown. The numerical data is presented in Table 9. Figure 26 is an SDS polyacrylamide gel electrophoresis of Low Skid silk / modified polypeptide compositions. Lanes are indicated by fraction number, at the order of elution from the Superdex 200 column, and their respective silk composition: fraction 6 is AS82, fraction 7 is AS83, fraction 8 is AS84, fraction 9 is AS85, and fraction 10 is AS86. Figures 27A and 27B are graphs illustrating self-assembly reactions of the of the Low Skid silk / modified peptide compositions. Mid Skid Silk reaction was used as a positive control. Fig.27A. Illustrates kinetic parameters of gel formation during self-assembly of silk. Self-Assembly parameters of Mid Skid silk: Amax is 0.6978 (Abs), SARF is 8.591, T0.5 is 3.361 h, and the FSAF is 3.46 (Abs / min). Fig.27B. Is a snapshot of a later time point of the same self-assembly assay, 18 days after setting the assay. AS87, AS88, and AS89 demonstrate gel formation at this time point, that was already observed five days post assay (LS, Low Skid silk; MS, Mid Skid silk). Figures 28A- 28C are graphs showing characterization of Low Skid silk compositions by Dynamic Light Scattering. Low skid silk / modified peptide DB1 / 158748174.5 17 compositions were diluted to a concentration of 1 mg / mL, filtered, and analyzed by the Zetasizer Pro to estimate particle size of each silk composition. Fig.28A. Shows intensity particle size distribution measured for silk compositions AS82, AS83, AS84, AS85, AS86, AS87, AS88, and AS89. Fig.28B. Shows intensity particle size distribution measured for silk compositions AS82, Low Skid silk / modified peptide compositions (LS), and Mid Skid silk / modified peptide compositions (MS). Fig.28C. Shows correlogram functions of silk compositions AS82, AS83, AS84, AS85, AS86, AS87, AS88, AS89, Low Skid silk / modified peptide compositions (LS), Mid Skid silk / modified peptide compositions (MS). Figure 29 illustrates anion exchange chromatography (Q), hydrophobic interaction chromatography (HIC), and size exclusion chromatography (SEC) scheme of the isolation of Low Skid silk / modified peptide compositions. Low Skid silk / modified polypeptide compositions is composed of a variety of peptide populations, in a wide range of sizes and charge. Using Q-Sepharose anion exchange chromatography as a first step, Butyl ImpRes Hydrophobic interactions resin as a second step, and HiLoad Superdex 200 size exclusion chromatography as a third purification step, distinct populations of Low Skid silk / modified polypeptide compositions were isolated. The Q-Sepharose eluate was loaded onto a Butyl ImpRes (HIC) column, and the HIC-eluate was loaded onto a HiLoad Superdex 200 size exclusion chromatography, which resulted in fractionation of negatively charged silk compositions / modified peptides with hydrophobicity characteristics fractionated by size. The Q-Sepharose eluate contained negatively charged peptides in all sizes. Resolving these peptides by Butyl ImpRes column resulted in elution of high- molecular-weight, negatively charged, somewhat hydrophobic silk compositions / modified peptides. The smaller negatively charged peptides were washed as flowthrough and did not bind the Butyl ImpRes column. The Q- HIC(elution) was loaded into Superdex 200 and was separated by size. Figures 30A- 30E are chromatograms of anion exchange chromatography, hydrophobic interactions chromatography, and the following size exclusion chromatography of Low Skid silk / modified polypeptide compositions. Fig.30A. illustrates anion exchange chromatography was performed with a Q-Sepharose column. Low Skid silk / modified peptide compositions were separated to uncharged peptide population (flowthrough – light blue background) and eluted negatively DB1 / 158748174.5 18 charged silk compositions (eluate – light pink background) by anion exchange chromatography. Light yellow background indicates column wash with 50 mM Tris pH=8.0 before eluting the charged peptide population. Fig.30B. illustrates the negatively charged eluate (Q-elution) was loaded onto a Butyl ImpRes column, in the presence of 300 mM ammonium sulfate [(NH4)2SO4], to expose hydrophobic domains of the silk peptides, which allows binding to the column. The highly charged peptide population did not bind the column (flowthrough), highlighted in light blue. The column was washed until OD280 was reduced to ~100 units (light yellow). Then, the bound silk peptides (Q-HIC(elution)) were eluted by using 50 mM Tris, pH=8.0 without ammonium sulfate (light pink). Fig.30C. illustrates the Q-HIC(elution) was further fractionated by size exclusion chromatography (SEC), using the gel filtration column Superdex 200. The Q-HIC(elution) fraction was flowed through the column with 50 mM Tris, 200 mM CaCl2, pH=8.0. When the UV-280 absorbance started to increase fractions were collected to separate the Low Skid silk / modified peptide compositions by size. The relative elution volume of silk compositions AS90 and AS94 are indicated on the chromatogram. Fig.30D. the Q-HIC(flowthrough) fraction was further fractionated by SEC, using the Superdex 200 column, at the same procedure as in (VC). The relative elution volume of silk compositions AS95 and AS100 are indicated on the chromatogram. Fig.30E. illustrates the superimposition of chromatograms (VC) and (VD). the Q-HIC(elution) fraction has a higher-molecular- weight range compared to the Q-HIC(flowthrough) fractions, which elutes later in SEC, and has lower-molecular-weight range. Figures 31A- 31B are graphs showing analytical Size Exclusion Chromatography of Low Skid silk / modified silk compositions and their constituent AS compositions. Fig.31A. Average molecular weight in kDa of Low Skid silk (LS) and AS90-AS100 are shown. Fig.31B. Polydispersity (PDI) measurements are shown. The numerical data is presented in Table 11. Figures 32A- 32B are SDS polyacrylamide gel electrophoresis of Low Skid silk / modified polypeptide compositions. Fig.32A. Q-HIC(elution) SEC fractions. Fig.32B. Q-HIC(flowthrough) SEC fractions. Lanes are indicated by fraction number, at the order of elution from the Superdex 200 column, and their respective silk composition: in Fig.32A, fraction 6 is AS90, fraction 7 is AS91, fraction 8 is AS92, fraction 9 is AS93, and fraction 10 is AS94. In Fig.32B, fraction 8 is AS95, DB1 / 158748174.5 19 fraction 9 is AS96, fraction 10 is AS97, fraction 11 is AS98, fraction 12 is AS99, and fraction 13 is AS100. Figure 33 illustrates self-assembly reactions of the of the Low Skid silk / modified peptide compositions. Mid Skid Silk reaction was used as a positive control. kinetic parameters of gel formation during self-assembly of silk. Q- HIC(elution) is the elution fraction that was eluted from the Butyl ImpRes column, prior to SEC purification; LS, Low Skid silk; MS, Mid Skid silk. Self-Assembly parameters of Mid Skid silk: Amax is 0.6974 (Abs), SARF is 8.661, T0.5 is 3.834 h, and the FSAF is 3.03 (Abs / min). Figures 34A- 34F illustrate the characterization of Low Skid silk compositions by Dynamic Light Scattering. Low and Mid skid silk / modified peptide compositions were diluted to a concentration of 1 mg / mL, filtered, and analyzed by the Zetasizer Pro to estimate the diameter particle size of each silk composition. Fig. 34A. Intensity diameter particle size distribution measured for silk compositions AS90, Q-HIC(elution) fraction (prior to fractionation by SEC), Low Skid silk (LS), and Mid Skid silk (MS). Fig.34B. Correlogram functions of silk compositions presented in (34A). Fig.34C. Intensity diameter particle size distribution measured for silk compositions AS90-AS94, derived from Q-HIC(elution)-SEC fractionation process. Fig.34D. Correlogram functions of silk compositions presented in (34C). Fig.34E. Intensity diameter particle size distribution measured for silk compositions AS95-AS100, derived from Q-HIC(flowthrough)-SEC fractionation process. Fig. 34F. Correlogram functions of silk compositions presented in (34E). Figure 35. illustrates size exclusion chromatography scheme of the isolation of Mid Skid silk / modified peptide compositions. Mid Skid silk / modified polypeptide compositions is composed of a variety of peptide populations, in a wide range of sizes, using HiLoad Superdex 200 size exclusion chromatography, distinct populations of Mid Skid silk / modified polypeptide compositions were able to be separated. Figure 36. Is a chromatogram of Mid Skid silk / modified polypeptide compositions loaded onto a Superdex 200 gel filtration column. Mid Skid silk / modified peptide compositions were loaded onto the Superdex 200 column and were flowed through the column with 50 mM Tris, 200 mM CaCl2, pH=8.0. When DB1 / 158748174.5 20 the UV-280 absorbance started to increase fractions were collected to separate the Mid Skid silk / modified peptide compositions by size. The relative elution volume of silk compositions AS107 and AS111 are indicated on the chromatogram. Figures 37A- 37B. Illustrates analytical Size Exclusion Chromatography of Mid Skid silk / modified silk compositions and their constituent AS compositions. Fig. 37A. Average molecular weight in kDa of Mid Skid silk (MS) and AS106-AS111 are shown. Fig.37B. Polydispersity (PDI) measurements are shown. The numerical data is presented in Table 14. Figure 38. Is a SDS polyacrylamide gel electrophoresis of Mid Skid silk / modified polypeptide compositions. Lanes are indicated by fraction number, at the order of elution from the Superdex 200 column, and their respective silk composition: fraction 6 is AS107, fraction 7 is AS108, fraction 8 is AS109, fraction 9 is AS110, and fraction 10 is AS111. Figure 39. Illustrates self-assembly reactions of the of the Mid Skid silk / modified peptide compositions. Kinetic parameters of gel formation during self- assembly of silk. Dashed red lines show how the self-assembly parameters Amax, SARF, and T0.5 were calculated for unfractionated Mid Skid silk (MS). These numerical calculated parameters of silk compositions AS106-AS111 can be found in Table 16. Low Skid silk (LS) was used as a negative control. LS, Low Skid silk; MS, Mid Skid silk. Figures 40A-40B. Illustrates characterization of Mid Skid silk compositions by Dynamic Light Scattering. Mid skid silk / modified peptide compositions were diluted to a concentration of 1 mg / mL, filtered, and analyzed by the Zetasizer Pro to estimate particle size of each silk composition. Fig.40A. Intensity particle size distribution measured for silk compositions AS106, AS107, AS108, AS109, AS110, AS111, and Mid Skid (MS). Fig.50B. Correlation functions of silk compositions presented in (40A). Figure 41. Illustrates anion exchange chromatography and size exclusion chromatography scheme of the isolation of Mid Skid silk / modified peptide compositions. Mid Skid silk / modified polypeptide compositions is composed of a variety of peptide populations, in a wide range of sizes and charge. Using Q- Sepharose anion exchange chromatography as a first step, and HiLoad Superdex 200 DB1 / 158748174.5 21 size exclusion chromatography as a second purification step, distinct populations of Mid Skid silk / modified polypeptide compositions were separated. The Q-Sepharose eluate was loaded onto HiLoad Superdex 200 size exclusion chromatography, which resulted in negatively charged silk compositions / modified peptides fractionated by size. Figures 42A-42B. Are chromatograms of the anion exchange chromatography and the following size exclusion chromatography of the eluate (Q-eluate) of Mid Skid silk / modified polypeptide compositions. Fig.42A. Anion exchange chromatography was performed with a Q-Sepharose column (Cytiva). Mid Skid silk / modified peptide compositions were separated to uncharged peptide population (flowthrough – light blue background) and eluted negatively charged silk compositions (eluate – light pink background) by anion exchange chromatography. Light yellow background indicates column wash with 50 mM Tris pH=8.0 before eluting the charged peptide population. Fig.42B. The negatively charged eluate (Q-elution) was loaded onto the Superdex 200 column and was flowed through the column with 50 mM Tris, 200 mM CaCl2, pH=8.0. When the UV-280 absorbance started to increase fractions were collected to separate the Mid Skid silk / modified peptide compositions by size. The relative elution volume of silk compositions AS101 and AS105 are indicated on the chromatogram. Figures 43A-43B. Illustrate analytical Size Exclusion Chromatography of Mid Skid silk / modified silk compositions and their constituent AS compositions. Fig. 43A. Average molecular weight in kDa of Mid Skid silk (MS) and AS101-AS105 are shown. Fig.43B. Polydispersity (PDI) measurements are shown. The numerical data is presented in Table 16. Figure 44A. Is a SDS polyacrylamide gel electrophoresis of Mid Skid silk / modified polypeptide compositions. Lanes are indicated by fraction number, at the order of elution from the Superdex 200 column, and their respective silk composition: fraction 6 is AS101, fraction 7 is AS102, fraction 8 is AS103, fraction 9 is AS104, and fraction 10 is AS105. Figure 44B illustrates self-assembly reactions of the of the Mid Skid silk / modified peptide compositions. Low Skid Silk reaction was used as a negative control. Kinetic parameters of gel formation during self-assembly of silk are shown. Red dotted lines are shown to clarify the calculations of Amax, SARF (Self-Assembly Rate Factor), and T0.5 parameters in Table 17. DB1 / 158748174.5 22 Figures 45A, 45B, and 45C. Are graphs illustrating characterization of Mid Skid silk compositions by Dynamic Light Scattering. Mid skid silk / modified peptide compositions were diluted to a concentration of 1 mg / mL, filtered, and analyzed by the Zetasizer Pro (Malvern) to estimate the diameter particle size of each silk composition. Fig.45A. Intensity diameter particle size distribution by intensity measured for silk compositions AS101, AS102, AS103, AS104, and AS105. Fig. 45B. Intensity diameter particle size distribution by intensity measured for silk compositions AS101, AS105, and Mid Skid silk (MS), to emphasize the size difference between AS101 and AS105. Fig.45C. Correlogram functions of silk compositions AS101, AS102, AS103, AS104, AS105, and Mid Skid silk (MS). Figure 46. is an illustration of the values for three molar mass moments (Mn, Mw, and Mz) as it relates to molar mass and the number of molecules at each molar mass. This example is applicable to a polydisperse sample; for a monodisperse sample, Mn = Mw = Mz. Figures 47A- 47B are analytical SEC-MALS of Low, Mid and High Molecular Weight Silk. Fig.47A. Weight Average Molecular Weight in kDa of Low, Mid, and High Molecular Weight Silk. Fig.47B. Polydispersity Index (PDI) measurements of Low, Mid, and High Molecular Weight Silk are shown. Figures 48A- 48B. Are analytical SEC-MALS of Low, Mid and High Molecular Weight Silk organized by Silk Type produced by different process parameters and variable levels. Individual data points are shown and the mean is represented by the heigh of the box. The bars encompass one standard deviation. Fig. 48A. Weight-Average Molecular Weight Ranges for Low, Mid, and High Molecular Weight Silk. Fig.48B. PDI Ranges for Low, Mid, and High Molecular Weight Silk. Figures 49A- 49B are nalytical SEC-MALS of Low Skid silk / modified silk compositions and the constituent AS compositions as separated by Q-SEC (Q-eluent). Fig.49A. Average molecular weight in kDa of Low Skid silk (LS) and AS77-AS81 are shown. Fig.49B. Polydispersity (PDI) measurements are shown. The numerical data is presented in Table 24. Figures 50A- 50B are analytical SEC-MALS of Low Skid silk / modified silk compositions and the constituent AS compositions as separated by SEC. Fig.50A. Average molecular weight in kDa of Low Skid silk (LS) and AS82-AS89 are shown. Fig.50B. Polydispersity (PDI) measurements are shown. The numerical data is presented in Table 25. DB1 / 158748174.5 23 Figures 51A- 51B are analytical SEC-MALS of Low Skid silk / modified silk compositions and the constituent AS compositions as separated by Q-HIC-SEC (Q- HIC-Eluent). Fig.51A. Average molecular weight in kDa of Low Skid silk (LS) and AS90-AS94 are shown. Fig.51B. Polydispersity (PDI) measurements are shown. The numerical data is presented in Table 26. Figures 52A- 52B are analytical SEC-MALS of Low Skid silk / modified silk compositions and the constituent AS compositions as separated by Q-HIC-SEC (Q- HIC-Flowthrough). Fig.52A. Average molecular weight in kDa of Low Skid silk (LS) and AS95-AS100 are shown. Fig.52B. Polydispersity (PDI) measurements are shown. The numerical data is presented in Table 26. Figures 53A- 53B are analytical SEC-MALS of Mid Skid silk / modified silk compositions and the constituent AS compositions as separated by Q--SEC (Q-flow through). Fig.53A. Average molecular weight in kDa of Mid Skid silk (MS) and AS101-AS105 are shown. Fig.53B. Polydispersity (PDI) measurements are shown. The numerical data is presented in Table 27. Figures 54A- 54B are analytical SEC-MALS of Mid Skid silk / modified silk compositions and the constituent AS compositions as separated by SEC. Fig.54A. Average molecular weight in kDa of Mid Skid silk (MS) and AS106-AS111 are shown. Fig.54B. Polydispersity (PDI) measurements are shown. The numerical data is presented in Table 28. Figures 55A, 55B, and 55C show the sequence listing for fibroin heavy chain. Figure 56 shows the sequence listing for fibroin light chain. Figure 57 shows the sequence listing for fibrohexamerin. Figure 58 illustrates three chromatography principles of silk fractionalization. Figure 59 illustrates the anion exchange chromatography followed by size exclusion chromatography of silk fractionalization. Figure 60 illustrates the anion exchange chromatography followed by hydrophobic interactions chromatography and size exclusion chromatography. Figure 61 is a chart including assays for characterizing silk fractions. Figure 62 shows graphs presenting the data of Tables 44 and 45. Data shown with standard deviation. “Nanoclay” refers to Elementis Bentone Hydroclay. Figure 63 is as diagram of the typical bentonite clay structure. DB1 / 158748174.5 24 Figure 64 shows SEM images of cross-sectional area of film cast with Elementis Bentone Hydroclay 2001. Highly-ordered stacking of clay layers is visible. Figure 65 is an SEM image of cross-sectional area of film cast with pure RSF. Figure 66 is an SEM image of cross-sectional area of 1:1 RSF / 2001 film cast under neutral (pH ~7.0) conditions. The layered structure of the clay is retained. Figure 67 is an SEM image of cross-sectional area of 1:1 RSF / 2001 film cast under acidic (pH ~3.5) conditions. Note the ribbon-like structure. Figure 68 illustrates the increased diffusive pathway created by the RSF / nanoclay composite. Figure 69 is an FTIR scan of the amide I region of RSF / 2001 films cast under neutral conditions. The concentration of nanoclay is varied from 0% (red) to 70% (yellow). As nanoclay content increases, the amide I peak shifts left, away from the beta sheet region. Figure 70 is a flow chart showing various embodiments for producing pure silk fibroin-based protein fragments (SPFs) of the present disclosure. Figure 71 is a flow chart showing various parameters that can be modified during the process of producing SPFs of the present disclosure during the extraction and the dissolution steps. Figures 72 and 73 are graphs representing the effect of extraction volume on % mass loss. Figure 74 is a graph summarizing the effect of Extraction Time on Molecular Weight of silk processed under the conditions of 100 °C Extraction Temperature, 100 °C LiBr and 100 °C Oven Dissolution (Oven / Dissolution Time was varied). Figure 75 is a graph summarizing the effect of Extraction Time on Molecular Weight of silk processed under the conditions of 100 °C Extraction Temperature, boiling LiBr and 60 °C Oven Dissolution (Oven / Dissolution Time was varied). Figure 76 is a graph summarizing the effect of Extraction Time on Molecular Weight of silk processed under the conditions of 100 °C Extraction Temperature, 60 °C LiBr and 60 °C Oven Dissolution (Oven / Dissolution Time was varied). Figure 77 is a graph summarizing the effect of Extraction Time on Molecular Weight of silk processed under the conditions of 100 °C Extraction Temperature, 80 °C LiBr and 80 °C Oven Dissolution (Oven / Dissolution Time was varied). DB1 / 158748174.5 25 Figure 78 is a graph summarizing the effect of Extraction Time on Molecular Weight of silk processed under the conditions of 100 °C Extraction Temperature, 80 °C LiBr and 60 °C Oven Dissolution (Oven / Dissolution Time was varied). Figure 79 is a graph summarizing the effect of Extraction Time on Molecular Weight of silk processed under the conditions of 100 °C Extraction Temperature, 100 °C LiBr and 60 °C Oven Dissolution (Oven / Dissolution Time was varied). Figure 80 is a graph summarizing the effect of Extraction Time on Molecular Weight of silk processed under the conditions of 100 °C Extraction Temperature, 140 °C LiBr and 140 °C Oven Dissolution (Oven / Dissolution Time was varied). Figure 81 is a graph summarizing the effect of Extraction Temperature on Molecular Weight of silk processed under the conditions of 60 minute Extraction Time, 100 °C LiBr and 100 °C Oven Dissolution (Oven / Dissolution Time was varied). Figure 82 is a graph summarizing the effect of LiBr Temperature on Molecular Weight of silk processed under the conditions of 60 minute Extraction Time, 100 °C Extraction Temperature and 60 °C Oven Dissolution (Oven / Dissolution Time was varied). Figure 83 is a graph summarizing the effect of LiBr Temperature on Molecular Weight of silk processed under the conditions of 30 minute Extraction Time, 100 °C Extraction Temperature and 60 °C Oven Dissolution (Oven / Dissolution Time was varied). Figure 84 is a graph summarizing the effect of Oven / Dissolution Temperature on Molecular Weight of silk processed under the conditions of 100 °C Extraction Temperature, 30 minute Extraction Time, and 100 °C Lithium Bromide (Oven / Dissolution Time was varied). Figure 85 is a graph summarizing the effect of Oven / Dissolution Temperature on Molecular Weight of silk processed under the conditions of 100 °C Extraction Temperature, 60 minute Extraction Time, and 100 °C Lithium Bromide. (Oven / Dissolution Time was varied). Figure 86 is a graph summarizing the effect of Oven / Dissolution Temperature on Molecular Weight of silk processed under the conditions of 100 °C Extraction Temperature, 60 minute Extraction Time, and 140 °C Lithium Bromide (Oven / Dissolution Time was varied). DB1 / 158748174.5 26 Figure 87 is a graph summarizing the effect of Oven / Dissolution Temperature on Molecular Weight of silk processed under the conditions of 100 °C Extraction Temperature, 30 minute Extraction Time, and 140 °C Lithium Bromide (Oven / Dissolution Time was varied). Figure 88 is a graph summarizing the effect of Oven / Dissolution Temperature on Molecular Weight of silk processed under the conditions of 100 °C Extraction Temperature, 60 minute Extraction Time, and 80 °C Lithium Bromide (Oven / Dissolution Time was varied). Figure 89 is a graph summarizing the Molecular Weights of silk processed under varying conditions including Extraction Time, Extraction Temperature, Lithium Bromide (LiBr) Temperature, Oven Temperature for Dissolution, Oven Time for Dissolution. Figure 90 is a graph summarizing the Molecular Weights of silk processed under conditions in which Oven / Dissolution Temperature is equal to LiBr Temperature. Figures 91A-91C illustrate Low-MW silk solid resulted from lyophilization described herein at different stages of grinding. Fig.91A illustrates the coarse particles of the Low-MW silk solid immediate after removal from the lyophilization bottle. Fig.91B illustrates the reduced size particle midway through grinding. Fig. 91C illustrates the fine particles with even size distribution at the completion grinding. Figure 92 illustrates solid particles of Mid-MW silk solid. Figure 93 illustrates example of two different particle size solid silk particles formed during thin film evaporation described herein. Figures 94A and 94B illustrate examples of microparticles prepared by a solution precipitation process described herein. Figure 95 illustrates milled silk powder for uses described herein. Figures 96A-96B illustrate a pouch containing the solid formulation comprising silk fibroin fragments described herein. Fig.96A illustrates a pouch described herein containing loose silk fibroin fragments. Fig.96B illustrates a pouch described herein containing a disc of cryo-pelletized silk fibroin fragments. Figures 97A illustrates lyophilized silk pellets. Fig.97B is a graph illustrating activated silk reconstitution yield. DB1 / 158748174.5 27 Figure 98A shows lyophilized silk. Fig.98B is a graph showing lyophilization temperatures. Figure 99A shows cryo-pelletized silk. Fig.99B is a graph showing lyophilization temperatures. Figure 100 illustrates lyophilized beads at various concentrations. Figures 101A- 101G are SEM images of Lyophilized Silk with Different Processing Conditions. Fig.101A shows silk lyophilized at 6% with no annealing. Fig.101B shows silk lyophilized at 6% with annealing. Fig.101C shows silk lyophilized at 6% with no annealing. Fig.101D shows silk lyophilized at 6% with annealing. Fig.101E shows 16% silk with no annealing. Fig.101F shows 16% silk with annealing at 4 hours. Fig.101G shows 16% silk with annealing at 20 hours. Figures 102A- 102B are images of powder lyophilized silk from densified lyophilized pellets. Fig.102A shows 10% Mid Mw Activated Silk™ grounded from densified pellets. Fig.102B shows 16% Low Mw Activated Silk™ grounded from densified pellets. Figure 103 is an images showing how particle size and reconstitution method impacts reconstitution yield. The finer grind silk powder stayed above liquid level and did not wet out for reconstitution using static method vs. the rougher grind. Figures 104A- 104C are images demonstrating the ability to spray Activated Silk™. Fig.104A is a close up of aerosol nozzle during spraying. Fig.104B illustrates a spray mist stream. Fig.104C illustrates the spray pattern using aerosol can 6” above surface. Figure 105A is an image illustrating bulk “heaving” away from tray during lyophilization. Figure 105B is an image illustrating meltback. Figure 106 is a graph illustrating a bulk lyophilization example profile. Figure 107 is an image of product from Bulk freeze lyophilization. Figure 108 is an image of product meltback. Figure 109 is an image showing the discoloration of the final product. Figure 110 is a graph illustrating Profile 5 results. Figures 111A- 111C are images of Cryo Lyophliized Pellets. Fig.111A is 6% Cryo Lyophliized Pellets. Fig.111B is 10% Cryo Lyophliized Pellets. Fig.111C is 17% Cryo Lyophliized Pellets. Figure 112 is a graph illustrating a BET Isotherm linear plot. DB1 / 158748174.5 28 Figure 113 are SEM image of Lyophlized Activated Silk™ via cryopelletizing method. Figure 114 is a graph illustrating “z-average” particle size. Figure 115 is an image showing samples of the silk solution. Figure 116 are graphs showing Sample output for both Intensity and Z- Average Particle Size. Over time, particle size distribution shifts towards higher size regimes, increasing intensity peaks in that region (Left). This is summarized by an increase in the Z-Average (Right).The Python program allows for quick comparison of data across timepoints and samples. Figure 117 is an image showing the workflow for Dynamic Light Scattering, Data Processing in Python and JMP. Figure 118 is a graph illustrating in silk-only controls, 27P is unsurprisingly orders of magnitude more stable than 33B over a range of temperatures and concentrations (Below Left, Top Right). However, 33B’s faster aggregation makes it a useful model system in which to study excipient impact on aggregation rate (Below Right). (n = 3 replicates unless otherwise noted). Figure 118 are graphs illustrating baseline system aggregation for both 27P and 33B. The graphs show that 27P is orders of magnitude more stable than 33B over a range of temperatures and concentrations. Figure 119A is a graph illustrating baseline aggregation of 27P. Figure 119B is a graph illustrating the main effects on aggregation rate of the baseline system. Figure 120 is a graph illustrating z- average for various silk solutions. Figure 121 is a graph illustrating z- average for various silk solutions. Figure 122 are graphs illustrating z- average for various silk solutions. Figure 123 is an image showing soluble silk, gel silk, and particulates in solution. Figure 124 is a graph illustrating z- average for various silk solutions. Figure 125 is a graph illustrating z- average for various silk solutions. Figure 126 is a graph illustrating z- average for various silk solutions. Figures 127A-127C are graphs illustrating testing stability of concentrated 33B solutions. Fig.127A shows results from DLS testing of 33B samples. Fig.127B shows the z-average for various silk solutions at 4 °C. Fig.127C shows incubation curves at 70 °C. These graphs highlight the vast differences in aggregation profile DB1 / 158748174.5 29 with temperature, and further shows the impressive performance of PBS buffer in slowing aggregation. Figures 128A- 128B shows results of excipients from 40C Testing. Fig.128A Arginine HCl, MgCl2 > NaCl, KCl > PBS > CaCl2. Fig.128B The two best performers (ArgHCl, MgCl2 have not changed pH nor aggregated after 1085hr (45 days). Equivalent 33B / DI water fully gelled after 10 days at this temperature. Figures 129A- 129B are scans taken of solutions stored at 40° C over the course of about 45 days (Fig.129A) show a similar aggregation profile as solutions continuously scanned at 70C over the course of 1hr (Fig.129B). Figures 130A- 130C are graphs illustrating how the normalized relative aggregation rates seem to correlate between temperatures. Figures 131A- 131B are graphs showing best-performing excipients at 40C also show marked improvements at 70C compared to DI water. Figure 132 shows the equation for modeling 70C aggregation in prism. Figure 133A- 133C show 70C curves that were analyzed via the One-Phase Association model in Prism software to extract better quantitative data from samples. Figure 134 is a graph showing the results of preservative screening, specifically the continuous z-average measurements at 70C. Figure 135 is a bar graph showing the effect of various preservatives on aggravation. Figure 136 is a graph showing that salts have potential to stabilize otherwise aggregation-prone solutions. Figure 137 is a bar graph showing that salts have potential to stabilize otherwise aggregation-prone solutions. Fig.138 is a bar graph illustrating the effect of pH adjustment on mid- molecular weight silk. DETAILED DESCRIPTION The disclosure provides a lyophilized or sprayable peptide or protein fragment comprising a plurality of amino acids selected from M, R, V, K, T, F, I, L, C, A, Q, Y, N, D, E, G, S, H, P, and W, wherein at least one of the amino acids is modified, substituted, or replaced as disclosed herein. The disclosure provides a pouch comprising a plurality of holes, wherein the pouch encloses a substantially solid formulation comprising silk fibroin fragments. DB1 / 158748174.5 30 The disclosure further provides a method of reconstituting a substantially solid formulation comprising silk fibroin fragments in a solvent. The disclosure also provides a method of making a pouch enclosing a substantially solid formulation of silk fibroin fragments. Silk is a natural polymer produced by a variety of insects and spiders. Silk produced by Bombyx mori (silkworm) comprises a filament core protein, silk fibroin, and a glue-like coating consisting of a nonfilamentous protein, sericin. Silk fibroin is a FDA approved, edible, non-toxic, and relative inexpensive silkworm cocoon derived proteins. The structure and content of amino acids in the silk fibroin protein are very similar to the tissue of the human body. Methods of making silk fibroin or silk fibroin-based protein fragments are known and are described for example in U.S. Patents Nos.9,187,538, 9,511,012, 9,517,191, 9,522,107, 9,522,108, 9,545,369, and 10,166,177, all of which are incorporated herein in their entireties. Definitions As used in the preceding sections and throughout the rest of this specification, unless defined otherwise, all technical and scientific terms used herein have the same meaning as is commonly understood by one skilled in the art to which this disclosure belongs. All patents and publications referred to herein are incorporated by reference in their entireties. All percentages, parts and ratios are based upon the total weight of the eye care compositions of the present disclosure, unless otherwise specified. All such weights as they pertain to listed ingredients are based on the active level and, therefore, do not include solvents or by-products that may be included in commercially available materials, unless otherwise specified. The term “weight percent” may be denoted as “wt. %” or % w / w herein. As used herein, the term “a”, “an”, or “the” generally is construed to cover both the singular and the plural forms. The term “about” as used herein, generally refers to a particular numeric value that include variation and an acceptable error range as determined by one of ordinary skill in the art, which will depend in part on how the numeric value is measured or determined, i.e., the limitations of the measurement system. For example, “about” can mean zero variation, and a range of ±20%, ±10%, or ±5% of a given numeric value. DB1 / 158748174.5 31 As used herein, the term “dermatologically acceptable carrier” means a carrier suitable for use in contact with mammalian keratinous tissue without causing any adverse effects such as undue toxicity, incompatibility, instability, allergic response, for example. A dermatologically acceptable carrier may include, without limitations, water, liquid or solid emollients, humectants, solvents, and the like. As used herein, the term “hydrophilic-lipophilic balance” (HLB) of a surfactant is a measure of the degree to which it is hydrophilic or hydrophobic, as determined by calculating values for the different regions of the molecule, as described by Griffin’s method HLB = 20 * Mh / M, where Mhis the molecular mass of the hydrophilic portion of the surfactant, and M is the molecular mass of the entire surfactant molecule, giving a result on a scale of 0 to 20. A HLB value of 0 corresponds to a completely lipophilic molecule, and a value of 20 corresponds to a completely hydrophilic molecule. The HLB value can be used to predict the surfactant properties of a molecule: HLB < 10: Lipid-soluble (water-insoluble), HLB >10: Water-soluble (lipid-insoluble), HLB = 1-3: anti-foaming agent, 3-6: W / O (water-in- oil) emulsifier, 7-9: wetting and spreading agent, 8-16: O / W (oil-in-water) emulsifier, 13-16: detergent, 16-18: solubilizer or hydrotrope. As used herein, “average weight average molecular weight” refers to an average of two or more values of weight average molecular weight of silk fibroin or fragments thereof of the same compositions, the two or more values determined by two or more separate experimental readings. As used herein, the term polymer “polydispersity (PD)” is generally used as a measure of the broadness of a molecular weight distribution of a polymer, and is defined by the formula polydispersity^^^^^^^^ PD = ^^^^^^^^ . As used herein, the term “substantially homogeneous” may refer to silk fibroin- based protein fragments that are distributed in a normal distribution about an identified molecular weight. As used herein, the term “substantially homogeneous” may refer to an even distribution of a component or an additive, for example, silk fibroin fragments, dermatologically acceptable carrier, etc., throughout a composition of the present disclosure. As used herein, the terms “silk fibroin peptide,” “silk fibroin protein fragment,” and “silk fibroin fragment” are used interchangeably. Molecular weight or DB1 / 158748174.5 32 number of amino acids units are defined when molecular size becomes an important parameter. As used herein, the term “fast-dissolving solid forms” refers to fast-dissolving solid forms including freeze dried forms (cakes, wafers, thin films), and compressed tablets. As used herein, the terms “peptide” or “protein” refers to a chain of amino acids that are held together by peptide bonds (also called amide bonds). The basic distinguishing factors for proteins and peptides are size and structure. Peptides are smaller than proteins. Traditionally, peptides are defined as molecules that consist of between 2 and 50 amino acids, whereas proteins are made up of 50 or more amino acids. In addition, peptides tend to be less well defined in structure than proteins, which can adopt complex conformations known as secondary, tertiary, and quaternary structures. As used herein, the term “fibroin” or “silk protein” is a type of structural protein produced by certain spider and insect species that produce silk (See definition provided in WIPO Pearl-WIPO’s Multilingual Terminology Portal database, https: / / wipopearl.wipo.int / en / linguistic). Fibroin may include silkworm fibroin, insect or spider silk protein (e.g., spidroin), recombinant spider protein, silk proteins present in other spider silk types, e.g., tubuliform silk protein (TuSP), flagelliform silk protein, minor ampullate silk proteins, aciniform silk protein, pyriform silk protein, aggregate silk glue), silkworm fibroin produced by genetically modified silkworm, or recombinant silkworm fibroin. As used herein, the term “silk fibroin” refers to silkworm fibroin, silk fibroin produced by genetically modified silkworm, or recombinant silkworm fibroin (See (1) Narayan Ed., Encyclopedia of Biomedical Engineering, Vol.2, Elsevier, 2019; (2) Kobayashi et al. Eds, Encyclopedia of Polymeric Nanomaterials, Springer, 2014, https: / / link.springer.com / referenceworkentry / 10.1007%2F978-3-642-36199-9_323-1). In an embodiment, silk fibroin is obtained from Bombyx mori. The term “solid solution” as used herein, refers to the active agent molecularly dissolved in the solid excipient matrix such as hydrophobic polymers, wherein the active agent is miscible with the polymer matrix excipient. The term “solid dispersion” as used herein, refers to the active agent dispersed as crystalline or amorphous particles, wherein the active agent is dispersed in an DB1 / 158748174.5 33 amorphous polymer and is distributed at random between the polymer matrix excipient. As used herein, the term “substantially homogeneous” may refer to silk fibroin-based protein fragments that are distributed in a normal distribution about an identified molecular weight. As used herein, the term “substantially homogeneous” may also refer to an even distribution of a component or an additive, for example, silk fibroin-based protein fragments, dermatologically acceptable carrier, etc., throughout a silk composition or formulation. As used herein, the term “surface tension” refers to the tendency of fluid surfaces to shrink into the minimum surface area possible. At liquid–air interfaces, surface tension results from the greater attraction of liquid molecules to each other (due to cohesion) than to the molecules in the air (due to adhesion). The net effect is an inward force at its surface that causes the liquid to behave as if its surface were covered with a stretched elastic membrane. Because of the relatively high attraction of water molecules to each other through a web of hydrogen bonds, water has a higher surface tension (72.8 mN / m at 20 °C) than most other liquids. SPF Definitions and Properties As used herein, “silk protein fragments” (SPF) include, without limitation, one or more of: “silk fibroin fragments” as defined herein; “recombinant silk fragments” as defined herein; “spider silk fragments” as defined herein; “silk fibroin-like protein fragments” as defined herein; “chemically modified silk fragments” as defined herein; and / or “sericin or sericin fragments” as defined herein. SPF may have any molecular weight values or ranges described herein, and any polydispersity values or ranges described herein. As used herein, in some embodiments the term “silk protein fragment” also refers to a silk protein that comprises or consists of at least two identical repetitive units which each independently selected from naturally-occurring silk polypeptides or of variations thereof, amino acid sequences of naturally-occurring silk polypeptides, or of combinations of both. SPF Molecular Weight and Polydispersity In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 1 to about 5 kDa. In an embodiment, a composition of the present disclosure includes SPF DB1 / 158748174.5 34 having an average weight average molecular weight selected from between about 5 to about 10 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 10 to about 15 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 15 to about 20 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 14 to about 30 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 20 to about 25 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 25 to about 30 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 30 to about 35 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 35 to about 40 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 39 to about 54 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 40 to about 45 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 45 to about 50 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 50 to about 55 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 55 to about 60 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 60 to about 65 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 65 to about 70 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 70 to about 75 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average DB1 / 158748174.5 35 molecular weight selected from between about 75 to about 80 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 80 to about 85 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 85 to about 90 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 90 to about 95 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 95 to about 100 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 100 to about 105 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 105 to about 110 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 110 to about 115 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 115 to about 120 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 120 to about 125 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 125 to about 130 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 130 to about 135 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 135 to about 140 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 140 to about 145 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 145 to about 150 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 150 to about 155 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected DB1 / 158748174.5 36 from between about 155 to about 160 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 160 to about 165 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 165 to about 170 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 170 to about 175 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 175 to about 180 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 180 to about 185 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 185 to about 190 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 190 to about 195 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 195 to about 200 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 200 to about 205 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 205 to about 210 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 210 to about 215 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 215 to about 220 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 220 to about 225 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 225 to about 230 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 230 to about 235 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about DB1 / 158748174.5 37 235 to about 240 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 240 to about 245 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 245 to about 250 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 250 to about 255 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 255 to about 260 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 260 to about 265 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 265 to about 270 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 270 to about 275 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 275 to about 280 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 280 to about 285 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 285 to about 290 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 290 to about 295 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 295 to about 300 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 300 to about 305 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 305 to about 310 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 310 to about 315 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 315 to about DB1 / 158748174.5 38 320 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 320 to about 325 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 325 to about 330 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 330 to about 335 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 335 to about 340 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 340 to about 345 kDa. In an embodiment, a composition of the present disclosure includes SPF having an average weight average molecular weight selected from between about 345 to about 350 kDa. In some embodiments, compositions of the present disclosure include SPF compositions selected from compositions #1001 to #3500, having weight average molecular weights selected from about 1 kDa to about 250 kDa, and a polydispersity selected from between 1 and about 5 (including, without limitation, a polydispersity of 1), between 1 and about 1.5 (including, without limitation, a polydispersity of 1), between about 1.5 and about 2, between about 1.5 and about 3, between about 2 and about 2.5, between about 2.5 and about 3, between about 3 and about 3.5, between about 3.5 and about 4, between about 4 and about 4.5, and between about 4.5 and about 5: 4.5-5 1010 1020 1030 1040 1050 1060 1070 1080 1090 DB1 / 158748174.5 39 1100 1110 1120 1130 1140 1150 1160 1170 1180 1190 1200 1210 1220 1230 1240 1250 1260 1270 1280 1290 1300 1310 1320 1330 1340 1350 1360 1370 1380 1390 1400 1410 1420 1430 1440 1450 1460 1470 1480 1490 1500 1510 1520 1530 1540 1550 DB1 / 158748174.5 40 1560 1570 1580 1590 1600 1610 1620 1630 1640 1650 1660 1670 1680 1690 1700 1710 1720 1730 1740 1750 1760 1770 1780 1790 1800 1810 1820 1830 1840 1850 1860 1870 1880 1890 1900 1910 1920 1930 1940 1950 1960 1970 1980 1990 2000 2010 DB1 / 158748174.5 41 020 030 040 050 060 070 080 090 100 110 120 130 140 150 160 170 180 190 200 210 220 230 240 250 260 270 280 290 300 310 320 330 340 350 360 370 380 390 400 410 420 430 440 450 2460 2470 DB1 / 158748174.5 42 2480 2490 2500 2510 2520 2530 2540 2550 2560 2570 2580 2590 2600 2610 2620 2630 2640 2650 2660 2670 2680 2690 2700 2710 2720 2730 2740 2750 2760 2770 2780 2790 2800 2810 2820 2830 2840 2850 2860 2870 2880 2890 2900 2910 2920 2930 DB1 / 158748174.5 43 2940 2950 2960 2970 2980 2990 3000 3010 3020 3030 3040 3050 3060 3070 3080 3090 3100 3110 3120 3130 3140 3150 3160 3170 3180 3190 3200 3210 3220 3230 3240 3250 3260 3270 3280 3290 3300 3310 3320 3330 3340 3350 3360 3370 3380 3390 DB1 / 158748174.5 44 3400 3410 3420 3430 3440 3450 3460 3470 3480 3490 3500 As used herein, “low molecular weight,” “low MW,” or “low-MW” SPF may include SPF having a weight average molecular weight, or average weight average molecular weight selected from between about 5 kDa to about 38 kDa, about 14 kDa to about 30 kDa, or about 6 kDa to about 17 kDa. In some embodiments, a target low molecular weight for certain SPF may be weight average molecular weight of about 5 kDa, about 6 kDa, about 7 kDa, about 8 kDa, about 9 kDa, about 10 kDa, about 11 kDa, about 12 kDa, about 13 kDa, about 14 kDa, about 15 kDa, about 16 kDa, about 17 kDa, about 18 kDa, about 19 kDa, about 20 kDa, about 21 kDa, about 22 kDa, about 23 kDa, about 24 kDa, about 25 kDa, about 26 kDa, about 27 kDa, about 28 kDa, about 29 kDa, about 30 kDa, about 31 kDa, about 32 kDa, about 33 kDa, about 34 kDa, about 35 kDa, about 36 kDa, about 37 kDa, or about 38 kDa. As used herein, “medium molecular weight,” “medium MW,” or “mid-MW” SPF may include SPF having a weight average molecular weight, or average weight average molecular weight selected from between about 31 kDa to about 55 kDa, or about 39 kDa to about 54 kDa. In some embodiments, a target medium molecular weight for certain SPF may be weight average molecular weight of about 31 kDa, about 32 kDa, about 33 kDa, about 34 kDa, about 35 kDa, about 36 kDa, about 37 kDa, about 38 kDa, about 39 kDa, about 40 kDa, about 41 kDa, about 42 kDa, about 43 kDa, about 44 kDa, about 45 kDa, about 46 kDa, about 47 kDa, about 48 kDa, about 49 kDa, about 50 kDa, about 51 kDa, about 52 kDa, about 53 kDa, about 54 kDa, or about 55 kDa. As used herein, “high molecular weight,” “high MW,” or “high-MW” SPF may include SPF having a weight average molecular weight, or average weight average molecular weight selected from between about 55 kDa to about 150 kDa. In some embodiments, a target high molecular weight for certain SPF may be about 55 DB1 / 158748174.5 45 kDa, about 56 kDa, about 57 kDa, about 58 kDa, about 59 kDa, about 60 kDa, about 61 kDa, about 62 kDa, about 63 kDa, about 64 kDa, about 65 kDa, about 66 kDa, about 67 kDa, about 68 kDa, about 69 kDa, about 70 kDa, about 71 kDa, about 72 kDa, about 73 kDa, about 74 kDa, about 75 kDa, about 76 kDa, about 77 kDa, about 78 kDa, about 79 kDa, or about 80 kDa. In some embodiments, the molecular weights described herein (e.g., low molecular weight silk, medium molecular weight silk, high molecular weight silk) may be converted to the approximate number of amino acids contained within the respective SPF, as would be understood by a person having ordinary skill in the art. For example, the average weight of an amino acid may be about 110 Daltons (i.e., 110 g / mol). Therefore, in some embodiments, dividing the molecular weight of a linear protein by 110 Daltons may be used to approximate the number of amino acid residues contained therein. In an embodiment, SPF in a composition of the present disclosure have a polydispersity selected from between 1 to about 5.0, including, without limitation, a polydispersity of 1. In an embodiment, SPF in a composition of the present disclosure have a polydispersity selected from between about 1.5 to about 3.0. In an embodiment, SPF in a composition of the present disclosure have a polydispersity selected from between 1 to about 1.5, including, without limitation, a polydispersity of 1. In an embodiment, SPF in a composition of the present disclosure have a polydispersity selected from between about 1.5 to about 2.0. In an embodiment, SPF in a composition of the present disclosure have a polydispersity selected from between about 2.0 to about 2.5. In an embodiment, SPF in a composition of the present disclosure have a polydispersity selected from between about 2.5 to about 3.0. In an embodiment, SPF in a composition of the present disclosure have a polydispersity selected from between about 3.0 to about 3.5. In an embodiment, SPF in a composition of the present disclosure have a polydispersity selected from between about 3.5 to about 4.0. In an embodiment, SPF in a composition of the present disclosure have a polydispersity selected from between about 4.0 to about 4.5. In an embodiment, SPF in a composition of the present disclosure have a polydispersity selected from between about 4.5 to about 5.0. In an embodiment, SPF in a composition of the present disclosure have a polydispersity of 1. In an embodiment, SPF in a composition of the present disclosure have a polydispersity of about 1.1. In an embodiment, SPF in a composition of the DB1 / 158748174.5 46 present disclosure have a polydispersity of about 1.2. In an embodiment, SPF in a composition of the present disclosure have a polydispersity of about 1.3. In an embodiment, SPF in a composition of the present disclosure have a polydispersity of about 1.4. In an embodiment, SPF in a composition of the present disclosure have a polydispersity of about 1.5. In an embodiment, SPF in a composition of the present disclosure have a polydispersity of about 1.6. In an embodiment, SPF in a composition of the present disclosure have a polydispersity of about 1.7. In an embodiment, SPF in a composition of the present disclosure have a polydispersity of about 1.8. In an embodiment, SPF in a composition of the present disclosure have a polydispersity of about 1.9. In an embodiment, SPF in a composition of the present disclosure have a polydispersity of about 2.0. In an embodiment, SPF in a composition of the present disclosure have a polydispersity of about 2.1. In an embodiment, SPF in a composition of the present disclosure have a polydispersity of about 2.2. In an embodiment, SPF in a composition of the present disclosure have a polydispersity of about 2.3. In an embodiment, SPF in a composition of the present disclosure have a polydispersity of about 2.4. In an embodiment, SPF in a composition of the present disclosure have a polydispersity of about 2.5. In an embodiment, SPF in a composition of the present disclosure have a polydispersity of about 2.6. In an embodiment, SPF in a composition of the present disclosure have a polydispersity of about 2.7. In an embodiment, SPF in a composition of the present disclosure have a polydispersity of about 2.8. In an embodiment, SPF in a composition of the present disclosure have a polydispersity of about 2.9. In an embodiment, SPF in a composition of the present disclosure have a polydispersity of about 3.0. In an embodiment, SPF in a composition of the present disclosure have a polydispersity of about 3.1. In an embodiment, SPF in a composition of the present disclosure have a polydispersity of about 3.2. In an embodiment, SPF in a composition of the present disclosure have a polydispersity of about 3.3. In an embodiment, SPF in a composition of the present disclosure have a polydispersity of about 3.4. In an embodiment, SPF in a composition of the present disclosure have a polydispersity of about 3.5. In an embodiment, SPF in a composition of the present disclosure have a polydispersity of about 3.6. In an embodiment, SPF in a composition of the present disclosure have a polydispersity of about 3.7. In an embodiment, SPF in a composition of the present disclosure have a polydispersity of about 3.8. In an embodiment, SPF in a composition of the present disclosure have a DB1 / 158748174.5 47 polydispersity of about 3.9. In an embodiment, SPF in a composition of the present disclosure have a polydispersity of about 4.0. In an embodiment, SPF in a composition of the present disclosure have a polydispersity of about 4.1. In an embodiment, SPF in a composition of the present disclosure have a polydispersity of about 4.2. In an embodiment, SPF in a composition of the present disclosure have a polydispersity of about 4.3. In an embodiment, SPF in a composition of the present disclosure have a polydispersity of about 4.4. In an embodiment, SPF in a composition of the present disclosure have a polydispersity of about 4.5. In an embodiment, SPF in a composition of the present disclosure have a polydispersity of about 4.6. In an embodiment, SPF in a composition of the present disclosure have a polydispersity of about 4.7. In an embodiment, SPF in a composition of the present disclosure have a polydispersity of about 4.8. In an embodiment, SPF in a composition of the present disclosure have a polydispersity of about 4.9. In an embodiment, SPF in a composition of the present disclosure have a polydispersity of about 5.0. In some embodiments, in compositions described herein having combinations of low, medium, and / or high molecular weight SPF, such low, medium, and / or high molecular weight SPF may have the same or different polydispersities. Silk Fibroin Fragments Methods of making silk fibroin or silk fibroin protein fragments and their applications in various fields are known and are described for example in U.S. Patents Nos.9,187,538, 9,511,012, 9,517,191, 9,522,107, 9,522,108, 9,545,369, and 10,166,177, 10,287,728 and 10,301,768, all of which are incorporated herein in their entireties. Raw silk from silkworm Bombyx mori is composed of two primary proteins: silk fibroin (approximately 75%) and sericin (approximately 25%). Silk fibroin is a fibrous protein with a semi-crystalline structure that provides stiffness and strength. As used herein, the term “silk fibroin” means the fibers of the cocoon of Bombyx mori having a weight average molecular weight of about 370,000 Da. The crude silkworm fiber consists of a double thread of fibroin. The adhesive substance holding these double fibers together is sericin. The silk fibroin is composed of a heavy chain having a weight average molecular weight of about 350,000 Da (H chain), and a light chain having a weight average molecular weight about 25,000 Da (L chain). Silk fibroin is an amphiphilic polymer with large hydrophobic domains occupying the DB1 / 158748174.5 48 major component of the polymer, which has a high molecular weight. The hydrophobic regions are interrupted by small hydrophilic spacers, and the N- and C- termini of the chains are also highly hydrophilic. The hydrophobic domains of the H- chain contain a repetitive hexapeptide sequence of Gly-Ala-Gly-Ala-Gly-Ser and repeats of Gly-Ala / Ser / Tyr dipeptides, which can form stable anti-parallel-sheet crystallites. The amino acid sequence of the L-chain is non-repetitive, so the L-chain is more hydrophilic and relatively elastic. The hydrophilic (Tyr, Ser) and hydrophobic (Gly, Ala) chain segments in silk fibroin molecules are arranged alternatively such that allows self-assembling of silk fibroin molecules. Provided herein are methods for producing pure and highly scalable silk fibroin-protein fragment mixture solutions that may be used across multiple industries for a variety of applications. Without wishing to be bound by any particular theory, it is believed that these methods are equally applicable to fragmentation of any SPF described herein, including without limitation recombinant silk proteins, and fragmentation of silk-like or fibroin-like proteins. As used herein, the term “fibroin” includes silk worm fibroin and insect or spider silk protein. In an embodiment, fibroin is obtained from Bombyx mori. Raw silk from Bombyx mori is composed of two primary proteins: silk fibroin (approximately 75%) and sericin (approximately 25%). Silk fibroin is a fibrous protein with a semi-crystalline structure that provides stiffness and strength. As used herein, the term “silk fibroin” means the fibers of the cocoon of Bombyx mori having a weight average molecular weight of about 370,000 Da. Conversion of these insoluble silk fibroin fibrils into water-soluble silk fibroin protein fragments requires the addition of a concentrated neutral salt (e.g., 8-10 M lithium bromide), which interferes with inter- and intramolecular ionic and hydrogen bonding that would otherwise render the fibroin protein insoluble in water. Methods of making silk fibroin protein fragments, and / or compositions thereof, are known and are described for example in U.S. Patents Nos.9,187,538, 9,511,012, 9,517,191, 9,522,107, 9,522,108, 9,545,369, and 10,166,177. The raw silk cocoons from the silkworm Bombyx mori was cut into pieces. The pieces silk cocoons were processed in an aqueous solution of Na2CO3 at about 100 °C for about 60 minutes to remove sericin (degumming). The volume of the water used equals about 0.4 x raw silk weight and the amount of Na2CO3is about 0.848 x the weight of the raw silk cocoon pieces. The resulting degummed silk cocoon pieces DB1 / 158748174.5 49 were rinsed with deionized water three times at about 60 °C (20 minutes per rinse). The volume of rinse water for each cycle was 0.2 L x the weight of the raw silk cocoon pieces. The excess water from the degummed silk cocoon pieces was removed. After the DI water washing step, the wet degummed silk cocoon pieces were dried at room temperature. The degummed silk cocoon pieces were mixed with a LiBr solution, and the mixture was heated to about 100 °C. The warmed mixture was placed in a dry oven and was heated at about 100 °C for about 60 minutes to achieve complete dissolution of the native silk protein. The resulting silk fibroin solution was filtered and dialyzed using Tangential Flow Filtration (TFF) and a 10 kDa membrane against deionized water for 72 hours. The resulting silk fibroin aqueous solution has a concentration of about 8.5 wt. %. Then, 8.5 % silk solution was diluted with water to result in a 1.0 % w / v silk solution. TFF can then be used to further concentrate the pure silk solution to a concentration of 20.0 % w / w silk to water. Dialyzing the silk through a series of water changes is a manual and time intensive process, which could be accelerated by changing certain parameters, for example diluting the silk solution prior to dialysis. The dialysis process could be scaled for manufacturing by using semi-automated equipment, for example a tangential flow filtration system. In some embodiments, the silk solutions are prepared under various preparation condition parameters such as: 90 °C 30 min, 90 °C 60 min, 100 °C 30 min, and 100 °C 60 min. Briefly, 9.3 M LiBr was prepared and allowed to sit at room temperature for at least 30 minutes.5 mL of LiBr solution was added to 1.25 g of silk and placed in the 60 °C oven. Samples from each set were removed at 4, 6, 8, 12, 24, 168 and 192 hours. In some embodiments, the silk solutions are prepared under various preparation condition parameters such as: 90 °C 30 min, 90 °C 60 min, 100 °C 30 min, and 100 °C 60 min. Briefly, 9.3 M LiBr solution was heated to one of four temperatures: 60 °C, 80 °C, 100 °C or boiling.5 mL of hot LiBr solution was added to 1.25 g of silk and placed in the 60 °C oven. Samples from each set were removed at 1, 4 and 6 hours. In some embodiments, the silk solutions are prepared under various preparation condition parameters such as: Four different silk extraction combinations were used: 90 °C 30 min, 90 °C 60 min, 100 °C 30 min, and 100 °C 60 min. Briefly, 9.3 M LiBr solution was heated to one of four temperatures: 60 °C, 80 °C, 100 °C or DB1 / 158748174.5 50 boiling.5 mL of hot LiBr solution was added to 1.25 g of silk and placed in the oven at the same temperature of the LiBr. Samples from each set were removed at 1, 4 and 6 hours.1 mL of each sample was added to 7.5 mL of 9.3 M LiBr and refrigerated for viscosity testing. In some embodiments, SPF are obtained by dissolving raw unscoured, partially scoured, or scoured silkworm fibers with a neutral lithium bromide salt. The raw silkworm silks are processed under selected temperature and other conditions in order to remove any sericin and achieve the desired weight average molecular weight (MW) and polydispersity (PD) of the fragment mixture. Selection of process parameters may be altered to achieve distinct final silk protein fragment characteristics depending upon the intended use. The resulting final fragment solution is silk fibroin protein fragments and water with parts per million (ppm) to non- detectable levels of process contaminants, levels acceptable in the pharmaceutical, medical and consumer eye care markets. The concentration, size and polydispersity of SPF may further be altered depending upon the desired use and performance requirements. Methods of making silk protein fragments used in the compositions of the present disclosure are demonstrated in U.S. Patent Application Publication Nos. 2015 / 00933340, 2015 / 0094269, 2016 / 0193130, 2016 / 0022560, 2016 / 0022561, 2016 / 0022562, 2016 / 0022563, and 2016 / 0222579, 2016 / 0281294, and U.S. Patent Nos.9,187,538, 9,522,107, 9,517,191, 9,522,108, 9,511,012, and 9,545,369, the entirety of which are incorporated herein by reference. However, an exemplary method is demonstrated in Fig.70, which is a flow chart showing various embodiments for producing pure silk fibroin-based protein fragments (SPFs) of the present disclosure. It should be understood that not all of the steps illustrated are necessarily required to fabricate all silk solutions of the present disclosure. As illustrated in Fig.70, step A, cocoons (heat-treated or non-heat-treated), silk fibers, silk powder or spider silk can be used as the silk source. If starting from raw silk cocoons from Bombyx mori, the cocoons can be cut into small pieces, for example pieces of approximately equal size, step B1. The raw silk is then extracted and rinsed to remove any sericin, step C1a. This results in substantially sericin free raw silk. In an embodiment, water is heated to a temperature between 84 °C and 100 °C (ideally boiling) and then Na2CO3(sodium carbonate) is added to the boiling water until the Na2CO3 is completely dissolved. The raw silk is added to the boiling water / Na2CO3 DB1 / 158748174.5 51 (100 °C) and submerged for approximately 15 - 90 minutes, where boiling for a longer time results in smaller silk protein fragments. In an embodiment, the water volume equals about 0.4 x raw silk weight and the Na2CO3volume equals about 0.848 x raw silk weight. In an embodiment, the water volume equals 0.1 x raw silk weight and the Na2CO3 volume is maintained at 2.12 g / L. This is demonstrated in Fig.72 and Fig.73: silk mass (x-axis) was varied in the same volume of extraction solution (i.e., the same volume of water and concentration of Na2CO3) achieving sericin removal (substantially sericin free) as demonstrated by an overall silk mass loss of 26 to 31 percent (y-axis). Subsequently, the water dissolved Na2CO3solution is drained and excess water / Na2CO3 is removed from the silk fibroin fibers (e.g., ring out the fibroin extract by hand, spin cycle using a machine, etc.). The resulting silk fibroin extract is rinsed with warm to hot water to remove any remaining adsorbed sericin or contaminate, typically at a temperature range of about 40 °C to about 80 °C, changing the volume of water at least once (repeated for as many times as required). The resulting silk fibroin extract is a substantially sericin-depleted silk fibroin. In an embodiment, the resulting silk fibroin extract is rinsed with water at a temperature of about 60 °C. In an embodiment, the volume of rinse water for each cycle equals 0.1 L to 0.2 L x raw silk weight. It may be advantageous to agitate, turn or circulate the rinse water to maximize the rinse effect. After rinsing, excess water is removed from the extracted silk fibroin fibers (e.g., ring out fibroin extract by hand or using a machine). Alternatively, methods known to one skilled in the art such as pressure, temperature, or other reagents or combinations thereof may be used for the purpose of sericin extraction. Alternatively, the silk gland (100% sericin free silk protein) can be removed directly from a worm. This would result in liquid silk protein, without any alteration of the protein structure, free of sericin. The extracted fibroin fibers are then allowed to dry completely. Once dry, the extracted silk fibroin is dissolved using a solvent added to the silk fibroin at a temperature between ambient and boiling, step C1b. In an embodiment, the solvent is a solution of Lithium bromide (LiBr) (boiling for LiBr is 140 °C). Alternatively, the extracted fibroin fibers are not dried but wet and placed in the solvent; solvent concentration can then be varied to achieve similar concentrations as to when adding dried silk to the solvent. The final concentration of LiBr solvent can range from 0.1 M to 9.3 M. Table D is a table summarizing the Molecular Weights of silk dissolved DB1 / 158748174.5 52 from different concentrations of Lithium Bromide (LiBr) and from different extraction and dissolution sizes. Complete dissolution of the extracted fibroin fibers can be achieved by varying the treatment time and temperature along with the concentration of dissolving solvent. Other solvents may be used including, but not limited to, phosphate phosphoric acid, calcium nitrate, calcium chloride solution or other concentrated aqueous solutions of inorganic salts. To ensure complete dissolution, the silk fibers should be fully immersed within the already heated solvent solution and then maintained at a temperature ranging from about 60 °C to about 140 °C for 1-168 hrs. In an embodiment, the silk fibers should be fully immersed within the solvent solution and then placed into a dry oven at a temperature of about 100 °C for about 1 hour. Table D: Molecular Weights of silk dissolved from different concentrations of LiBr and from different extraction and dissolution sizes The temperature at which the silk fibroin extract is added to the LiBr solution (or vice versa) has an effect on the time required to completely dissolve the fibroin and on the resulting molecular weight and polydispersity of the final SPF mixture solution. In an embodiment, silk solvent solution concentration is less than or equal to 20% w / v. In addition, agitation during introduction or dissolution may be used to DB1 / 158748174.5 53 facilitate dissolution at varying temperatures and concentrations. The temperature of the LiBr solution will provide control over the silk protein fragment mixture molecular weight and polydispersity created. In an embodiment, a higher temperature will more quickly dissolve the silk offering enhanced process scalability and mass production of silk solution. In an embodiment, using a LiBr solution heated to a temperature between 80 °C - 140 °C reduces the time required in an oven in order to achieve full dissolution. Varying time and temperature at or above 60 °C of the dissolution solvent will alter and control the MW and polydispersity of the SPF mixture solutions formed from the original molecular weight of the native silk fibroin protein. Alternatively, whole cocoons may be placed directly into a solvent, such as LiBr, bypassing extraction, step B2. This requires subsequent filtration of silk worm particles from the silk and solvent solution and sericin removal using methods know in the art for separating hydrophobic and hydrophilic proteins such as a column separation and / or chromatography, ion exchange, chemical precipitation with salt and / or pH, and or enzymatic digestion and filtration or extraction, all methods are common examples and without limitation for standard protein separation methods, step C2. Non-heat treated cocoons with the silkworm removed, may alternatively be placed into a solvent such as LiBr, bypassing extraction. The methods described above may be used for sericin separation, with the advantage that non-heat treated cocoons will contain significantly less worm debris. Dialysis may be used to remove the dissolution solvent from the resulting dissolved fibroin protein fragment solution by dialyzing the solution against a volume of water, step E1. Pre-filtration prior to dialysis is helpful to remove any debris (i.e., silk worm remnants) from the silk and LiBr solution, step D. In one example, a 3 μm or 5 μm filter is used with a flow-rate of 200-300 mL / min to filter a 0.1% to 1.0% silk-LiBr solution prior to dialysis and potential concentration if desired. A method disclosed herein, as described above, is to use time and / or temperature to decrease the concentration from 9.3 M LiBr to a range from 0.1 M to 9.3 M to facilitate filtration and downstream dialysis, particularly when considering creating a scalable process method. Alternatively, without the use of additional time or temperate, a 9.3 M LiBr- silk protein fragment solution may be diluted with water to facilitate debris filtration and dialysis. The result of dissolution at the desired time and temperate filtration is a translucent particle-free room temperature shelf-stable silk protein fragment-LiBr DB1 / 158748174.5 54 solution of a known MW and polydispersity. It is advantageous to change the dialysis water regularly until the solvent has been removed (e.g., change water after 1 hour, 4 hours, and then every 12 hours for a total of 6 water changes). The total number of water volume changes may be varied based on the resulting concentration of solvent used for silk protein dissolution and fragmentation. After dialysis, the final silk solution maybe further filtered to remove any remaining debris (i.e., silk worm remnants). Alternatively, Tangential Flow Filtration (TFF), which is a rapid and efficient method for the separation and purification of biomolecules, may be used to remove the solvent from the resulting dissolved fibroin solution, step E2. TFF offers a highly pure aqueous silk protein fragment solution and enables scalability of the process in order to produce large volumes of the solution in a controlled and repeatable manner. The silk and LiBr solution may be diluted prior to TFF (20% down to 0.1% silk in either water or LiBr). Pre-filtration as described above prior to TFF processing may maintain filter efficiency and potentially avoids the creation of silk gel boundary layers on the filter’s surface as the result of the presence of debris particles. Pre- filtration prior to TFF is also helpful to remove any remaining debris (i.e., silk worm remnants) from the silk and LiBr solution that may cause spontaneous or long-term gelation of the resulting water only solution, step D. TFF, recirculating or single pass, may be used for the creation of water-silk protein fragment solutions ranging from 0.1% silk to 30.0% silk (more preferably, 0.1% - 6.0% silk). Different cutoff size TFF membranes may be required based upon the desired concentration, molecular weight and polydispersity of the silk protein fragment mixture in solution. Membranes ranging from 1-100 kDa may be necessary for varying molecular weight silk solutions created for example by varying the length of extraction boil time or the time and temperate in dissolution solvent (e.g., LiBr). In an embodiment, a TFF 5 or 10 kDa membrane is used to purify the silk protein fragment mixture solution and to create the final desired silk-to-water ratio. As well, TFF single pass, TFF, and other methods known in the art, such as a falling film evaporator, may be used to concentrate the solution following removal of the dissolution solvent (e.g., LiBr) (with resulting desired concentration ranging from 0.1% to 30% silk). This can be used as an alternative to standard HFIP concentration methods known in the art to create a water- based solution. A larger pore membrane could also be utilized to filter out small silk DB1 / 158748174.5 55 protein fragments and to create a solution of higher molecular weight silk with and / or without tighter polydispersity values. Table C is a table summarizing Molecular Weights for some embodiments of silk protein solutions of the present disclosure. Silk protein solution processing conditions were as follows: 100 °C extraction for 20 min, room temperature rinse, LiBr in 60 °C oven for 4-6 hours. TFF processing conditions for water-soluble films were as follows: 100 °C extraction for 60 min, 60 °C rinse, 100 °C LiBr in 100 °C oven for 60 min. Figs.93-104 further demonstrate manipulation of extraction time, LiBr dissolution conditions, and TFF processing and resultant example molecular weights and polydispersities. These examples are not intended to be limiting, but rather to demonstrate the potential of specifying parameters for specific molecular weight silk fragment solutions. Table C: Molecular Weights of silk protein solutions of the present disclosure An assay for LiBr and Na2CO3detection was performed using an HPLC system equipped with evaporative light scattering detector (ELSD). The calculation was performed by linear regression of the resulting peak areas for the analyte plotted against concentration. More than one sample of a number of formulations of the present disclosure was used for sample preparation and analysis. Generally, four samples of different formulations were weighed directly in a 10 mL volumetric flask. The samples were suspended in 5 mL of 20 mM ammonium formate (pH 3.0) and kept at 2-8 °C for 2 hours with occasional shaking to extract analytes from the film. After 2 hours the solution was diluted with 20 mM ammonium formate (pH 3.0). The sample solution from the volumetric flask was transferred into HPLC vials and injected into the HPLC-ELSD system for the estimation of sodium carbonate and lithium bromide. The analytical method developed for the quantitation of Na2CO3 and LiBr in silk protein formulations was found to be linear in the range 10 - 165 μg / mL, with RSD for injection precision as 2% and 1% for area and 0.38% and 0.19% for retention DB1 / 158748174.5 56 time for sodium carbonate and lithium bromide respectively. The analytical method can be applied for the quantitative determination of sodium carbonate and lithium bromide in silk protein formulations. The final silk protein fragment solution is pure silk protein fragments and water with PPM to undetectable levels of particulate debris and / or process contaminants, including LiBr and Na2CO3. Tables A and B are tables summarizing LiBr and Na2CO3concentrations in solutions of the present disclosure. In Table A, the processing conditions included 100 °C extraction for 60 min, 60 °C rinse, 100 °C LiBr in 100 °C oven for 60 min. TFF conditions including pressure differential and number of dia-filtration volumes were varied. In Table B, the processing conditions included 100 °C boil for 60 min, 60 °C rinse, LiBr in 60 °C oven for 4-6 hours. Table A: Lithium Bromide and Sodium Carbonate Concentration in Silk Protein Solution of DB1 / 158748174.5 57 Table B: Lithium Bromide and Sodium Carbonate content in Silk Protein Solution ND ND ND ND ND *ND=None Detected Either the silk fragment-water solutions, the lyophilized silk protein fragment mixture, or any other compositions including SPFs, can be sterilized following standard methods in the art not limited to filtration, heat, radiation or e-beam. It is anticipated that the silk protein fragment mixture, because of its shorter protein polymer length, will withstand sterilization better than intact silk protein solutions described in the art. Additionally, silk articles created from the SPF mixtures described herein may be sterilized as appropriate to application. Fig.71 is a flow chart showing various parameters that can be modified during the process of producing a silk protein fragment solution of the present disclosure during the extraction and the dissolution steps. Select method parameters may be altered to achieve distinct final solution characteristics depending upon the intended use, e.g., molecular weight and polydispersity. It should be understood that not all of DB1 / 158748174.5 58 the steps illustrated are necessarily required to fabricate all silk solutions of the present disclosure. In an embodiment, a process for producing a silk protein fragment solution of the present disclosure includes forming pieces of silk cocoons from the Bombyx mori silk worm; extracting the pieces at about 100 °C in a solution of water and Na2CO3 for about 60 minutes, wherein a volume of the water equals about 0.4 x raw silk weight and the amount of Na2CO3is about 0.848 x the weight of the pieces to form a silk fibroin extract; triple rinsing the silk fibroin extract at about 60 °C for about 20 minutes per rinse in a volume of rinse water, wherein the rinse water for each cycle equals about 0.2 L x the weight of the pieces; removing excess water from the silk fibroin extract; drying the silk fibroin extract; dissolving the dry silk fibroin extract in a LiBr solution, wherein the LiBr solution is first heated to about 100 °C to create a silk and LiBr solution and maintained; placing the silk and LiBr solution in a dry oven at about 100 °C for about 60 minutes to achieve complete dissolution and further fragmentation of the native silk protein structure into mixture with desired molecular weight and polydispersity; filtering the solution to remove any remaining debris from the silkworm; diluting the solution with water to result in a 1% silk solution; and removing solvent from the solution using Tangential Flow Filtration (TFF). In an embodiment, a 10 kDa membrane is utilized to purify the silk solution and create the final desired silk-to-water ratio. TFF can then be used to further concentrate the pure silk solution to a concentration of 2% silk to water. Each process step from raw cocoons to dialysis is scalable to increase efficiency in manufacturing. Whole cocoons are currently purchased as the raw material, but pre-cleaned cocoons or non-heat treated cocoons, where worm removal leaves minimal debris, have also been used. Cutting and cleaning the cocoons is a manual process, however for scalability this process could be made less labor intensive by, for example, using an automated machine in combination with compressed air to remove the worm and any particulates, or using a cutting mill to cut the cocoons into smaller pieces. The extraction step, currently performed in small batches, could be completed in a larger vessel, for example an industrial washing machine where temperatures at or in between 60 °C to 100 °C can be maintained. The rinsing step could also be completed in the industrial washing machine, eliminating the manual rinse cycles. Dissolution of the silk in LiBr solution could occur in a vessel other than a convection oven, for example a stirred tank reactor. Dialyzing the DB1 / 158748174.5 59 silk through a series of water changes is a manual and time intensive process, which could be accelerated by changing certain parameters, for example diluting the silk solution prior to dialysis. The dialysis process could be scaled for manufacturing by using semi-automated equipment, for example a tangential flow filtration system. Without wishing to be bound by any particular theory, varying extraction (i.e., time and temperature), LiBr (i.e., temperature of LiBr solution when added to silk fibroin extract or vice versa) and dissolution (i.e., time and temperature) parameters results in solvent and silk solutions with different viscosities, homogeneities, and colors. While also not wishing to be bound by any particular theory, increasing the temperature for extraction, lengthening the extraction time, using a higher temperature LiBr solution at emersion and over time when dissolving the silk and increasing the time at temperature (e.g., in an oven as shown here, or an alternative heat source) all resulted in less viscous and more homogeneous solvent and silk solutions. While almost all parameters resulted in a viable silk solution, methods that allow complete dissolution to be achieved in fewer than 4 to 6 hours are preferred for process scalability. In an embodiment, solutions of silk fibroin protein fragments having a weight average selected from between about 6 kDa to about 17 kDa are prepared according to following steps: degumming a silk source by adding the silk source to a boiling (100 °C) aqueous solution of sodium carbonate for a treatment time of between about 30 minutes to about 60 minutes; removing sericin from the solution to produce a silk fibroin extract comprising non- detectable levels of sericin; draining the solution from the silk fibroin extract; dissolving the silk fibroin extract in a solution of lithium bromide having a starting temperature upon placement of the silk fibroin extract in the lithium bromide solution that ranges from about 60 °C to about 140 °C; maintaining the solution of silk fibroin-lithium bromide in an oven having a temperature of about 140 °C for a period of at most 1 hour; removing the lithium bromide from the silk fibroin extract; and producing an aqueous solution of silk protein fragments, the aqueous solution comprising: fragments having a weight average molecular weight selected from between about 6 kDa to about 17 kDa, and a polydispersity of between 1 and about 5, or between about 1.5 and about 3.0. The method may further comprise drying the silk fibroin extract prior to the dissolving step. The aqueous solution of silk fibroin protein fragments may comprise lithium bromide residuals of less than 300 ppm as measured using a high-performance liquid chromatography lithium bromide DB1 / 158748174.5 60 assay. The aqueous solution of silk fibroin protein fragments may comprise sodium carbonate residuals of less than 100 ppm as measured using a high-performance liquid chromatography sodium carbonate assay. The aqueous solution of silk fibroin protein fragments may be lyophilized. In some embodiments, the silk fibroin protein fragment solution may be further processed into various forms including gel, powder, and nanofiber. In an embodiment, solutions of silk fibroin protein fragments having a weight average molecular weight selected from between about 17 kDa to about 39 kDa are prepared according to the following steps: adding a silk source to a boiling (100 °C) aqueous solution of sodium carbonate for a treatment time of between about 30 minutes to about 60 minutes so as to result in degumming; removing sericin from the solution to produce a silk fibroin extract comprising non-detectable levels of sericin; draining the solution from the silk fibroin extract; dissolving the silk fibroin extract in a solution of lithium bromide having a starting temperature upon placement of the silk fibroin extract in the lithium bromide solution that ranges from about 80 °C to about 140 °C; maintaining the solution of silk fibroin-lithium bromide in a dry oven having a temperature in the range between about 60 °C to about 100 °C for a period of at most 1 hour; removing the lithium bromide from the silk fibroin extract; and producing an aqueous solution of silk fibroin protein fragments, wherein the aqueous solution of silk fibroin protein fragments comprises lithium bromide residuals of between about 10 ppm and about 300 ppm, wherein the aqueous solution of silk protein fragments comprises sodium carbonate residuals of between about 10 ppm and about 100 ppm, wherein the aqueous solution of silk fibroin protein fragments comprises fragments having a weight average molecular weight selected from between about 17 kDa to about 39 kDa, and a polydispersity of between 1 and about 5, or between about 1.5 and about 3.0. The method may further comprise drying the silk fibroin extract prior to the dissolving step. The aqueous solution of silk fibroin protein fragments may comprise lithium bromide residuals of less than 300 ppm as measured using a high- performance liquid chromatography lithium bromide assay. The aqueous solution of silk fibroin protein fragments may comprise sodium carbonate residuals of less than 100 ppm as measured using a high-performance liquid chromatography sodium carbonate assay. In some embodiments, a method for preparing an aqueous solution of silk fibroin protein fragments having an average weight average molecular weight selected DB1 / 158748174.5 61 from between about 6 kDa to about 17 kDa includes the steps of: degumming a silk source by adding the silk source to a boiling (100 °C) aqueous solution of sodium carbonate for a treatment time of between about 30 minutes to about 60 minutes; removing sericin from the solution to produce a silk fibroin extract comprising non- detectable levels of sericin; draining the solution from the silk fibroin extract; dissolving the silk fibroin extract in a solution of lithium bromide having a starting temperature upon placement of the silk fibroin extract in the lithium bromide solution that ranges from about 60 °C to about 140 °C; maintaining the solution of silk fibroin- lithium bromide in an oven having a temperature of about 140 °C for a period of at least 1 hour; removing the lithium bromide from the silk fibroin extract; and producing an aqueous solution of silk protein fragments, the aqueous solution comprising: fragments having an average weight average molecular weight selected from between about 6 kDa to about 17 kDa, and a polydispersity of between 1 and about 5, or between about 1.5 and about 3.0. The method may further comprise drying the silk fibroin extract prior to the dissolving step. The aqueous solution of pure silk fibroin protein fragments may comprise lithium bromide residuals of less than 300 ppm as measured using a high-performance liquid chromatography lithium bromide assay . The aqueous solution of pure silk fibroin protein fragments may comprise sodium carbonate residuals of less than 100 ppm as measured using a high- performance liquid chromatography sodium carbonate assay. The method may further comprise adding a therapeutic agent to the aqueous solution of pure silk fibroin protein fragments. The method may further comprise adding a molecule selected from one of an antioxidant or an enzyme to the aqueous solution of pure silk fibroin protein fragments. The method may further comprise adding a vitamin to the aqueous solution of pure silk fibroin protein fragments. The vitamin may be vitamin C or a derivative thereof. The aqueous solution of pure silk fibroin protein fragments may be lyophilized. The method may further comprise adding an alpha hydroxy acid to the aqueous solution of pure silk fibroin protein fragments. The alpha hydroxy acid may be selected from the group consisting of glycolic acid, lactic acid, tartaric acid and citric acid. The method may further comprise adding hyaluronic acid or its salt form at a concentration of about 0.5 % to about 10.0 % to the aqueous solution of pure silk fibroin protein fragments. The method may further comprise adding at least one of zinc oxide or titanium dioxide. A film may be fabricated from the aqueous solution of pure silk fibroin protein fragments produced by this method. The film may comprise DB1 / 158748174.5 62 from about 1.0 wt. % to about 50.0 wt. % of vitamin C or a derivative thereof. The film may have a water content ranging from about 2.0 wt. % to about 20.0 wt. %. The film may comprise from about 30.0 wt. % to about 99.5 wt. % of pure silk fibroin protein fragments. A gel may be fabricated from the aqueous solution of pure silk fibroin protein fragments produced by this method. The gel may comprise from about 0.5 wt. % to about 20.0 wt. % of vitamin C or a derivative thereof. The gel may have a silk content of at least 2 % and a vitamin content of at least 20 %. In some embodiments, a method for preparing an aqueous solution of silk fibroin protein fragments having an average weight average molecular weight selected from between about 17 kDa to about 39 kDa includes the steps of: adding a silk source to a boiling (100 °C) aqueous solution of sodium carbonate for a treatment time of between about 30 minutes to about 60 minutes so as to result in degumming; removing sericin from the solution to produce a silk fibroin extract comprising non- detectable levels of sericin; draining the solution from the silk fibroin extract; dissolving the silk fibroin extract in a solution of lithium bromide having a starting temperature upon placement of the silk fibroin extract in the lithium bromide solution that ranges from about 80 °C to about 140 °C; maintaining the solution of silk fibroin- lithium bromide in a dry oven having a temperature in the range between about 60 °C to about 100 °C for a period of at least 1 hour; removing the lithium bromide from the silk fibroin extract; and producing an aqueous solution of pure silk fibroin protein fragments, wherein the aqueous solution of pure silk fibroin protein fragments comprises lithium bromide residuals of between about 10 ppm and about 300 ppm, wherein the aqueous solution of silk protein fragments comprises sodium carbonate residuals of between about 10 ppm and about 100 ppm, wherein the aqueous solution of pure silk fibroin protein fragments comprises fragments having an average weight average molecular weight selected from between about 17 kDa to about 39 kDa, and a polydispersity of between 1 and about 5, or between about 1.5 and about 3.0. The method may further comprise drying the silk fibroin extract prior to the dissolving step. The aqueous solution of pure silk fibroin protein fragments may comprise lithium bromide residuals of less than 300 ppm as measured using a high-performance liquid chromatography lithium bromide assay. The aqueous solution of pure silk fibroin protein fragments may comprise sodium carbonate residuals of less than 100 ppm as measured using a high-performance liquid chromatography sodium carbonate assay. The method may further comprise adding a therapeutic agent to the aqueous DB1 / 158748174.5 63 solution of pure silk fibroin protein fragments. The method may further comprise adding a molecule selected from one of an antioxidant or an enzyme to the aqueous solution of pure silk fibroin protein fragments. The method may further comprise adding a vitamin to the aqueous solution of pure silk fibroin protein fragments. The vitamin may be vitamin C or a derivative thereof. The aqueous solution of pure silk fibroin protein fragments may be lyophilized. The method may further comprise adding an alpha hydroxy acid to the aqueous solution of pure silk fibroin protein fragments. The alpha hydroxy acid may be selected from the group consisting of glycolic acid, lactic acid, tartaric acid and citric acid. The method may further comprise adding hyaluronic acid or its salt form at a concentration of about 0.5% to about 10.0% to the aqueous solution of pure silk fibroin protein fragments. The method may further comprise adding at least one of zinc oxide or titanium dioxide. A film may be fabricated from the aqueous solution of pure silk fibroin protein fragments produced by this method. The film may comprise from about 1 ,0 wt. % to about 50.0 wt. % of vitamin C or a derivative thereof. The film may have a water content ranging from about 2.0 wt. % to about 20.0 wt. %. The film may comprise from about 30.0 wt. % to about 99.5 wt. % of pure silk fibroin protein fragments. A gel may be fabricated from the aqueous solution of pure silk fibroin protein fragments produced by this method. The gel may comprise from about 0.5 wt. % to about 20.0 wt. % of vitamin C or a derivative thereof. The gel may have a silk content of at least 2% and a vitamin content of at least 20%. In an embodiment, solutions of silk fibroin protein fragments having a weight average molecular weight selected from between about 39 kDa to about 80 kDa are prepared according to the following steps: adding a silk source to a boiling (100 °C) aqueous solution of sodium carbonate for a treatment time of about 30 minutes so as to result in degumming; removing sericin from the solution to produce a silk fibroin extract comprising non-detectable levels of sericin; draining the solution from the silk fibroin extract; dissolving the silk fibroin extract in a solution of lithium bromide having a starting temperature upon placement of the silk fibroin extract in the lithium bromide solution that ranges from about 80 °C to about 140 °C; maintaining the solution of silk fibroin-lithium bromide in a dry oven having a temperature in the range between about 60 °C to about 100 °C for a period of at most 1 hour; removing the lithium bromide from the silk fibroin extract; and producing an aqueous solution of silk fibroin protein fragments, wherein the aqueous solution of silk fibroin protein DB1 / 158748174.5 64 fragments comprises lithium bromide residuals of between about 10 ppm and about 300 ppm, sodium carbonate residuals of between about 10 ppm and about 100 ppm, fragments having a weight average molecular weight selected from between about 39 kDa to about 80 kDa, and a polydispersity of between 1 and about 5, or between about 1.5 and about 3.0. The method may further comprise drying the silk fibroin extract prior to the dissolving step. The aqueous solution of silk fibroin protein fragments may comprise lithium bromide residuals of less than 300 ppm as measured using a high-performance liquid chromatography lithium bromide assay. The aqueous solution of silk fibroin protein fragments may comprise sodium carbonate residuals of less than 100 ppm as measured using a high-performance liquid chromatography sodium carbonate assay. In some embodiments, the method may further comprise adding an active agent (e.g., therapeutic agent) to the aqueous solution of pure silk fibroin protein fragments. The method may further comprise adding an active agent selected from one of an antioxidant or an enzyme to the aqueous solution of pure silk fibroin protein fragments. The method may further comprise adding a vitamin to the aqueous solution of pure silk fibroin protein fragments. The vitamin may be vitamin C or a derivative thereof. The aqueous solution of pure silk fibroin protein fragments may be lyophilized. The method may further comprise adding an alpha-hydroxy acid to the aqueous solution of pure silk fibroin protein fragments. The alpha hydroxy acid may be selected from the group consisting of glycolic acid, lactic acid, tartaric acid and citric acid. The method may further comprise adding hyaluronic acid or its salt form at a concentration of about 0.5% to about 10.0% to the aqueous solution of pure silk fibroin protein fragments. A film may be fabricated from the aqueous solution of pure silk fibroin protein fragments produced by this method. The film may comprise from about 1.0 wt. % to about 50.0 wt. % of vitamin C or a derivative thereof. The film may have a water content ranging from about 2.0 wt. % to about 20.0 wt. %. The film may comprise from about 30.0 wt. % to about 99.5 wt. % of pure silk fibroin protein fragments. A gel may be fabricated from the aqueous solution of pure silk fibroin protein fragments produced by this method. The gel may comprise from about 0.5 wt. % to about 20.0 wt. % of vitamin C or a derivative thereof. The gel may have a silk content of at least 2 wt. % and a vitamin content of at least 20 wt. %. Molecular weight of the silk protein fragments may be controlled based upon the specific parameters utilized during the extraction step, including extraction time and temperature; specific parameters utilized during the dissolution step, including the DB1 / 158748174.5 65 LiBr temperature at the time of submersion of the silk in to the lithium bromide and time that the solution is maintained at specific temperatures; and specific parameters utilized during the filtration step. By controlling process parameters using the disclosed methods, it is possible to create SPF mixture solutions with polydispersity equal to or lower than 2.5 at a variety of different molecular weight ranging from 1 kDa to 250 kDa, 5 kDa to 200 kDa, 5 kDa to 150 kDa, 10 kDa to 150 kDa, or 10 kDa to 80 kDa. By altering process parameters to achieve silk solutions with different molecular weights, a range of fragment mixture end products, with desired polydispersity of equal to or less than 2.5 may be targeted based upon the desired performance requirements. For example, a lower molecular weight silk film containing a drug may have a faster release rate compared to a higher molecular weight SPF preparation. Additionally, SPF mixture solutions with a polydispersity of greater than 2.5 can be achieved. Further, two solutions with different average molecular weights and polydispersities can be mixed to create combination solutions. Alternatively, a liquid silk gland (100% sericin free silk protein) that has been removed directly from a worm could be used in combination with any of the SPF mixture solutions of the present disclosure. Molecular weight of the pure silk fibroin- based protein fragment composition was determined using High Pressure Liquid Chromatography (HPLC) with a Refractive Index Detector (RID). Polydispersity was calculated using Cirrus GPC Online GPC / SEC Software Version 3.3 (Agilent). Differences in the processing parameters can result in regenerated silk fibroins that vary in molecular weight, and peptide chain size distribution (polydispersity, PD). This, in turn, influences the regenerated silk fibroin performance, including mechanical strength, water solubility etc. Parameters were varied during the processing of raw silk cocoons into the silk solution. Varying these parameters affected the MW of the resulting silk solution. Parameters manipulated included (i) time and temperature of extraction, (ii) temperature of LiBr, (iii) temperature of dissolution oven, and (iv) dissolution time. Molecular weight was determined with mass spec as shown in Figs.74-90. Experiments were carried out to determine the effect of varying the extraction time. Figs.74-90 are graphs showing these results and Tables A-G summarize the results. Below is a summary: – A sericin extraction time of 30 minutes resulted in larger molecular weight than a sericin extraction time of 60 minutes DB1 / 158748174.5 66 – Molecular weight decreases with time in the oven – 140 °C LiBr and oven resulted in the low end of the confidence interval to be below a molecular weight of 9500 Da – 30 min extraction at the 1 hour and 4 hour time points have undigested silk – 30 min extraction at the 1 hour time point resulted in a significantly high molecular weight with the low end of the confidence interval being 35,000 Da – The range of molecular weight reached for the high end of the confidence interval was 18000 to 216000 Da (important for offering solutions with specified upper limit). DB1 / 158748174.5 67 e 2.63 2.66 , 80 PD .40 .61 , 80 e D 10 56 59 59 r) DB1 / 158748174.5 68 D 00865 2358 1749 0298 r) Experiments were carried out to determine the effect of varying the extraction temperature. Fig.74 is a graph showing these results and Table H summarizes the results. Below is a summary: – Sericin extraction at 90 °C resulted in higher MW than sericin extraction at 100 °C extraction – Both 90 °C and 100 °C show decreasing MW over time in the oven. f silk iBr) DB1 / 158748174.5 69 Experiments were carried out to determine the effect of varying the Lithium Bromide (LiBr) temperature when added to silk. Figs.82-83 are graphs showing these results and Tables I-J summarize the results. Below is a summary: – No impact on molecular weight or confidence interval (all CI ~10500-6500 Da) – Studies illustrated that the temperature of LiBr-silk dissolution, as LiBr is added and begins dissolving, rapidly drops below the original LiBr temperature due to the majority of the mass being silk at room temperature ht of eight n DB1 / 158748174.5 70 2.89 3.10 2.42 2.59 2.89 Experiments were carried out to determine the effect of oven / dissolution temperature. Figs.84-88 are graphs showing these results and Tables K-O summarize the results. Below is a summary: – Oven temperature has less of an effect on 60 min extracted silk than 30 min extracted silk. Without wishing to be bound by theory, it is believed that the 30 min silk is less degraded during extraction and therefore the oven temperature has more of an effect on the larger MW, less degraded portion of the silk. – For 60 °C vs.140 °C oven the 30 min extracted silk showed a very significant effect of lower MW at higher oven temp, while 60 min extracted silk had an effect but much less – The 140 °C oven resulted in a low end in the confidence interval at ~6000 Da. silk on DB1 / 158748174.5 71 2 7 9 0 silk on D 60 71 62 38 46 08 f silk on D 69 14 DB1 / 158748174.5 72 silk on D 87 01 37 17 silk on D 56 47 59 61 In an embodiment, the methods disclosed herein result in a solution with characteristics that can be controlled during manufacturing, including, but not limited to: MW – may be varied by changing extraction and / or dissolution time and temp (e.g., LiBr temperature), pressure, and filtration (e.g., size exclusion chromatography); Structure – removal or cleavage of heavy or light chain of the fibroin protein polymer; Purity – hot water rinse temperature for improved sericin removal or filter capability for improved particulate removal that adversely affects shelf stability of the silk fragment protein mixture solution; Color – the color of the solution can be controlled with, for example, LiBr temp and time; Viscosity; Clarity; and Stability of solution. The resultant pH of the solution is typically about 7 and can be altered using an acid or base as appropriate to storage requirements. DB1 / 158748174.5 73 The raw silk cocoons from the silkworm Bombyx mori was cut into pieces. The pieces of raw silk cocoons were boiled in an aqueous solution of Na2CO3 (about 100 °C) for a period of time between about 30 minutes to about 60 minutes to remove sericin (degumming). The volume of the water used equals about 0.4 x raw silk weight and the amount of Na2CO3 is about 0.848 x the weight of the raw silk cocoon pieces. The resulting degummed silk cocoon pieces were rinsed with deionized water three times at about 60 °C (20 minutes per rinse). The volume of rinse water for each cycle was 0.2 L x the weight of the raw silk cocoon pieces. The excess water from the degummed silk cocoon pieces was removed. After the DI water washing step, the wet degummed silk cocoon pieces were dried at room temperature. The degummed silk cocoon pieces were mixed with a LiBr solution, and the mixture was heated to about 100 °C. The warmed mixture was placed in a dry oven and was heated at a temperature ranging from about 60 °C to about 140 °C for about 60 minutes to achieve complete dissolution of the native silk protein. The resulting solution was allowed to cool to room temperature and then was dialyzed to remove LiBr salts using a 3,500 Da MWCO membrane. Multiple exchanges were performed in Di water until Br−ions were less than 1 ppm as determined in the hydrolyzed fibroin solution read on an Oakton Bromide (Br−) double-junction ion-selective electrode. The resulting silk fibroin aqueous solution has a concentration of about 8.0 % w / v containing pure silk fibroin protein fragments having an average weight average molecular weight selected from between about 6 kDa to about 16 kDa, about 17 kDa to about 39 kDa, and about 39 kDa to about 80 kDa and a polydispersity of between about 1.5 and about 3.0. The 8.0 % w / v was diluted with DI water to provide a 1.0 % w / v, 2.0 % w / v, 3.0 % w / v, 4.0 % w / v, 5.0 % w / v by the coating solution. A variety of % silk concentrations have been produced through the use of Tangential Flow Filtration (TFF). In all cases a 1 % silk solution was used as the input feed. A range of 750-18,000 mL of 1% silk solution was used as the starting volume. Solution is diafiltered in the TFF to remove lithium bromide. Once below a specified level of residual LiBr, solution undergoes ultrafiltration to increase the concentration through removal of water. See examples below. Six (6) silk solutions were utilized in standard silk structures with the following results: Solution #1 is a silk concentration of 5.9 wt. %, average MW of 19.8 kDa and 2.2 PDI (made with a 60 min boil extraction, 100 °C LiBr dissolution for 1 hour). DB1 / 158748174.5 74 Solution #2 is a silk concentration of 6.4 wt. % (made with a 30 min boil extraction, 60 °C LiBr dissolution for 4 hrs). Solution #3 is a silk concentration of 6.17 wt. % (made with a 30 min boil extraction 100 °C LiBr dissolution for 1 hour). Solution #4 is a silk concentration of 7.30 wt. %: A 7.30 % silk solution was produced beginning with 30 minute extraction batches of 100 g silk cocoons per batch. Extracted silk fibers were then dissolved using 100 °C 9.3 M LiBr in a 100 °C oven for 1 hour. 100 g of silk fibers were dissolved per batch to create 20% silk in LiBr. Dissolved silk in LiBr was then diluted to 1% silk and filtered through a 5 µm filter to remove large debris.15,500 mL of 1 %, filtered silk solution was used as the starting volume / diafiltration volume for TFF. Once LiBr was removed, the solution was ultrafiltered to a volume around 1300 mL.1262 mL of 7.30 % silk was then collected. Water was added to the feed to help remove the remaining solution and 547 mL of 3.91 % silk was then collected. Solution #5 is a silk concentration of 6.44 wt. %: A 6.44 wt. % silk solution was produced beginning with 60 minute extraction batches of a mix of 25, 33, 50, 75 and 100 g silk cocoons per batch. Extracted silk fibers were then dissolved using 100 °C 9.3 M LiBr in a 100 °C oven for 1 hour. 35, 42, 50 and 71 g per batch of silk fibers were dissolved to create 20 % silk in LiBr and combined. Dissolved silk in LiBr was then diluted to 1 % silk and filtered through a 5 µm filter to remove large debris. 17,000 mL of 1 %, filtered silk solution was used as the starting volume / diafiltration volume for TFF. Once LiBr was removed, the solution was ultrafiltered to a volume around 3000 mL.1490 mL of 6.44 % silk was then collected. Water was added to the feed to help remove the remaining solution and 1454 mL of 4.88 % silk was then collected. Solution #6 is a silk concentration of 2.70 wt. %: A 2.70 % silk solution was produced beginning with 60-minute extraction batches of 25 g silk cocoons per batch. Extracted silk fibers were then dissolved using 100 °C 9.3 M LiBr in a 100 °C oven for 1 hour. 35.48 g of silk fibers were dissolved per batch to create 20 % silk in LiBr. Dissolved silk in LiBr was then diluted to 1% silk and filtered through a 5 µm filter to remove large debris.1000 mL of 1%, filtered silk solution was used as the starting volume / diafiltration volume for TFF. Once LiBr was removed, the solution was ultrafiltered to a volume around 300 mL.312 mL of 2.7 % silk was then collected. DB1 / 158748174.5 75 The preparation of silk fibroin solutions with higher molecular weights is given in Table O. Table O. Preparation and properties of silk fibroin solutions. ersity Silk aqueous coating composition for application to fabrics are given in Tables P and Q below. .5% DB1 / 158748174.5 76 .5% Three (3) silk solutions were utilized in film making with the following results: Solution #1 is a silk concentration of 5.9 %, average MW of 19.8 kDa and 2.2 PD (made with a 60 min boil extraction, 100 °C LiBr dissolution for 1 hr). Solution #2 is a silk concentration of 6.4 % (made with a 30 min boil extraction, 60 °C LiBr dissolution for 4 hrs). Solution #3 is a silk concentration of 6.17 % (made with a 30 min boil extraction, 100 °C LiBr dissolution for 1 hour). Films were made in accordance with Rockwood et al. (Nature Protocols; Vol. 6; No.10; published on-line Sep.22, 2011; doi:10.1038 / nprot.2011.379).4 mL of 1% or 2% (wt / vol) aqueous silk solution was added into 100 mm Petri dish (Volume of silk can be varied for thicker or thinner films and is not critical) and allowed to dry overnight uncovered. The bottom of a vacuum desiccator was filled with water. Dry films were placed in the desiccator and vacuum applied, allowing the films to water DB1 / 158748174.5 77 anneal for 4 hours prior to removal from the dish. Films cast from solution #1 did not result in a structurally continuous film; the film was cracked in several pieces. These pieces of film dissolved in water in spite of the water annealing treatment. Silk solutions of various molecular weights and / or combinations of molecular weights can be optimized for gel applications. The following provides an example of this process but it not intended to be limiting in application or formulation. Three (3) silk solutions were utilized in gel making with the following results: Solution #1 is a silk concentration of 5.9 %, average MW of 19.8 kDa and 2.2 PD (made with a 60 min boil extraction, 100 °C LiBr dissolution for 1 hr). Solution #2 is a silk concentration of 6.4 % (made with a 30 min boil extraction, 60 °C LiBr dissolution for 4 hrs). Solution #3 is a silk concentration of 6.17 % (made with a 30 min boil extraction, 100 °C LiBr dissolution for 1 hour). “Egel” is an electrogelation process as described in Rockwood of al. Briefly, 10 ml of aqueous silk solution is added to a 50 ml conical tube and a pair of platinum wire electrodes immersed into the silk solution. A 20 volt potential was applied to the platinum electrodes for 5 minutes, the power supply turned off and the gel collected. Solution #1 did not form an EGEL over the 5 minutes of applied electric current. Solutions #2 and #3 were gelled in accordance with the published horseradish peroxidase (HRP) protocol. Behavior seemed typical of published solutions. Materials and Methods: the following equipment and material are used in determination of Silk Molecular weight: Agilent 1100 with chemstation software ver. 10.01; Refractive Index Detector (RID); analytical balance; volumetric flasks (1000 mL, 10 mL and 5 mL); HPLC grade water; ACS grade sodium chloride; ACS grade sodium phosphate dibasic heptahydrate; phosphoric acid; dextran MW Standards- Nominal Molecular Weights of 5 kDa, 11.6 kDa, 23.8 kDa, 48.6 kDa, and 148 kDa; 50 mL PET or polypropylene disposable centrifuge tubes; graduated pipettes; amber glass HPLC vials with Teflon caps; Phenomenex PolySep GFC P-4000 column (size: 7.8 mm x 300 mm). Procedural Steps: A) Preparation of 1 L Mobile Phase (0.1 M Sodium Chloride solution in 0.0125 M Sodium phosphate buffer) DB1 / 158748174.5 78 Take a 250 mL clean and dry beaker, place it on the balance and tare the weight. Add about 3.3509 g of sodium phosphate dibasic heptahydrate to the beaker. Note down the exact weight of sodium phosphate dibasic weighed. Dissolve the weighed sodium phosphate by adding 100 mL of HPLC water into the beaker. Take care not to spill any of the content of the beaker. Transfer the solution carefully into a clean and dry 1000 mL volumetric flask. Rinse the beaker and transfer the rinse into the volumetric flask. Repeat the rinse 4-5 times. In a separate clean and dry 250 mL beaker weigh exactly about 5.8440 g of sodium chloride. Dissolve the weighed sodium chloride in 50 mL of water and transfer the solution to the sodium phosphate solution in the volumetric flask. Rinse the beaker and transfer the rinse into the volumetric flask. Adjust the pH of the solution to 7.0 ± 0.2 with phosphoric acid. Make up the volume in volumetric flask with HPLC water to 1000 mL and shake it vigorously to homogeneously mix the solution. Filter the solution through 0.45 µm polyamide membrane filter. Transfer the solution to a clean and dry solvent bottle and label the bottle. The volume of the solution can be varied to the requirement by correspondingly varying the amount of sodium phosphate dibasic heptahydrate and sodium chloride. B) Preparation of Dextran Molecular Weight Standard solutions At least five different molecular weight standards are used for each batch of samples that are run so that the expected value of the sample to be tested is bracketed by the value of the standard used. Label six 20 mL scintillation glass vials respective to the molecular weight standards. Weigh accurately about 5 mg of each of dextran molecular weight standards and record the weights. Dissolve the dextran molecular weight standards in 5 mL of mobile phase to make a 1 mg / mL standard solution. C) Preparation of Sample Solutions When preparing sample solutions, if there are limitations on how much sample is available, the preparations may be scaled as long as the ratios are maintained. Depending on sample type and silk protein content in sample weigh enough sample in a 50 mL disposable centrifuge tube on an analytical balance to make a 1 mg / mL sample solution for analysis. Dissolve the sample in equivalent volume of mobile phase make a 1 mg / mL solution. Tightly cap the tubes and mix the samples (in solution). Leave the sample solution for 30 minutes at room temperature. Gently mix the sample solution again for 1 minute and centrifuge at 4000 RPM for 10 minutes. D) HPLC analysis of the samples DB1 / 158748174.5 79 Transfer 1.0 mL of all the standards and sample solutions into individual HPLC vials. Inject the molecular weight standards (one injection each) and each sample in duplicate. Analyze all the standards and sample solutions using the following HPLC conditions: Data analysis and calculations – Calculation of Average Molecular Weight using Cirrus Software Upload the chromatography data files of the standards and the analytical samples into Cirrus SEC data collection and molecular weight analysis software. Calculate the weight average molecular weight (Mw), number average molecular weight (Mn), peak average molecular weight (Mp), and polydispersity for each injection of the sample. Spider Silk Fragments Spider silks are natural polymers that consist of three domains: a repetitive middle core domain that dominates the protein chain, and non-repetitive N-terminal and C-terminal domains. The large core domain is organized in a block copolymer- like arrangement, in which two basic sequences, crystalline [poly(A) or poly(GA)] and less crystalline (GGX or GPGXX (SEQ ID NO: 6)) polypeptides alternate. Dragline silk is the protein complex composed of major ampullate dragline silk protein 1 (MaSp1) and major ampullate dragline silk protein 2 (MaSp2). Both silks are approximately 3500 amino acid long. MaSp1 can be found in the fibre core and the periphery, whereas MaSp2 forms clusters in certain core areas. The large central DB1 / 158748174.5 80 domains of MaSp1 and MaSp2 are organized in block copolymer-like arrangements, in which two basic sequences, crystalline [poly(A) or poly(GA)] and less crystalline (GGX or GPGXX (SEQ ID NO: 6)) polypeptides alternate in core domain. Specific secondary structures have been assigned to poly(A) / (GA), GGX and GPGXX (SEQ ID NO: 6) motifs including β-sheet, α-helix and β-spiral respectively. The primary sequence, composition and secondary structural elements of the repetitive core domain are responsible for mechanical properties of spider silks; whereas, non- repetitive N- and C-terminal domains are essential for the storage of liquid silk dope in a lumen and fibre formation in a spinning duct. The main difference between MaSp1 and MaSp2 is the presence of proline (P) residues accounting for 15% of the total amino acid content in MaSp2, whereas MaSp1 is proline-free. By calculating the number of proline residues in N. clavipes dragline silk, it is possible to estimate the presence of the two proteins in fibres; 81% MaSp1 and 19% MaSp2. Different spiders have different ratios of MaSp1 and MaSp2. For example, a dragline silk fibre from the orb weaver Argiope aurantia contains 41% MaSp1 and 59% MaSp2. Such changes in the ratios of major ampullate silks can dictate the performance of the silk fibre. At least seven different types of silk proteins are known for one orb-weaver species of spider. Silks differ in primary sequence, physical properties and functions. For example, dragline silks used to build frames, radii and lifelines are known for outstanding mechanical properties including strength, toughness and elasticity. On an equal weight basis, spider silk has a higher toughness than steel and Kevlar. Flageliform silk found in capture spirals has extensibility of up to 500%. Minor ampullate silk, which is found in auxiliary spirals of the orb-web and in prey wrapping, possesses high toughness and strength almost similar to major ampullate silks, but does not supercontract in water. Spider silks are known for their high tensile strength and toughness. The recombinant silk proteins also confer advantageous properties to cosmetic or dermatological compositions, in particular to be able to improve the hydrating or softening action, good film forming property and low surface density. Diverse and unique biomechanical properties together with biocompatibility and a slow rate of degradation make spider silks excellent candidates as biomaterials for tissue engineering, guided tissue repair and drug delivery, for cosmetic products (e.g. nail DB1 / 158748174.5 81 and hair strengthener, skin care products), and industrial materials (e.g. nanowires, nanofibers, surface coatings). In an embodiment, a silk protein may include a polypeptide derived from natural spider silk proteins. The polypeptide is not limited particularly as long as it is derived from natural spider silk proteins, and examples of the polypeptide include natural spider silk proteins and recombinant spider silk proteins such as variants, analogs, derivatives or the like of the natural spider silk proteins. In terms of excellent tenacity, the polypeptide may be derived from major dragline silk proteins produced in major ampullate glands of spiders. Examples of the major dragline silk proteins include major ampullate spidroin MaSp1 and MaSp2 from Nephila clavipes, and ADF3 and ADF4 from Araneus diadematus, etc. Examples of the polypeptide derived from major dragline silk proteins include variants, analogs, derivatives or the like of the major dragline silk proteins. Further, the polypeptide may be derived from flagelliform silk proteins produced in flagelliform glands of spiders. Examples of the flagelliform silk proteins include flagelliform silk proteins derived from Nephila clavipes, etc. Examples of the polypeptide derived from major dragline silk proteins include a polypeptide containing two or more units of an amino acid sequence represented by the formula 1: REP1-REP2 (1), preferably a polypeptide containing five or more units thereof, and more preferably a polypeptide containing ten or more units thereof. Alternatively, the polypeptide derived from major dragline silk proteins may be a polypeptide that contains units of the amino acid sequence represented by the formula 1: REP1-REP2 (1) and that has, at a C-terminal, an amino acid sequence represented by any of SEQ ID NOS: 52 to 54, which is also described in U.S. Patent No. 9,051,453, which is incorporated by reference herein in its entirety, or an amino acid sequence having a homology of 90% or more with the amino acid sequence represented by any of SEQ ID NOS: 52 to 54, which is also described in U.S. Patent No.9,051,453, which is incorporated by reference herein in its entirety. In the polypeptide derived from major dragline silk proteins, units of the amino acid sequence represented by the formula 1: REP1-REP2 (1) may be the same or may be different from each other. In the case of producing a recombinant protein using a microbe such as Escherichia coli as a host, the molecular weight of the polypeptide derived from major dragline silk proteins is 500 kDa or less, or 300 kDa or less, or 200 kDa or less, in terms of productivity. DB1 / 158748174.5 82 In the formula (1), the REP1 indicates polyalanine. In the REP1, the number of alanine residues arranged in succession is preferably 2 or more, more preferably 3 or more, further preferably 4 or more, and particularly preferably 5 or more. Further, in the REP1, the number of alanine residues arranged in succession is preferably 20 or less, more preferably 16 or less, further preferably 12 or less, and particularly preferably 10 or less. In the formula (1), the REP2 is an amino acid sequence composed of 10 to 200 amino acid residues. The total number of glycine, serine, glutamine and alanine residues contained in the amino acid sequence is 40% or more, preferably 60% or more, and more preferably 70% or more with respect to the total number of amino acid residues contained therein. In the major dragline silk, the REP1 corresponds to a crystal region in a fiber where a crystal β sheet is formed, and the REP2 corresponds to an amorphous region in a fiber where most of the parts lack regular configurations and that has more flexibility. Further, the [REP1-REP2] corresponds to a repetitious region (repetitive sequence) composed of the crystal region and the amorphous region, which is a characteristic sequence of dragline silk proteins. Recombinant Silk Fragments In some embodiments, the recombinant silk protein refers to recombinant spider silk polypeptides, recombinant insect silk polypeptides, or recombinant mussel silk polypeptides. In some embodiments, the recombinant silk protein fragment disclosed herein include recombinant spider silk polypeptides of Araneidae or Araneoids, or recombinant insect silk polypeptides of Bombyx mori. In some embodiments, the recombinant silk protein fragment disclosed herein include recombinant spider silk polypeptides of Araneidae or Araneoids. In some embodiments, the recombinant silk protein fragment disclosed herein include block copolymer having repetitive units derived from natural spider silk polypeptides of Araneidae or Araneoids. In some embodiments, the recombinant silk protein fragment disclosed herein include block copolymer having synthetic repetitive units derived from spider silk polypeptides of Araneidae or Araneoids and non-repetitive units derived from natural repetitive units of spider silk polypeptides of Araneidae or Araneoids. Recent advances in genetic engineering have provided a route to produce various types of recombinant silk proteins. Recombinant DNA technology has been DB1 / 158748174.5 83 used to provide a more practical source of silk proteins. As used herein “recombinant silk protein” refers to synthetic proteins produced heterologously in prokaryotic or eukaryotic expression systems using genetic engineering methods. Various methods for synthesizing recombinant silk peptides are known and have been described by Ausubel et al., Current Protocols in Molecular Biology § 8 (John Wiley & Sons 1987, (1990)), incorporated herein by reference. A gram- negative, rod-shaped bacterium E. coli is a well-established host for industrial scale production of proteins. Therefore, the majority of recombinant silks have been produced in E. coli. E. coli which is easy to manipulate, has a short generation time, is relatively low cost and can be scaled up for larger amounts protein production. The recombinant silk proteins can be produced by transformed prokaryotic or eukaryotic systems containing the cDNA coding for a silk protein, for a fragment of this protein or for an analog of such a protein. The recombinant DNA approach enables the production of recombinant silks with programmed sequences, secondary structures, architectures and precise molecular weight. There are four main steps in the process: (i) design and assembly of synthetic silk-like genes into genetic ‘cassettes’, (ii) insertion of this segment into a DNA recombinant vector, (iii) transformation of this recombinant DNA molecule into a host cell and (iv) expression and purification of the selected clones. The term “recombinant vectors”, as used herein, includes any vectors known to the skilled person including plasmid vectors, cosmid vectors, phage vectors such as lambda phage, viral vectors such as adenoviral or baculoviral vectors, or artificial chromosome vectors such as bacterial artificial chromosomes (BAC), yeast artificial chromosomes (YAC), or P1 artificial chromosomes (PAC). Said vectors include expression as well as cloning vectors. Expression vectors comprise plasmids as well as viral vectors and generally contain a desired coding sequence and appropriate DNA sequences necessary for the expression of the operably linked coding sequence in a particular host organism (e.g., bacteria, yeast, or plant) or in in vitro expression systems. Cloning vectors are generally used to engineer and amplify a certain desired DNA fragment and may lack functional sequences needed for expression of the desired DNA fragments. The prokaryotic systems include Gram-negative bacteria or Gram-positive bacteria. The prokaryotic expression vectors can include an origin of replication which can be recognized by the host organism, a homologous or heterologous DB1 / 158748174.5 84 promoter which is functional in the said host, the DNA sequence coding for the spider silk protein, for a fragment of this protein or for an analogous protein. Nonlimiting examples of prokaryotic expression organisms are Escherichia coli, Bacillus subtilis, Bacillus megaterium, Corynebacterium glutamicum, Anabaena, Caulobacter, Gluconobacter, Rhodobacter, Pseudomonas, Para coccus, Bacillus (e.g. Bacillus subtilis) Brevibacterium, Corynebacterium, Rhizobium (Sinorhizobium), Flavobacterium, Klebsiella, Enterobacter, Lactobacillus, Lactococcus, Methylobacterium, Propionibacterium, Staphylococcus or Streptomyces cells. The eukaryotic systems include yeasts and insect, mammalian or plant cells. In this case, the expression vectors can include a yeast plasmid origin of replication or an autonomous replication sequence, a promoter, a DNA sequence coding for a spider silk protein, for a fragment or for an analogous protein, a polyadenylation sequence, a transcription termination site and, lastly, a selection gene. Nonlimiting examples of eukaryotic expression organisms include yeasts, such as Saccharomyces cerevisiae, Pichia pastoris, basidiosporogenous, ascosporogenous, filamentous fungi, such as Aspergillus niger, Aspergillus oryzae, Aspergillus nidulans, Trichoderma reesei, Acremonium chrysogenum, Candida, Hansenula, Kluyveromyces, Saccharomyces (e.g. Saccharomyces cerevisiae), Schizosaccharomyces, Pichia (e.g. Pichia pastoris) or Yarrowia cells etc., mammalian cells, such as HeLa cells, COS cells, CHO cells etc., insect cells, such as Sf9 cells, MEL cells, etc., “insect host cells” such as Spodoptera frugiperda or Trichoplusia ni cells. SF9 cells, SF-21 cells or High-Five cells, wherein SF-9 and SF-21 are ovarian cells from Spodoptera frugiperda, and High-Five cells are egg cells from Trichoplusia ni., “plant host cells”, such as tobacco, potato or pea cells. A variety of heterologous host systems have been explored to produce different types of recombinant silks. Recombinant partial spidroins as well as engineered silks have been cloned and expressed in bacteria (Escherichia coli), yeast (Pichia pastoris), insects (silkworm larvae), plants (tobacco, soybean, potato, Arabidopsis), mammalian cell lines (BHT / hamster) and transgenic animals (mice, goats). Most of the silk proteins are produced with an N- or C-terminal His-tags to make purification simple and produce enough amounts of the protein. In some embodiments, the host suitable for expressing the recombinant spider silk protein using heterogeneous system may include transgenic animals and plants. In some embodiments, the host suitable for expressing the recombinant spider silk DB1 / 158748174.5 85 protein using heterogeneous system comprises bacteria, yeasts, mammalian cell lines. In some embodiments, the host suitable for expressing the recombinant spider silk protein using heterogeneous system comprises E. coli. In some embodiments, the host suitable for expressing the recombinant spider silk protein using heterogeneous system comprises transgenic B. mori silkworm generated using genome editing technologies (e.g. CRISPR). The recombinant silk protein in this disclosure comprises synthetic proteins which are based on repeat units of natural silk proteins. Besides the synthetic repetitive silk protein sequences, these can additionally comprise one or more natural nonrepetitive silk protein sequences. In some embodiments, “recombinant silk protein” refers to recombinant silkworm silk protein or fragments thereof. The recombinant production of silk fibroin and silk sericin has been reported. A variety of hosts are used for the production including E. coli, Sacchromyces cerevisiae, Pseudomonas sp., Rhodopseudomonas sp., Bacillus sp., and Strepomyces. See EP 0230702, which is incorporate by reference herein by its entirety. Provided herein also include design and biological-synthesis of silk fibroin protein-like multiblock polymer comprising GAGAGX (SEQ ID NO: 1) hexapeptide (X is A, Y, V or S) derived from the repetitive domain of B. mori silk heavy chain (H chain) In some embodiments, this disclosure provides silk protein-like multiblock polymers derived from the repetitive domain of B. mori silk heavy chain (H chain) comprising the GAGAGS (SEQ ID NO: 2) hexapeptide repeating units. The GAGAGS (SEQ ID NO: 2) hexapeptide is the core unit of H-chain and plays an important role in the formation of crystalline domains. The silk protein-like multiblock polymers containing the GAGAGS (SEQ ID NO: 2) hexapeptide repeating units spontaneously aggregate into β-sheet structures, similar to natural silk fibroin protein, where in the silk protein-like multiblock polymers having any weight average molecular weight described herein. In some embodiments, this disclosure provides silk-peptide like multiblock copolymers composed of the GAGAGS (SEQ ID NO: 2) hexapeptide repetitive fragment derived from H chain of B. mori silk heavy chain and mammalian elastin VPGVG (SEQ ID NO: 3) motif produced by E. coli. In some embodiments, this disclosure provides fusion silk fibroin proteins composed of the GAGAGS (SEQ ID DB1 / 158748174.5 86 NO: 2) hexapeptide repetitive fragment derived from H chain of B. mori silk heavy chain and GVGVP (SEQ ID NO: 4) produced by E. coli, where in the silk protein-like multiblock polymers having any weight average molecular weight described herein. In some embodiments, this disclosure provides B. mori silkworm recombinant proteins composed of the (GAGAGS)16 (SEQ ID NO: 55) repetitive fragment. In some embodiments, this disclosure provides recombinant proteins composed of the (GAGAGS)16(SEQ ID NO: 55) repetitive fragment and the non-repetitive (GAGAGS)16 –F-COOH (SEQ ID NO: 56), (GAGAGS)16 –F-F-COOH (SEQ ID NO: 57), (GAGAGS)16–F-F-F-COOH (SEQ ID NO: 58), (GAGAGS)16–F-F-F-F-COOH (SEQ ID NO: 59), (GAGAGS)16–F-F-F-F-F-F-F-F-COOH (SEQ ID NO: 60), (GAGAGS)16 –F-F-F-F–F-F-F-F-F-F-F-F-COOH (SEQ ID NO: 61) produced by E. coli, where F has the following amino acid sequence SGFGPVANGGSGEASSESDFGSSGFGPVANASSGEASSESDFAG (SEQ ID NO: 5), and where in the silk protein-like multiblock polymers having any weight average molecular weight described herein. In some embodiments, “recombinant silk protein” refers to recombinant spider silk protein or fragments thereof. The productions of recombinant spider silk proteins based on a partial cDNA clone have been reported. The recombinant spider silk proteins produced as such comprise a portion of the repetitive sequence derived from a dragline spider silk protein, Spidroin 1, from the spider Nephila clavipes. see Xu et al. (Proc. Natl. Acad. Sci. U.S.A., 87:7120–7124 (1990). cDNA clone encoding a portion of the repeating sequence of a second fibroin protein, Spidroin 2, from dragline silk of Nephila clavipes and the recombinant synthesis thereof is described in J. Biol. Chem., 1992, volume 267, pp.19320–19324. The recombinant synthesis of spider silk proteins including protein fragments and variants of Nephila clavipes from transformed E. coli is described in U.S. Pat. Nos.5,728,810 and 5,989,894. cDNA clones encoding minor ampullate spider silk proteins and the expression thereof is described in U.S. Pat. Nos.5,733,771 and 5,756,677. cDNA clone encoding the flagelliform silk protein from an orb-web spinning spider is described in U.S. Pat. No. 5,994,099. U.S. Pat. No.6,268,169 describes the recombinant synthesis of spider silk like proteins derived from the repeating peptide sequence found in the natural spider dragline of Nephila clavipes by E. coli, Bacillus subtilis, and Pichia pastoris recombinant expression systems. WO 03 / 020916 describes the cDNA clone encoding and recombinant production of spider spider silk proteins having repeative sequences DB1 / 158748174.5 87 derived from the major ampullate glands of Nephila madagascariensis, Nephila senegalensis, Tetragnatha kauaiensis, Tetragnatha versicolor, Argiope aurantia, Argiope trifasciata, Gasteracantha mammosa, and Latrodectus geometricus, the flagelliform glands of Argiope trifasciata, the ampullate glands of Dolomedes tenebrosus, two sets of silk glands from Plectreurys tristis, and the silk glands of the mygalomorph Euagrus chisoseus. Each of the above reference is incorporated herein by reference in its entirety. In some embodiments, the recombinant spider silk protein is a hybrid protein of a spider silk protein and an insect silk protein, a spider silk protein and collagen, a spider silk protein and resilin, or a spider silk protein and keratin. The spider silk repetitive unit comprises or consists of an amino acid sequence of a region that comprises or consists of at least one peptide motif that repetitively occurs within a naturally occurring major ampullate gland polypeptide, such as a dragline spider silk polypeptide, a minor ampullate gland polypeptide, a flagelliform polypeptide, an aggregate spider silk polypeptide, an aciniform spider silk polypeptide or a pyriform spider silk polypeptide. In some embodiments, the recombinant spider silk protein in this disclosure comprises synthetic spider silk proteins derived from repetitive units of natural spider silk proteins, consensus sequence, and optionally one or more natural non-repetitive spider silk protein sequences. The repeated units of natural spider silk polypeptide may include dragline spider silk polypeptides or flagelliform spider silk polypeptides of Araneidae or Araneoids. As used herein, the spider silk “repetitive unit” comprises or consists of at least one peptide motif that repetitively occurs within a naturally occurring major ampullate gland polypeptide, such as a dragline spider silk polypeptide, a minor ampullate gland polypeptide, a flagelliform polypeptide, an aggregate spider silk polypeptide, an aciniform spider silk polypeptide or a pyriform spider silk polypeptide. A “repetitive unit” refers to a region which corresponds in amino acid sequence to a region that comprises or consists of at least one peptide motif (e.g. AAAAAA (SEQ ID NO: 20)) or GPGQQ (SEQ ID NO: 15)) that repetitively occurs within a naturally occurring silk polypeptide (e.g. MaSpI, ADF-3, ADF-4, or Flag) (i.e. identical amino acid sequence) or to an amino acid sequence substantially similar thereto (i.e. variational amino acid sequence). A “repetitive unit” having an amino acid sequence which is “substantially similar” to a corresponding amino acid DB1 / 158748174.5 88 sequence within a naturally occurring silk polypeptide (i.e. wild-type repetitive unit) is also similar with respect to its properties, e.g. a silk protein comprising the “substantially similar repetitive unit” is still insoluble and retains its insolubility. A “repetitive unit” having an amino acid sequence which is “identical” to the amino acid sequence of a naturally occurring silk polypeptide, for example, can be a portion of a silk polypeptide corresponding to one or more peptide motifs of MaSpI (SEQ ID NO: 48), MaSpII (SEQ ID NO: 49), ADF-3 (SEQ ID NO: 50) and / or ADF-4 (SEQ ID NO: 51). A “repetitive unit” having an amino acid sequence which is “substantially similar” to the amino acid sequence of a naturally occurring silk polypeptide, for example, can be a portion of a silk polypeptide corresponding to one or more peptide motifs of MaSpI (SEQ ID NO: 48), MaSpII (SEQ ID NO: 49), ADF-3 (SEQ ID NO: 50) and / or ADF-4 (SEQ ID NO: 51)but having one or more amino acid substitution at specific amino acid positions. As used herein, the term “consensus peptide sequence” refers to an amino acid sequence which contains amino acids which frequently occur in a certain position (e.g. “G”) and wherein, other amino acids which are not further determined are replaced by the place holder “X”. In some embodiments, the consensus sequence is at least one of (i) GPGXX (SEQ ID NO: 6), wherein X is an amino acid selected from A, S, G, Y, P and Q; (ii) GGX, wherein X is an amino acid selected from Y, P, R, S, A, T, N and Q, preferably Y, P and Q; (iii) Ax, wherein x is an integer from 5 to 10. The consensus peptide sequences GPGXX (SEQ ID NO: 6) and GGX, i.e. glycine rich motifs, provide flexibility to the silk polypeptide and thus, to the thread formed from the silk protein containing said motifs. In detail, the iterated GPGXX (SEQ ID NO: 6) motif forms turn spiral structures, which imparts elasticity to the silk polypeptide. Major ampullate and flagelliform silks both have a GPGXX (SEQ ID NO: 6) motif. The iterated GGX motif is associated with a helical structure having three amino acids per turn and is found in most spider silks. The GGX motif may provide additional elastic properties to the silk. The iterated polyalanine Ax (peptide) motif forms a crystalline β-sheet structure that provides strength to the silk polypeptide, as described for example in WO 03 / 057727. In some embodiments, the recombinant spider silk protein in this disclosure comprises two identical repetitive units each comprising at least one, preferably one, amino acid sequence selected from the group consisting of: GGRPSDTYG (SEQ ID NO: 7) and GGRPSSSYG (SEQ ID NO: 8) derived from Resilin. Resilin is an DB1 / 158748174.5 89 elastomeric protein found in most arthropods that provides low stiffness and high strength. As used herein, “non-repetitive units” refers to an amino acid sequence which is “substantially similar” to a corresponding non-repetitive (carboxy terminal) amino acid sequence within a naturally occurring dragline polypeptide (i.e. wild-type non- repetitive (carboxy terminal) unit), preferably within ADF-3 (SEQ ID NO:50), ADF-4 (SEQ ID NO: 51), NR3 (SEQ ID NO: 62), NR4 (SEQ ID NO: 63) of the spider Araneus diadematus, which is also described in U.S. Pat. No.9,217,017, which is incorporated by reference herein in its entirety, C16 peptide (spider silk protein eADF4, molecular weight of 47.7 kDa, AMSilk) comprising the 16 repeats of the sequence GSSAAAAAAAASGPGGYGPENQGPSGPGGYGPGGP (SEQ ID NO: 9), an amino acid sequence adapted from the natural sequence of ADF4 from A. diadematus. Non-repetitive ADF-4 and variants thereof display efficient assembly behavior. Among the synthetic spider silk proteins, the recombinant silk protein in this disclosure comprises in some embodiments the C16-protein having the polypeptide sequence SEQ ID NO: 64, which is also described in U.S. Patent No.8,288,512, which is incorporated by reference herein in its entirety. Besides the polypeptide sequence shown in SEQ ID NO: 64, particularly functional equivalents, functional derivatives and salts of this sequence are also included. As used herein, “functional equivalents” refers to mutant which, in at least one sequence position of the abovementioned amino acid sequences, have an amino acid other than that specifically mentioned. In some embodiments, the recombinant spider silk protein in this disclosure comprises, in an effective amount, at least one natural or recombinant silk protein including spider silk protein, corresponding to Spidroin major 1 described by Xu et al., PNAS, USA, 87, 7120, (1990), Spidroin major 2 described by Hinman and Lewis, J. Biol. Chem., 267, 19320, (1922), recombinant spider silk protein as described in U.S. Patent Application No.2016 / 0222174 and U.S. Patent Nos.9,051,453, 9,617,315, 9,689,089, 8,173,772, 8,642,734, 8,367,8038,097,583, 8,030,024, 7,754,851, 7,148,039, 7,060,260, or alternatively the minor Spidroins described in patent application WO 95 / 25165. Each of the above-cited references is incorporated herein by reference in its entirety. Additional recombinant spider silk proteins suitable DB1 / 158748174.5 90 for the recombinant RSPF of this disclosure include ADF3 and ADF4 from the “Major Ampullate” gland of Araneus diadematus. Recombinant silk is also described in other patents and patent applications, incorporated by reference herein: US 2004590196, US 7,754,851, US 2007654470, US 7,951,908, US 2010785960, US 8,034,897, US 20090263430, US 2008226854, US 20090123967, US 2005712095, US 2007991037, US 20090162896, US 200885266, US 8,372,436, US 2007989907, US 2009267596, US 2010319542, US 2009265344, US 2012684607, US 2004583227, US 8,030,024, US 2006643569, US 7,868,146, US 2007991916, US 8,097,583, US 2006643200, US 8,729,238, US 8,877,903, US 20190062557, US 20160280960, US 20110201783, US 2008991916, US 2011986662, US 2012697729, US 20150328363, US 9,034,816, US 20130172478, US 9,217,017, US 20170202995, US 8,721,991, US 2008227498, US 9,233,067, US 8,288,512, US 2008161364, US 7,148,039, US 1999247806, US 2001861597, US 2004887100, US 9,481,719, US 8,765,688, US 200880705, US 2010809102, US 8,367,803, US 2010664902, US 7,569,660, US 1999138833, US 2000591632, US 20120065126, US 20100278882, US 2008161352, US 20100015070, US 2009513709, US 20090194317, US 2004559286, US 200589551, US 2008187824, US 20050266242, US 20050227322, and US 20044418. Recombinant silk is also described in other patents and patent applications, incorporated by reference herein: US 20190062557, US 20150284565, US 20130225476, US 20130172478, US 20130136779, US 20130109762, US 20120252294, US 20110230911, US 20110201783, US 20100298877, US 10,478,520, US 10,253,213, US 10,072,152, US 9,233,067, US 9,217,017, US 9,034,816, US 8,877,903, US 8,729,238, US 8,721,991, US 8,097,583, US 8,034,897, US 8,030,024, US 7,951,908, US 7,868,146, and US 7,754,851. In some embodiments, the recombinant spider silk protein in this disclosure comprises or consists of 2 to 80 repetitive units, each independently selected from GPGXX (SEQ ID NO: 6), GGX and Ax as defined herein. In some embodiments, the recombinant spider silk protein in this disclosure comprises or consists of repetitive units each independently selected from selected from the group consisting of GPGAS (SEQ ID NO: 10), GPGSG (SEQ ID NO: 11), GPGGY (SEQ ID NO: 12), GPGGP (SEQ ID NO: 13), GPGGA (SEQ ID NO: 14), GPGQQ (SEQ ID NO: 15), GPGGG (SEQ ID NO: 16), GPGQG (SEQ ID NO: 17), GPGGS (SEQ ID NO: 18), GGY, GGP, GGA, GGR, GGS, GGT, GGN, GGQ, DB1 / 158748174.5 91 AAAAA (SEQ ID NO: 19), AAAAAA (SEQ ID NO: 20), AAAAAAA (SEQ ID NO: 21), AAAAAAAA (SEQ ID NO: 22), AAAAAAAAA (SEQ ID NO: 23), AAAAAAAAAA (SEQ ID NO: 24), GGRPSDTYG (SEQ ID NO: 7) and GGRPSSSYG (SEQ ID NO: 8), (i) GPYGPGASAAAAAAGGYGPGSGQQ (SEQ ID NO: 25), (ii) GSSAAAAAAAASGPGGYGPENQGPSGPGGYGPGGP (SEQ ID NO: 9), (iii) GPGQQGPGQQGPGQQGPGQQ (SEQ ID NO: 26): (iv) GPGGAGGPYGPGGAGGPYGPGGAGGPY (SEQ ID NO: 27), (v) GGTTIIEDLDITIDGADGPITISEELTI (SEQ ID NO: 28), (vi) PGSSAAAAAAAASGPGQGQGQGQGQGGRPSDTYG (SEQ ID NO: 29), (vii) SAAAAAAAAGPGGGNGGRPSDTYGAPGGGNGGRPSSSYG (SEQ ID NO: 30), (viii) GGAGGAGGAGGSGGAGGS (SEQ ID NO: 31), (ix) GPGGAGPGGYGPGGSGPGGYGPGGSGPGGY (SEQ ID NO: 32), (x) GPYGPGASAAAAAAGGYGPGCGQQ (SEQ ID NO: 33), (xi) GPYGPGASAAAAAAGGYGPGKGQQ (SEQ ID NO: 34), (xii) GSSAAAAAAAASGPGGYGPENQGPCGPGGYGPGGP (SEQ ID NO: 35), (xiii) GSSAAAAAAAASGPGGYGPKNQGPSGPGGYGPGGP (SEQ ID NO: 36), (xiv) GSSAAAAAAAASGPGGYGPKNQGPCGPGGYGPGGP (SEQ ID NO: 37), or variants thereof as described in U.S. Pat. No.8,877,903, for example, a synthetic spider peptide having sequential order of GPGAS (SEQ ID NO: 10), GGY, GPGSG (SEQ ID NO: 11) in the peptide chain, or sequential order of AAAAAAAA (SEQ ID NO: 22), GPGGY (SEQ ID NO: 12), GPGGP (SEQ ID NO: 13) in the peptide chain, sequential order of AAAAAAAA (SEQ ID NO: 22), GPGQG (SEQ ID NO: 17), GGR in the peptide chain. In some embodiments, this disclosure provides silk protein-like multiblock peptides that imitate the repeating units of amino acids derived from natural spider silk proteins such as Spidroin major 1 domain, Spidroin major 2 domain or Spidroin minor 1 domain and the profile of variation between the repeating units without modifying their three-dimensional conformation, wherein these silk protein-like multiblock peptides comprise a repeating unit of amino acids corresponding to one of the sequences (I), (II), (III) and / or (IV) below. [(XGG)w(XGA)(GXG)x(AGA)y(G)zAG]p (SEQ ID NO: 38) Formula (I) in which: X corresponds to tyrosine or to glutamine, w is an integer equal to 2 or 3, x is an integer from 1 to 3, y is an integer from 5 to 7, z is an integer equal to 1 or 2, and p DB1 / 158748174.5 92 is an integer and having any weight average molecular weight described herein, and / or [(GPG2YGPGQ2)a(X’)2S(A)b]p(SEQ ID NO: 39) Formula (II) in which: X’ corresponds to the amino acid sequence GPS or GPG, a is equal to 2 or 3, b is an integer from 7 to 10, and p is an integer and having any weight average molecular weight described herein, and / or [(GR)(GA)l(A)m(GGX)n(GA)l(A)m]p(SEQ ID NO: 40) Formula (III) and / or [(GGX”)n(GA)m(A)l]p (SEQ ID NO: 41) Formula (IV) in which: X” corresponds to tyrosine, glutamine or alanine, l is an integer from 1 to 6, m is an integer from 0 to 4, n is an integer from 1 to 4, and p is an integer. In some embodiments, the recombinant spider silk protein or an analog of a spider silk protein comprising an amino acid repeating unit of sequence (V): [(Xaa Gly Gly)w(Xaa Gly Ala)(Gly Xaa Gly)x(Ala Gly Ala)y(Gly)zAla Gly]pFormula (V), wherein Xaa is tyrosine or glutamine, w is an integer equal to 2 or 3, x is an integer from 1 to 3, y is an integer from 5 to 7, z is an integer equal to 1 or 2, and p is an integer. In some embodiments, the recombinant spider silk protein in this disclosure is selected from the group consisting of ADF-3 or variants thereof, ADF-4 or variants thereof, MaSpI or variants thereof, MaSpII or variants thereof as described in U.S. Pat. No.9,217,017. In some embodiments, this disclosure provides water soluble recombinant spider silk proteins produced in mammalian cells. The solubility of the spider silk proteins produced in mammalian cells was attributed to the presence of the COOH- terminus in these proteins, which makes them more hydrophilic. These COOH- terminal amino acids are absent in spider silk proteins expressed in microbial hosts. In some embodiments, the recombinant spider silk protein in this disclosure comprises water soluble recombinant spider silk protein C16 modified with an amino or carboxyl terminal selected from the amino acid sequences consisting of: GCGGGGGG (SEQ ID NO: 42), GKGGGGGG (SEQ ID NO: 43), GCGGSGGGGSGGGG (SEQ ID NO: 44), GKGGGGGGSGGGG (SEQ ID NO: 45), and GCGGGGGGSGGGG (SEQ ID NO: 46). In some embodiments, the recombinant spider silk protein in this disclosure comprises C16NR4, C32NR4, C16, C32, NR4C16NR4, NR4C32NR4, NR3C16NR3, or NR3C32NR3 such that the molecular weight of the protein ranges as described herein. DB1 / 158748174.5 93 In some embodiments, the recombinant spider silk protein in this disclosure comprises recombinant spider silk protein having a synthetic repetitive peptide segments and an amino acid sequence adapted from the natural sequence of ADF4 from A. diadematus as described in U.S. Pat. No.8,877,903. In some embodiments, the RSPF in this disclosure comprises the recombinant spider silk proteins having repeating peptide units derived from natural spider silk proteins such as Spidroin major 1 domain, Spidroin major 2 domain or Spidroin minor 1 domain, wherein the repeating peptide sequence is GSSAAAAAAAASGPGQGQGQGQGQGGRPSDTYG (SEQ ID NO: 47) or SAAAAAAAAGPGGGNGGRPSDTYGAPGGGNGGRPSSSYG (SEQ ID NO: 30), as described in U.S. Pat. No.8,367,803, which is incorporated by reference herein in its entirety. In some embodiments, this disclosure provides recombinant spider proteins composed of the GPGGAGPGGYGPGGSGPGGYGPGGSGPGGY (SEQ ID NO: 32) repetitive fragment and having a molecular weight as described herein. As used herein, the term “recombinant silk” refers to recombinant spider and / or silkworm silk protein or fragments thereof. In an embodiment, the spider silk protein is selected from the group consisting of swathing silk (Achniform gland silk), egg sac silk (Cylindriform gland silk), egg case silk (Tubuliform silk), non-sticky dragline silk (Ampullate gland silk), attaching thread silk (Pyriform gland silk), sticky silk core fibers (Flagelliform gland silk), and sticky silk outer fibers (Aggregate gland silk). For example, recombinant spider silk protein, as described herein, includes the proteins described in U.S. Patent Application No.2016 / 0222174 and U.S. Patent Nos. 9,051,453, 9,617,315, 9,689,089, 8,173,772, and 8,642,734. Some organisms make multiple silk fibers with unique sequences, structural elements, and mechanical properties. For example, orb weaving spiders have six unique types of glands that produce different silk polypeptide sequences that are polymerized into fibers tailored to fit an environmental or lifecycle niche. The fibers are named for the gland they originate from and the polypeptides are labeled with the gland abbreviation (e.g. “Ma”) and “Sp” for spidroin (short for spider fibroin). In orb weavers, these types include Major Ampullate (MaSp, also called dragline), Minor Ampullate (MiSp), Flagelliform (Flag), Aciniform (AcSp), Tubuliform (TuSp), and Pyriform (PySp). This combination of polypeptide sequences across fiber types, domains, and variation amongst different genus and species of organisms leads to a DB1 / 158748174.5 94 vast array of potential properties that can be harnessed by commercial production of the recombinant fibers. To date, the vast majority of the work with recombinant silks has focused on the Major Ampullate Spidroins (MaSp). Aciniform (AcSp) silks tend to have high toughness, a result of moderately high strength coupled with moderately high extensibility. AcSp silks are characterized by large block (“ensemble repeat”) sizes that often incorporate motifs of poly serine and GPX. Tubuliform (TuSp or Cylindrical) silks tend to have large diameters, with modest strength and high extensibility. TuSp silks are characterized by their poly serine and poly threonine content, and short tracts of poly alanine. Major Ampullate (MaSp) silks tend to have high strength and modest extensibility. MaSp silks can be one of two subtypes: MaSp1 and MaSp2. MaSp1 silks are generally less extensible than MaSp2 silks, and are characterized by poly alanine, GX, and GGX motifs. MaSp2 silks are characterized by poly alanine, GGX, and GPX motifs. Minor Ampullate (MiSp) silks tend to have modest strength and modest extensibility. MiSp silks are characterized by GGX, GA, and poly A motifs, and often contain spacer elements of approximately 100 amino acids. Flagelliform (Flag) silks tend to have very high extensibility and modest strength. Flag silks are usually characterized by GPG, GGX, and short spacer motifs. Silk polypeptides are characteristically composed of a repeat domain (REP) flanked by non-repetitive regions (e.g., C-terminal and N-terminal domains). In an embodiment, both the C-terminal and N-terminal domains are between 75-350 amino acids in length. The repeat domain exhibits a hierarchical architecture. The repeat domain comprises a series of blocks (also called repeat units). The blocks are repeated, sometimes perfectly and sometimes imperfectly (making up a quasi-repeat domain), throughout the silk repeat domain. The length and composition of blocks varies among different silk types and across different species. Table 1 of U.S. Published Application No.2016 / 0222174, the entirety of which is incorporated herein, lists examples of block sequences from selected species and silk types, with further examples presented in Rising, A. et al., Spider silk proteins: recent advances in recombinant production, structure-function relationships and biomedical applications, Cell Mol. Life Sci., 68:2, pg 169-184 (2011); and Gatesy, J. et al., Extreme diversity, conservation, and convergence of spider silk fibroin sequences, Science, 291:5513, pg.2603-2605 (2001). In some cases, blocks may be arranged in a regular pattern, forming larger macro-repeats that appear multiple times (usually 2-8) in the repeat DB1 / 158748174.5 95 domain of the silk sequence. Repeated blocks inside a repeat domain or macro-repeat, and repeated macro-repeats within the repeat domain, may be separated by spacing elements. The construction of certain spider silk block copolymer polypeptides from the blocks and / or macro-repeat domains, according to certain embodiments of the disclosure, is illustrated in U.S. Published Patent Application No.2016 / 0222174. The recombinant block copolymer polypeptides based on spider silk sequences produced by gene expression in a recombinant prokaryotic or eukaryotic system can be purified according to methods known in the art. In a preferred embodiment, a commercially available expression / secretion system can be used, whereby the recombinant polypeptide is expressed and thereafter secreted from the host cell, to be easily purified from the surrounding medium. If expression / secretion vectors are not used, an alternative approach involves purifying the recombinant block copolymer polypeptide from cell lysates (remains of cells following disruption of cellular integrity) derived from prokaryotic or eukaryotic cells in which a polypeptide was expressed. Methods for generation of such cell lysates are known to those of skill in the art. In some embodiments, recombinant block copolymer polypeptides are isolated from cell culture supernatant. Recombinant block copolymer polypeptide may be purified by affinity separation, such as by immunological interaction with antibodies that bind specifically to the recombinant polypeptide or nickel columns for isolation of recombinant polypeptides tagged with 6-8 histidine residues at their N-terminus or C- terminus Alternative tags may comprise the FLAG epitope or the hemagglutinin epitope. Such methods are commonly used by skilled practitioners. A solution of such polypeptides (i.e., recombinant silk protein) may then be prepared and used as described herein. In another embodiment, recombinant silk protein may be prepared according to the methods described in U.S. Patent No.8,642,734, the entirety of which is incorporated herein, and used as described herein. In an embodiment, a recombinant spider silk protein is provided. The spider silk protein typically consists of from 170 to 760 amino acid residues, such as from 170 to 600 amino acid residues, preferably from 280 to 600 amino acid residues, such as from 300 to 400 amino acid residues, more preferably from 340 to 380 amino acid residues. The small size is advantageous because longer spider silk proteins tend to DB1 / 158748174.5 96 form amorphous aggregates, which require use of harsh solvents for solubilization and polymerization. The recombinant spider silk protein may contain more than 760 residues, in particular in cases where the spider silk protein contains more than two fragments derived from the N-terminal part of a spider silk protein, The spider silk protein comprises an N-terminal fragment consisting of at least one fragment (NT) derived from the corresponding part of a spider silk protein, and a repetitive fragment (REP) derived from the corresponding internal fragment of a spider silk protein. Optionally, the spider silk protein comprises a C-terminal fragment (CT) derived from the corresponding fragment of a spider silk protein. The spider silk protein comprises typically a single fragment (NT) derived from the N-terminal part of a spider silk protein, but in preferred embodiments, the N-terminal fragment include at least two, such as two fragments (NT) derived from the N-terminal part of a spider silk protein. Thus, the spidroin can schematically be represented by the formula NTm-REP, and alternatively NTm-REP-CT, where m is an integer that is 1 or higher, such as 2 or higher, preferably in the ranges of 1-2, 1-4, 1-6, 2-4 or 2-6. Preferred spidroins can schematically be represented by the formulas NT2-REP or NT-REP, and alternatively NT2-REP-CT or NT-REP-CT. The protein fragments are covalently coupled, typically via a peptide bond. In one embodiment, the spider silk protein consists of the NT fragment(s) coupled to the REP fragment, which REP fragment is optionally coupled to the CT fragment. In one embodiment, the first step of the method of producing polymers of an isolated spider silk protein involves expression of a polynucleic acid molecule which encodes the spider silk protein in a suitable host, such as Escherichia coli. The thus obtained protein is isolated using standard procedures. Optionally, lipopolysaccharides and other pyrogens are actively removed at this stage. In the second step of the method of producing polymers of an isolated spider silk protein, a solution of the spider silk protein in a liquid medium is provided. By the terms “soluble” and “in solution” is meant that the protein is not visibly aggregated and does not precipitate from the solvent at 60,000×g. The liquid medium can be any suitable medium, such as an aqueous medium, preferably a physiological medium, typically a buffered aqueous medium, such as a 10-50 mM Tris-HCl buffer or phosphate buffer. The liquid medium has a pH of 6.4 or higher and / or an ion composition that prevents polymerization of the spider silk protein. That is, the liquid DB1 / 158748174.5 97 medium has either a pH of 6.4 or higher or an ion composition that prevents polymerization of the spider silk protein, or both. Ion compositions that prevent polymerization of the spider silk protein can readily be prepared by the skilled person utilizing the methods disclosed herein. A preferred ion composition that prevents polymerization of the spider silk protein has an ionic strength of more than 300 mM. Specific examples of ion compositions that prevent polymerization of the spider silk protein include above 300 mM NaCl, 100 mM phosphate and combinations of these ions having desired preventive effect on the polymerization of the spider silk protein, e.g. a combination of 10 mM phosphate and 300 mM NaCl. The presence of an NT fragment improves the stability of the solution and prevents polymer formation under these conditions. This can be advantageous when immediate polymerization may be undesirable, e.g. during protein purification, in preparation of large batches, or when other conditions need to be optimized. It is preferred that the pH of the liquid medium is adjusted to 6.7 or higher, such as 7.0 or higher, or even 8.0 or higher, such as up to 10.5, to achieve high solubility of the spider silk protein. It can also be advantageous that the pH of the liquid medium is adjusted to the range of 6.4-6.8, which provides sufficient solubility of the spider silk protein but facilitates subsequent pH adjustment to 6.3 or lower. In the third step, the properties of the liquid medium are adjusted to a pH of 6.3 or lower and ion composition that allows polymerization. That is, if the liquid medium wherein the spider silk protein is dissolved has a pH of 6.4 or higher, the pH is decreased to 6.3 or lower. The skilled person is well aware of various ways of achieving this, typically involving addition of a strong or weak acid. If the liquid medium wherein the spider silk protein is dissolved has an ion composition that prevents polymerization, the ion composition is changed so as to allow polymerization. The skilled person is well aware of various ways of achieving this, e.g. dilution, dialysis or gel filtration. If required, this step involves both decreasing the pH of the liquid medium to 6.3 or lower and changing the ion composition so as to allow polymerization. It is preferred that the pH of the liquid medium is adjusted to 6.2 or lower, such as 6.0 or lower. In particular, it may be advantageous from a practical point of view to limit the pH drop from 6.4 or 6.4-6.8 in the preceding step to 6.3 or 6.0-6.3, e.g.6.2 in this step. In a preferred embodiment, the pH of the liquid DB1 / 158748174.5 98 medium of this step is 3 or higher, such as 4.2 or higher. The resulting pH range, e.g. 4.2-6.3 promotes rapid polymerization, In the fourth step, the spider silk protein is allowed to polymerize in the liquid medium having pH of 6.3 or lower and an ion composition that allows polymerization of the spider silk protein. Although the presence of the NT fragment improves solubility of the spider silk protein at a pH of 6.4 or higher and / or an ion composition that prevents polymerization of the spider silk protein, it accelerates polymer formation at a pH of 6.3 or lower when the ion composition allows polymerization of the spider silk protein. The resulting polymers are preferably solid and macroscopic, and they are formed in the liquid medium having a pH of 6.3 or lower and an ion composition that allows polymerization of the spider silk protein. In a preferred embodiment, the pH of the liquid medium of this step is 3 or higher, such as 4.2 or higher. The resulting pH range, e.g.4.2-6.3 promotes rapid polymerization, Resulting polymer may be provided at the molecular weights described herein and prepared as a solution form that may be used as necessary for article coatings. Ion compositions that allow polymerization of the spider silk protein can readily be prepared by the skilled person utilizing the methods disclosed herein. A preferred ion composition that allows polymerization of the spider silk protein has an ionic strength of less than 300 mM. Specific examples of ion compositions that allow polymerization of the spider silk protein include 150 mM NaCl, 10 mM phosphate, 20 mM phosphate and combinations of these ions lacking preventive effect on the polymerization of the spider silk protein, e.g. a combination of 10 mM phosphate or 20 mM phosphate and 150 mM NaCl. It is preferred that the ionic strength of this liquid medium is adjusted to the range of 1-250 mM. Without desiring to be limited to any specific theory, it is envisaged that the NT fragments have oppositely charged poles, and that environmental changes in pH affects the charge balance on the surface of the protein followed by polymerization, whereas salt inhibits the same event. At neutral pH, the energetic cost of burying the excess negative charge of the acidic pole may be expected to prevent polymerization. However, as the dimer approaches its isoelectric point at lower pH, attractive electrostatic forces will eventually become dominant, explaining the observed salt and pH-dependent polymerization behavior of NT and NT-containing minispidroins. It is proposed that, in some embodiments, pH-induced NT polymerization, and increased efficiency of DB1 / 158748174.5 99 fiber assembly of NT-minispidroins, are due to surface electrostatic potential changes, and that clustering of acidic residues at one pole of NT shifts its charge balance such that the polymerization transition occurs at pH values of 6.3 or lower. In a fifth step, the resulting, preferably solid spider silk protein polymers are isolated from said liquid medium. Optionally, this step involves actively removing lipopolysaccharides and other pyrogens from the spidroin polymers. Without desiring to be limited to any specific theory, it has been observed that formation of spidroin polymers progresses via formation of water-soluble spidroin dimers. The present disclosure thus also provides a method of producing dimers of an isolated spider silk protein, wherein the first two method steps are as described above. The spider silk proteins are present as dimers in a liquid medium at a pH of 6.4 or higher and / or an ion composition that prevents polymerization of said spider silk protein. The third step involves isolating the dimers obtained in the second step, and optionally removal of lipopolysaccharides and other pyrogens. In a preferred embodiment, the spider silk protein polymer of the disclosure consists of polymerized protein dimers. The present disclosure thus provides a novel use of a spider silk protein, preferably those disclosed herein, for producing dimers of the spider silk protein. According to another aspect, the disclosure provides a polymer of a spider silk protein as disclosed herein. In an embodiment, the polymer of this protein is obtainable by any one of the methods therefor according to the disclosure. Thus, the disclosure provides various uses of recombinant spider silk protein, preferably those disclosed herein, for producing polymers of the spider silk protein as recombinant silk based coatings. According to one embodiment, the present disclosure provides a novel use of a dimer of a spider silk protein, preferably those disclosed herein, for producing polymers of the isolated spider silk protein as recombinant silk based coatings. In these uses, it is preferred that the polymers are produced in a liquid medium having a pH of 6.3 or lower and an ion composition that allows polymerization of said spider silk protein. In an embodiment, the pH of the liquid medium is 3 or higher, such as 4.2 or higher. The resulting pH range, e.g.4.2-6.3 promotes rapid polymerization, Using the method(s) of the present disclosure, it is possible to control the polymerization process, and this allows for optimization of parameters for obtaining silk polymers with desirable properties and shapes. DB1 / 158748174.5 100 In an embodiment, the recombinant silk proteins described herein, include those described in U.S. patent No.8,642,734, the entirety of which is incorporated by reference. In another embodiment, the recombinant silk proteins described herein may be prepared according to the methods described in U.S. Patent No.9,051,453, the entirety of which is incorporated herein by reference. An amino acid sequence represented by SEQ ID NO: 52, which is also described in U.S. Patent No.9,051,453, is identical to an amino acid sequence that is composed of 50 amino acid residues of an amino acid sequence of ADF3 at the C- terminal (NCBI Accession No.: AAC47010, GI: 1263287). An amino acid sequence represented by SEQ ID NO: 53, which is also described in U.S. Patent No.9,051,453, is identical to an amino acid sequence represented by SEQ ID NO: 52, which is also described in U.S. Patent No.9,051,453, from which 20 residues have been removed from the C-terminal. An amino acid sequence represented by SEQ ID NO: 54, which is also described in U.S. Patent No.9,051,453, is identical to an amino acid sequence represented by SEQ ID NO: 52 from which 29 residues have been removed from the C-terminal. An example of the polypeptide that contains units of the amino acid sequence represented by the formula 1: REP1-REP2 (1) and that has, at a C-terminal, an amino acid sequence represented by any of SEQ ID NOS: 52 to 54 or an amino acid sequence having a homology of 90% or more with the amino acid sequence represented by any of SEQ ID NOS: 52 to 54, which are also described in U.S. Patent No.9,051,453, is a polypeptide having an amino acid sequence represented by SEQ ID NO: 65, which is also described in U.S. Patent No.9,051,453, which is incorporated by reference herein in its entirety. The polypeptide having the amino acid sequence represented by SEQ ID NO: 65, which is also described in U.S. Patent No.9,051,453, is obtained by the following mutation: in an amino acid sequence of ADF3 (NCBI Accession No.: AAC47010, GI: 1263287) to the N-terminal of which has been added an amino acid sequence (SEQ ID NO: 66, which is also described in U.S. Patent No.9,051,453) composed of a start codon, His 10 tags and an HRV3C Protease (Human rhinovirus 3C Protease) recognition site, 1stto 13threpetitive regions are about doubled and the translation ends at the 1154thamino acid residue. In the polypeptide having the amino acid sequence represented by SEQ ID NO: 65, which is DB1 / 158748174.5 101 also described in U.S. Patent No.9,051,453, the C-terminal sequence is identical to the amino acid sequence represented by SEQ ID NO: 54. Further, the polypeptide that contains units of the amino acid sequence represented by the formula 1: REP1-REP2 (1) and that has, at a C-terminal, an amino acid sequence represented by any of SEQ ID NOS: 52 to 54, which are also described in U.S. Patent No.9,051,453, or an amino acid sequence having a homology of 90% or more with the amino acid sequence represented by any of SEQ ID NOS: 52 to 54, which are also described in U.S. Patent No.9,051,453, may be a protein that has an amino acid sequence represented by SEQ ID NO: 65, which is also described in U.S. Patent No.9,051,453, in which one or a plurality of amino acids have been substituted, deleted, inserted and / or added and that has a repetitious region composed of a crystal region and an amorphous region. Further, an example of the polypeptide containing two or more units of the amino acid sequence represented by the formula 1: REP1-REP2 (1) is a recombinant protein derived from ADF4 having an amino acid sequence represented by SEQ ID NO: 67, which is also described in U.S. Patent No.9,051,453, which is incorporated by reference herein in its entirety. The amino acid sequence represented by SEQ ID NO: 67, which is also described in U.S. Patent No.9,051,453, is an amino acid sequence obtained by adding the amino acid sequence (SEQ ID NO: 66, which is also described in U.S. Patent No.9,051,453) composed of a start codon, His 10 tags and an HRV3C Protease (Human rhinovirus 3C Protease) recognition site, to the N-terminal of a partial amino acid sequence of ADF4 obtained from the NCBI database (NCBI Accession No.: AAC47011, GI: 1263289). Further, the polypeptide containing two or more units of the amino acid sequence represented by the formula 1: REP1-REP2 (1) may be a polypeptide that has an amino acid sequence represented by SEQ ID NO: 67, which is also described in U.S. Patent No.9,051,453, in which one or a plurality of amino acids have been substituted, deleted, inserted and / or added and that has a repetitious region composed of a crystal region and an amorphous region. Further, an example of the polypeptide containing two or more units of the amino acid sequence represented by the formula 1: REP1-REP2 (1) is a recombinant protein derived from MaSp2 that has an amino acid sequence represented by SEQ ID NO: 68, which is also described in of U.S. Patent No.9,051,453, which is incorporated by reference here in its entirety. The amino acid sequence represented by SEQ ID NO: 68, which is also described in of U.S. Patent No.9,051,453, is an amino acid sequence obtained by DB1 / 158748174.5 102 adding the amino acid sequence (SEQ ID NO: 66, which is also described in of U.S. Patent No.9,051,453,) composed of a start codon, His 10 tags and an HRV3C Protease (Human rhinovirus 3C Protease) recognition site, to the N-terminal of a partial sequence of MaSp2 obtained from the NCBI web database (NCBI Accession No.: AAT75313, GI: 50363147). Furthermore, the polypeptide containing two or more units of the amino acid sequence represented by the formula 1: REP1-REP2 (1) may be a polypeptide that has an amino acid sequence represented by SEQ ID NO: 68, which is also described in of U.S. Patent No.9,051,453, in which one or a plurality of amino acids have been substituted, deleted, inserted and / or added and that has a repetitious region composed of a crystal region and an amorphous region. Examples of the polypeptide derived from flagelliform silk proteins include a polypeptide containing 10 or more units of an amino acid sequence represented by the formula 2: REP3 (2), preferably a polypeptide containing 20 or more units thereof, and more preferably a polypeptide containing 30 or more units thereof. In the case of producing a recombinant protein using a microbe such as Escherichia coli as a host, the molecular weight of the polypeptide derived from flagelliform silk proteins is preferably 500 kDa or less, more preferably 300 kDa or less, and further preferably 200 kDa or less, in terms of productivity. In the formula (2), the REP 3 indicates an amino acid sequence composed of Gly-Pro-Gly-Gly-X (SEQ ID NO: 69), where X indicates an amino acid selected from the group consisting of Ala, Ser, Tyr and Val. A major characteristic of the spider silk is that the flagelliform silk does not have a crystal region, but has a repetitious region composed of an amorphous region. Since the major dragline silk and the like have a repetitious region composed of a crystal region and an amorphous region, they are expected to have both high stress and stretchability. Meanwhile, as to the flagelliform silk, although the stress is inferior to that of the major dragline silk, the stretchability is high. The reason for this is considered to be that most of the flagelliform silk is composed of amorphous regions. An example of the polypeptide containing 10 or more units of the amino acid sequence represented by the formula 2: REP3 (2) is a recombinant protein derived from flagelliform silk proteins having an amino acid sequence represented by SEQ ID NO: 70, which is also described in U.S. Patent No.9,051,453, which is incorporated by reference herein in its entirety. The amino acid sequence represented by SEQ ID NO: 70, which is also described in U.S. Patent No.9,051,453, is an amino acid DB1 / 158748174.5 103 sequence obtained by combining a partial sequence of flagelliform silk protein of Nephila clavipes obtained from the NCBI database (NCBI Accession No.: AAF36090, GI: 7106224), specifically, an amino acid sequence thereof from the 1220thresidue to the 1659thresidue from the N-terminal that corresponds to repetitive sections and motifs (referred to as a PR1 sequence), with a partial sequence of flagelliform silk protein of Nephila clavipes obtained from the NCBI database (NCBI Accession No.: AAC38847, GI: 2833649), specifically, a C-terminal amino acid sequence thereof from the 816thresidue to the 907thresidue from the C-terminal, and thereafter adding the amino acid sequence (SEQ ID NO: 66, which is also described in U.S. Patent No.9,051,453,) composed of a start codon, His 10 tags and an HRV3C Protease recognition site, to the N-terminal of the combined sequence. Further, the polypeptide containing 10 or more units of the amino acid sequence represented by the formula 2: REP3 (2) may be a polypeptide that has an amino acid sequence represented by SEQ ID NO: 70, which is also described in U.S. Patent No.9,051,453, in which one or a plurality of amino acids have been substituted, deleted, inserted and / or added and that has a repetitious region composed of an amorphous region. The polypeptide can be produced using a host that has been transformed by an expression vector containing a gene encoding a polypeptide. A method for producing a gene is not limited particularly, and it may be produced by amplifying a gene encoding a natural spider silk protein from a cell derived from spiders by a polymerase chain reaction (PCR), etc., and cloning it, or may be synthesized chemically. Also, a method for chemically synthesizing a gene is not limited particularly, and it can be synthesized as follows, for example: based on information of amino acid sequences of natural spider silk proteins obtained from the NCBI web database, etc., oligonucleotides that have been synthesized automatically with AKTA oligopilot plus 10 / 100 (GE Healthcare Japan Corporation) are linked by PCR, etc. At this time, in order to facilitate the purification and observation of protein, it is possible to synthesize a gene that encodes a protein having an amino acid sequence of the above-described amino acid sequence to the N-terminal of which has been added an amino acid sequence composed of a start codon and His 10 tags. Examples of the expression vector include a plasmid, a phage, a virus, and the like that can express protein based on a DNA sequence. The plasmid-type expression vector is not limited particularly as long as it allows a target gene to be expressed in a host cell and it can amplify itself. For example, in the case of using Escherichia coli DB1 / 158748174.5 104 Rosetta (DE3) as a host, a pET22b(+) plasmid vector, a pCold plasmid vector, and the like can be used. Among these, in terms of productivity of protein, it is preferable to use the pET22b(+) plasmid vector. Examples of the host include animal cells, plant cells, microbes, etc. The polypeptide used in the present disclosure is preferably a polypeptide derived from ADF3, which is one of two principal dragline silk proteins of Araneus diadematus. This polypeptide has advantages of basically having high strength- elongation and toughness and of being synthesized easily. Accordingly, the recombinant silk protein (e.g., the recombinant spider silk- based protein) used in accordance with the embodiments, articles, and / or methods described herein, may include one or more recombinant silk proteins described above or recited in U.S. Patent Nos.8,173,772, 8,278,416, 8,618,255, 8,642,734, 8,691,581, 8,729,235, 9,115,204, 9,157,070, 9,309,299, 9,644,012, 9,708,376, 9,051,453, 9,617,315, 9,968,682, 9,689,089, 9,732,125, 9,856,308, 9,926,348, 10,065,997, 10,316,069, and 10,329,332; and U.S. Patent Publication Nos.2009 / 0226969, 2011 / 0281273, 2012 / 0041177, 2013 / 0065278, 2013 / 0115698, 2013 / 0316376, 2014 / 0058066, 2014 / 0079674, 2014 / 0245923, 2015 / 0087046, 2015 / 0119554, 2015 / 0141618, 2015 / 0291673, 2015 / 0291674, 2015 / 0239587, 2015 / 0344542, 2015 / 0361144, 2015 / 0374833, 2015 / 0376247, 2016 / 0024464, 2017 / 0066804, 2017 / 0066805, 2015 / 0293076, 2016 / 0222174, 2017 / 0283474, 2017 / 0088675, 2019 / 0135880, 2015 / 0329587, 2019 / 0040109, 2019 / 0135881, 2019 / 0177363, 2019 / 0225646, 2019 / 0233481, 2019 / 0031842, 2018 / 0355120, 2019 / 0186050, 2019 / 0002644, 2020 / 0031887, 2018 / 0273590, 20191 / 094403, 2019 / 0031843, 2018 / 0251501, 2017 / 0066805, 2018 / 0127553, 2019 / 0329526, 2020 / 0031886, 2018 / 0080147, 2019 / 0352349, 2020 / 0043085, 2019 / 0144819, 2019 / 0228449, 2019 / 0340666, 2020 / 0000091, 2019 / 0194710, 2019 / 0151505, 2018 / 0265555, 2019 / 0352330, 2019 / 0248847, and 2019 / 0378191, the entirety of which are incorporated herein by reference. Silk Fibroin-like Protein Fragments The recombinant silk protein in this disclosure comprises synthetic proteins which are based on repeat units of natural silk proteins. Besides the synthetic repetitive silk protein sequences, these can additionally comprise one or more natural nonrepetitive silk protein sequences. As used herein, “silk fibroin-like protein DB1 / 158748174.5 105 fragments” refer to protein fragments having a molecular weight and polydispersity as defined herein, and a certain degree of homology to a protein selected from native silk protein, fibroin heavy chain, fibroin light chain, or any protein comprising one or more GAGAGS (SEQ ID NO: 2) hexa amino acid repeating units. In some embodiments, a degree of homology is selected from about 99%, about 98%, about 97%, about 96%, about 95%, about 94%, about 93%, about 92%, about 91%, about 90%, about 89%, about 88%, about 87%, about 86%, about 85%, about 84%, about 83%, about 82%, about 81%, about 80%, about 79%, about 78%, about 77%, about 76%, about 75%, or less than 75%. As described herein, a protein such as native silk protein, fibroin heavy chain, fibroin light chain, or any protein comprising one or more GAGAGS (SEQ ID NO: 2) hexa amino acid repeating units includes between about 9% and about 45% glycine, or about 9% glycine, or about 10% glycine, about 43% glycine, about 44% glycine, about 45% glycine, or about 46% glycine. As described herein, a protein such as native silk protein, fibroin heavy chain, fibroin light chain, or any protein comprising one or more GAGAGS (SEQ ID NO: 2) hexa amino acid repeating units includes between about 13% and about 30% alanine, or about 13% alanine, or about 28% alanine, or about 29% alanine, or about 30% alanine, or about 31% alanine. As described herein, a protein such as native silk protein, fibroin heavy chain, fibroin light chain, or any protein comprising one or more GAGAGS (SEQ ID NO: 2) hexa amino acid repeating units includes between 9% and about 12% serine, or about 9% serine, or about 10% serine, or about 11% serine, or about 12% serine. In some embodiments, a silk fibroin-like protein described herein includes about 5%, about 6%, about 7%, about 8%, about 9%, about 10%, about 11%, about 12%, about 13%, about 14%, about 15%, about 16%, about 17%, about 18%, about 19%, about 20%, about 21%, about 22%, about 23 %, about 24%, about 25%, about 26%, about 27%, about 28%, about 29%, about 30%, about 31%, about 32%, about 33%, about 34%, about 35%, about 36%, about 37%, about 38%, about 39%, about 40%, about 41%, about 42%, about 43%, about 44%, about 45%, about 46%, about 47%, about 48%, about 49%, about 50%, about 51%, about 52%, about 53%, about 54%, or about 55% glycine. In some embodiments, a silk fibroin-like protein described herein includes about 13%, about 14%, about 15%, about 16%, about 17%, about 18%, about 19%, about 20%, about 21%, about 22%, about 23%, about 24%, about 25%, about 26%, about 27%, about 28%, about 29%, about 30%, about 31%, DB1 / 158748174.5 106 about 32%, about 33%, about 34%, about 35%, about 36%, about 37%, about 38%, or about 39% alanine. In some embodiments, a silk fibroin-like protein described herein includes about 2%, about 3%, about 4%, about 5%, about 6%, about 7%, about 8%, about 9%, about 10%, about 11%, about 12%, about 13%, about 14%, about 15%, about 16%, about 17%, about 18%, about 19%, about 20%, about 21%, or about 22% serine. In some embodiments, a silk fibroin-like protein described herein may include independently any amino acid known to be included in natural fibroin. In some embodiments, a silk fibroin-like protein described herein may exclude independently any amino acid known to be included in natural fibroin. In some embodiments, on average 2 out of 6 amino acids, 3 out of 6 amino acids, or 4 out of 6 amino acids in a silk fibroin-like protein described herein is glycine. In some embodiments, on average 1 out of 6 amino acids, 2 out of 6 amino acids, or 3 out of 6 amino acids in a silk fibroin-like protein described herein is alanine. In some embodiments, on average none out of 6 amino acids, 1 out of 6 amino acids, or 2 out of 6 amino acids in a silk fibroin-like protein described herein is serine. Sericin or Sericin Fragments The main body of the raw silk is silk fibroin fiber, and the silk fibroin fiber is coated with an adhesive substance silk sericin. Sericin is a colloidal silk protein that covers the surface of the silk thread and is composed of bulky amino acids rich in chemical reactivity such as serine, threonine, and aspartic acid, in addition to glycine and alanine. In the various processes of producing silk from raw silk, sericin is important in controlling the solubility of silk and producing high quality silk. Moreover, it plays an extremely important role as an adhesion functional protein. When silk fiber is used as a clothing material, most of the silk sericin covering the silk thread is removed and discarded, so sericin is a valuable unused resource. In some embodiments, the silk protein fragments described herein include sericin or sericin fragments. Methods of preparing sericin or sericin fragments and their applications in various fields are known and are described herein , and are also described, for example, in U.S. Patents Nos.7,115,388, 7,157,273, and 9,187,538, all of which are incorporated by reference herein in their entireties. In some embodiments, sericin removed from the raw silk cocoons, such as in a degumming step, can be collected and used in the methods described herein. Sericin DB1 / 158748174.5 107 can also be reconstituted from a powder, and used within the compositions and methods of the disclosure. Other Properties of SPF Compositions of the present disclosure are “biocompatible” or otherwise exhibit “biocompatibility” meaning that the compositions are compatible with living tissue or a living system by not being toxic, injurious, or physiologically reactive and not causing immunological rejection or an inflammatory response. Such biocompatibility can be evidenced by participants topically applying compositions of the present disclosure on their skin for an extended period of time. In an embodiment, the extended period of time is about 3 days. In an embodiment, the extended period of time is about 7 days. In an embodiment, the extended period of time is about 14 days. In an embodiment, the extended period of time is about 21 days. In an embodiment, the extended period of time is about 30 days. In an embodiment, the extended period of time is selected from the group consisting of about 1 month, about 2 months, about 3 months, about 4 months, about 5 months, about 6 months, about 7 months, about 8 months, about 9 months, about 10 months, about 11 months, about 12 months, and indefinitely. For example, in some embodiments, the coatings described herein are biocompatible coatings. In some embodiments, compositions described herein, which may be biocompatible compositions (e.g., biocompatible coatings that include silk), may be evaluated and comply with International Standard ISO 10993-1, titled the “Biological evaluation of medical devices – Part 1: Evaluation and testing within a risk management process.” In some embodiments, compositions described herein, which may be biocompatible compositions, may be evaluated under ISO 106993-1 for one or more of cytotoxicity, sensitization, hemocompatibility, pyrogenicity, implantation, genotoxicity, carcinogenicity, reproductive and developmental toxicity, and degradation. Compositions of the present disclosure are “hypoallergenic” meaning that they are relatively unlikely to cause an allergic reaction. Such hypoallergenicity can be evidenced by participants topically applying compositions of the present disclosure on their skin for an extended period of time. In an embodiment, the extended period of time is about 3 days. In an embodiment, the extended period of time is about 7 days. In an embodiment, the extended period of time is about 14 days. In an embodiment, DB1 / 158748174.5 108 the extended period of time is about 21 days. In an embodiment, the extended period of time is about 30 days. In an embodiment, the extended period of time is selected from the group consisting of about 1 month, about 2 months, about 3 months, about 4 months, about 5 months, about 6 months, about 7 months, about 8 months, about 9 months, about 10 months, about 11 months, about 12 months, and indefinitely. In an embodiment, the stability of a composition of the present disclosure is about 1 day. In an embodiment, the stability of a composition of the present disclosure is about 2 days. In an embodiment, the stability of a composition of the present disclosure is about 3 days. In an embodiment, the stability of a composition of the present disclosure is about 4 days. In an embodiment, the stability of a composition of the present disclosure is about 5 days. In an embodiment, the stability of a composition of the present disclosure is about 6 days. In an embodiment, the stability of a composition of the present disclosure is about 7 days. In an embodiment, the stability of a composition of the present disclosure is about 8 days. In an embodiment, the stability of a composition of the present disclosure is about 9 days. In an embodiment, the stability of a composition of the present disclosure is about 10 days. In an embodiment, the stability of a composition of the present disclosure is about 11 days, about 12 days, about 13 days, about 14 days, about 15 days, about 16 days, about 17 days, about 18 days, about 19 days, about 20 days, about 21 days, about 22 days, about 23 days, about 24 days, about 25 days, about 26 days, about 27 days, about 28 days, about 29 days, or about 30 days. In an embodiment, the stability of a composition of the present disclosure is 10 days to 6 months. In an embodiment, the stability of a composition of the present disclosure is 6 months to 12 months. In an embodiment, the stability of a composition of the present disclosure is 12 months to 18 months. In an embodiment, the stability of a composition of the present disclosure is 18 months to 24 months. In an embodiment, the stability of a composition of the present disclosure is 24 months to 30 months. In an embodiment, the stability of a composition of the present disclosure is 30 months to 36 months. In an embodiment, the stability of a composition of the present disclosure is 36 months to 48 months. In an embodiment, the stability of a composition of the present disclosure is 48 months to 60 months. In an embodiment, a SPF composition of the present disclosure is not soluble in an aqueous solution due to the crystallinity of the protein. In an embodiment, a SPF composition of the present disclosure is soluble in an aqueous solution. In an DB1 / 158748174.5 109 embodiment, the SPF of a composition of the present disclosure include a crystalline portion of about two-thirds and an amorphous region of about one-third. In an embodiment, the SPF of a composition of the present disclosure include a crystalline portion of about one-half and an amorphous region of about one-half. In an embodiment, the SPF of a composition of the present disclosure include a 99% crystalline portion and a 1% amorphous region. In an embodiment, the SPF of a composition of the present disclosure include a 95% crystalline portion and a 5% amorphous region. In an embodiment, the SPF of a composition of the present disclosure include a 90% crystalline portion and a 10% amorphous region. In an embodiment, the SPF of a composition of the present disclosure include a 85% crystalline portion and a 15% amorphous region. In an embodiment, the SPF of a composition of the present disclosure include a 80% crystalline portion and a 20% amorphous region. In an embodiment, the SPF of a composition of the present disclosure include a 75% crystalline portion and a 25% amorphous region. In an embodiment, the SPF of a composition of the present disclosure include a 70% crystalline portion and a 30% amorphous region. In an embodiment, the SPF of a composition of the present disclosure include a 65% crystalline portion and a 35% amorphous region. In an embodiment, the SPF of a composition of the present disclosure include a 60% crystalline portion and a 40% amorphous region. In an embodiment, the SPF of a composition of the present disclosure include a 50% crystalline portion and a 50% amorphous region. In an embodiment, the SPF of a composition of the present disclosure include a 40% crystalline portion and a 60% amorphous region. In an embodiment, the SPF of a composition of the present disclosure include a 35% crystalline portion and a 65% amorphous region. In an embodiment, the SPF of a composition of the present disclosure include a 30% crystalline portion and a 70% amorphous region. In an embodiment, the SPF of a composition of the present disclosure include a 25% crystalline portion and a 75% amorphous region. In an embodiment, the SPF of a composition of the present disclosure include a 20% crystalline portion and a 80% amorphous region. In an embodiment, the SPF of a composition of the present disclosure include a 15% crystalline portion and a 85% amorphous region. In an embodiment, the SPF of a composition of the present disclosure include a 10% crystalline portion and a 90% amorphous region. In an embodiment, the SPF of a composition of the present disclosure include a 5% crystalline portion and a 90% amorphous region. In an DB1 / 158748174.5 110 embodiment, the SPF of a composition of the present disclosure include a 1% crystalline portion and a 99% amorphous region. As used herein, the term “substantially free of inorganic residuals” means that the composition exhibits residuals of 0.1 % (w / w) or less. In an embodiment, substantially free of inorganic residuals refers to a composition that exhibits residuals of 0.05% (w / w) or less. In an embodiment, substantially free of inorganic residuals refers to a composition that exhibits residuals of 0.01 % (w / w) or less. In an embodiment, the amount of inorganic residuals is between 0 ppm (“non-detectable” or “ND”) and 1000 ppm. In an embodiment, the amount of inorganic residuals is ND to about 500 ppm. In an embodiment, the amount of inorganic residuals is ND to about 400 ppm. In an embodiment, the amount of inorganic residuals is ND to about 300 ppm. In an embodiment, the amount of inorganic residuals is ND to about 200 ppm. In an embodiment, the amount of inorganic residuals is ND to about 100 ppm. In an embodiment, the amount of inorganic residuals is between 10 ppm and 1000 ppm. As used herein, the term “substantially free of organic residuals” means that the composition exhibits residuals of 0.1 % (w / w) or less, in an embodiment, substantially free of organic residuals refers to a composition that exhibits residuals of 0.05% (w / w) or less. In an embodiment, substantially free of organic residuals refers to a composition that exhibits residuals of 0.01% (w / w) or less. In an embodiment, the amount of organic residuals is between 0 ppm (“non-detectable” or “ND”) and 1000 ppm. In an embodiment, the amount of organic residuals is ND to about 500 ppm. In an embodiment, the amount of organic residuals is ND to about 400 ppm. In an embodiment, the amount of organic residuals is ND to about 300 ppm. In an embodiment, the amount of organic residuals is ND to about 200 ppm. In an embodiment, the amount of organic residuals is ND to about 100 ppm. In an embodiment, the amount of organic residuals is between 10 ppm and 1000 ppm. Compositions of the present disclosure exhibit “biocompatibility” meaning that the compositions are compatible with living tissue or a living system by not being toxic, injurious, or physiologically reactive and not causing immunological rejection. Such biocompatibility can be evidenced by participants topically applying compositions of the present disclosure on their skin for an extended period of time. In an embodiment, the extended period of time is about 3 days. In an embodiment, the extended period of time is about 7 days, in an embodiment, the extended period of time is about 14 days, in an embodiment, the extended period of time is about 21 DB1 / 158748174.5 111 days. In an embodiment, the extended period of time is about 30 days. In an embodiment, the extended period of time is selected from the group consisting of about I month, about 2 months, about 3 months, about 4 months, about 5 months, about 6 months, about 7 months, about 8 months, about 9 months, about 10 months, about 11 months, about 12 months, and indefinitely. Compositions of the present disclosure are “hypoallergenic” meaning that they are relatively unlikely to cause an allergic reaction. Such hypoallergenicity can be evidenced by participants topically applying compositions of the present disclosure on their skin for an extended period of time. In an embodiment, the extended period of time is about 3 days. In an embodiment, the extended period of time is about 7 days. In an embodiment, the extended period of time is about 14 days. In an embodiment, the extended period of time is about 21 days. In an embodiment, the extended period of time is about 30 days. In an embodiment, the extended period of time is selected from the group consisting of about 1 month, about 2 months, about 3 months, about 4 months, about 5 months, about 6 months, about 7 months, about 8 months, about 9 months, about 10 months, about 11 months, about 12 months, and indefinitely. Following are non-limiting examples of suitable ranges for various parameters in and for preparation of the silk solutions of the present disclosure. The silk solutions of the present disclosure may include one or more, but not necessarily all, of these parameters and may be prepared using various combinations of ranges of such parameters. In an embodiment, the percent SPF in the solution is less than 30.0 wt. %. In an embodiment, the percent SPF in the solution is less than 25.0 wt. %. In an embodiment, the percent SPF in the solution is less than 20.0 wt. %. In an embodiment, the percent SPF in the solution is less than 19.0 wt. %. In an embodiment, the percent SPF in the solution is less than 18.0 wt. %. In an embodiment, the percent SPF in the solution is less than 17.0 wt. %. In an embodiment, the percent SPF in the solution is less than 16.0 wt. %. In an embodiment, the percent SPF in the solution is less than 15.0 wt. %. In an embodiment, the percent SPF in the solution is less than 14.0 wt. %. In an embodiment, the percent SPF in the solution is less than 13.0 wt. %. In an embodiment, the percent SPF in the solution is less than 12.0 wt. %. In an embodiment, the percent SPF in the solution is less than 11.0 wt. %. In an embodiment, the percent SPF in the solution is less than 10.0 wt. %. In an DB1 / 158748174.5 112 embodiment, the percent SPF in the solution is less than 9.0 wt. %. In an embodiment, the percent SPF in the solution is less than 8.0 wt. %. In an embodiment, the percent SPF in the solution is less than 7.0 wt. %. In an embodiment, the percent SPF in the solution is less than 6.0 wt. %. In an embodiment, the percent SPF in the solution is less than 5.0 wt. %. In an embodiment, the percent SPF in the solution is less than 4.0 wt. %. In an embodiment, the percent SPF in the solution is less than 3.0 wt. %. In an embodiment, the percent SPF in the solution is less than 2.0 wt. %. In an embodiment, the percent SPF in the solution is less than 1.0 wt. %. In an embodiment, the percent SPF in the solution is less than 0.9 wt. %. In an embodiment, the percent SPF in the solution is less than 0.8 wt. %. In an embodiment, the percent SPF in the solution is less than 0.7 wt. %. In an embodiment, the percent SPF in the solution is less than 0.6 wt. %. In an embodiment, the percent SPF in the solution is less than 0.5 wt. %. In an embodiment, the percent SPF in the solution is less than 0.4 wt. %. In an embodiment, the percent SPF in the solution is less than 0.3 wt. %. In an embodiment, the percent SPF in the solution is less than 0.2 wt. %. In an embodiment, the percent SPF in the solution is less than 0.1 wt. %. In an embodiment, the percent SPF in the solution is greater than 0.1 wt. %. In an embodiment, the percent SPF in the solution is greater than 0.2 wt. %. In an embodiment, the percent SPF in the solution is greater than 0.3 wt. %. In an embodiment, the percent SPF in the solution is greater than 0.4 wt. %. In an embodiment, the percent SPF in the solution is greater than 0.5 wt. %. In an embodiment, the percent SPF in the solution is greater than 0.6 wt. %. In an embodiment, the percent SPF in the solution is greater than 0.7 wt. %. In an embodiment, the percent SPF in the solution is greater than 0.8 wt. %. In an embodiment, the percent SPF in the solution is greater than 0.9 wt. %. In an embodiment, the percent SPF in the solution is greater than 1.0 wt. %. In an embodiment, the percent SPF in the solution is greater than 2.0 wt. %. In an embodiment, the percent SPF in the solution is greater than 3.0 wt. %. In an embodiment, the percent SPF in the solution is greater than 4.0 wt. %. In an embodiment, the percent SPF in the solution is greater than 5.0 wt. %. In an embodiment, the percent SPF in the solution is greater than 6.0 wt. %. In an embodiment, the percent SPF in the solution is greater than 7.0 wt. %. In an embodiment, the percent SPF in the solution is greater than 8.0 wt. %. In an embodiment, the percent SPF in the solution is greater than 9.0 wt. %. In an DB1 / 158748174.5 113 embodiment, the percent SPF in the solution is greater than 10.0 wt. %. In an embodiment, the percent SPF in the solution is greater than 11.0 wt. %. In an embodiment, the percent SPF in the solution is greater than 12.0 wt. %. In an embodiment, the percent SPF in the solution is greater than 13.0 wt. %. In an embodiment, the percent SPF in the solution is greater than 14.0 wt. %. In an embodiment, the percent SPF in the solution is greater than 15.0 wt. %. In an embodiment, the percent SPF in the solution is greater than 16.0 wt. %. In an embodiment, the percent SPF in the solution is greater than 17.0 wt. %. In an embodiment, the percent SPF in the solution is greater than 18.0 wt. %. In an embodiment, the percent SPF in the solution is greater than 19.0 wt. %. In an embodiment, the percent SPF in the solution is greater than 20.0 wt. %. In an embodiment, the percent SPF in the solution is greater than 25.0 wt. %. In an embodiment, the percent SPF in the solution ranges from about 0.1 wt. % to about 30.0 wt. %. In an embodiment, the percent SPF in the solution ranges from about 0.1 wt. % to about 25.0 wt. %. In an embodiment, the percent SPF in the solution ranges from about 0.1 wt. % to about 20.0 wt. %. In an embodiment, the percent SPF in the solution ranges from about 0.1 wt. % to about 15.0 wt. %. In an embodiment, the percent SPF in the solution ranges from about 0.1 wt. % to about 10.0 wt. %. In an embodiment, the percent SPF in the solution ranges from about 0.1 wt. % to about 9.0 wt. %. In an embodiment, the percent SPF in the solution ranges from about 0.1 wt. % to about 8.0 wt. %. In an embodiment, the percent SPF in the solution ranges from about 0.1 wt. % to about 7.0 wt. %. In an embodiment, the percent SPF in the solution ranges from about 0.1 wt. % to about 6.5 wt. %. In an embodiment, the percent SPF in the solution ranges from about 0.1 wt. % to about 6.0 wt. %. In an embodiment, the percent SPF in the solution ranges from about 0.1 wt. % to about 5.5 wt. %. In an embodiment, the percent SPF in the solution ranges from about 0.1 wt. % to about 5.0 wt. %. In an embodiment, the percent SPF in the solution ranges from about 0.1 wt. % to about 4.5 wt. %. In an embodiment, the percent SPF in the solution ranges from about 0.1 wt. % to about 4.0 wt. %. In an embodiment, the percent SPF in the solution ranges from about 0.1 wt. % to about 3.5 wt. %. In an embodiment, the percent SPF in the solution ranges from about 0.1 wt. % to about 3.0 wt. %. In an embodiment, the percent SPF in the solution ranges from about 0.1 wt. % to about 2.5 wt. %. In an embodiment, the percent SPF in the solution ranges from about 0.1 wt. % to about 2.0 wt. %. In an embodiment, the percent SPF in the solution DB1 / 158748174.5 114 ranges from about 0.1 wt. % to about 2.4 wt. %. In an embodiment, the percent SPF in the solution ranges from about 0.5 wt. % to about 5.0 wt. %. In an embodiment, the percent SPF in the solution ranges from about 0.5 wt. % to about 4.5 wt. %. In an embodiment, the percent SPF in the solution ranges from about 0.5 wt. % to about 4.0 wt. %. In an embodiment, the percent SPF in the solution ranges from about 0.5 wt. % to about 3.5 wt. %. In an embodiment, the percent SPF in the solution ranges from about 0.5 wt. % to about 3.0 wt. %. In an embodiment, the percent SPF in the solution ranges from about 0.5 wt. % to about 2.5 wt. %. In an embodiment, the percent SPF in the solution ranges from about 1.0 wt. % to about 4.0 wt. %. In an embodiment, the percent SPF in the solution ranges from about 1.0 wt. % to about 3.5 wt. %. In an embodiment, the percent SPF in the solution ranges from about 1.0 wt. % to about 3.0 wt. %. In an embodiment, the percent SPF in the solution ranges from about 1.0 wt. % to about 2.5 wt. %. In an embodiment, the percent SPF in the solution ranges from about 1.0 wt. % to about 2.4 wt. %. In an embodiment, the percent SPF in the solution ranges from about 1.0 wt. % to about 2.0 wt. %. In an embodiment, the percent SPF in the solution ranges from about 20.0 wt. % to about 30.0 wt. %. In an embodiment, the percent SPF in the solution ranges from about 0.1 wt. % to about 10.0 wt. %. In an embodiment, the percent SPF in the solution ranges from about 1.0 wt. % to about 10.0 wt. %. In an embodiment, the percent SPF in the solution ranges from about 2 wt. % to about 10.0 wt. %. In an embodiment, the percent SPF in the solution ranges from about 0.1 wt. % to about 6.0 wt. %. In an embodiment, the percent SPF in the solution ranges from about 6.0 wt. % to about 10.0 wt. %. In an embodiment, the percent SPF in the solution ranges from about 6.0 wt. % to about 8.0 wt. %. In an embodiment, the percent SPF in the solution ranges from about 6.0 wt. % to about 9.0 wt. %. In an embodiment, the percent SPF in the solution ranges from about 10.0 wt. % to about 20.0 wt. %. In an embodiment, the percent SPF in the solution ranges from about 11.0 wt. % to about 19.0 wt. %. In an embodiment, the percent SPF in the solution ranges from about 12.0 wt. % to about 18.0 wt. %. In an embodiment, the percent SPF in the solution ranges from about 13.0 wt. % to about 17.0 wt. %. In an embodiment, the percent SPF in the solution ranges from about 14.0 wt. % to about 16.0 wt. %. In an embodiment, the percent SPF in the solution is about 1.0 wt. %. In an embodiment, the percent SPF in the solution is about 0.5 wt. %. In an embodiment, the percent SPF in the solution is about 1.5 wt. %. In an embodiment, the percent SPF in the solution is about 2.0 wt.%. In an DB1 / 158748174.5 115 embodiment, the percent SPF in the solution is about 2.4 wt. %. In an embodiment, the percent SPF in the solution is 3.0 wt. %. In an embodiment, the percent SPF in the solution is 3.5 wt. %. In an embodiment, the percent SPF in the solution is about 4.0 wt. %. In an embodiment, the percent SPF in the solution is about 4.5 wt. %. In an embodiment, the percent SPF in the solution is about 5.0 wt. %. In an embodiment, the percent SPF in the solution is about 5.5 wt. %. In an embodiment the percent SPF in the solution is about 6.0 wt. %. In an embodiment, the percent SPF in the solution is about 6.5 wt. %. In an embodiment, the percent SPF in the solution is about 7.0 wt. %. In an embodiment, the percent SPF in the solution is about 7.5 wt. %. In an embodiment, the percent SPF in the solution is about 8.0 wt. %. In an embodiment, the percent SPF in the solution is about 8.5 wt. %. In an embodiment, the percent SPF in the solution is about 9.0 wt. %. In an embodiment, the percent SPF in the solution is about 9.5 wt. %. In an embodiment, the percent SPF in the solution is about 10.0 wt. %. In an embodiment, the percent sericin in the solution is non-detectable to 25.0 wt. %. In an embodiment, the percent sericin in the solution is non-detectable to 5.0 wt. %. In an embodiment, the percent sericin in the solution is 1.0 wt. %. In an embodiment, the percent sericin in the solution is 2.0 wt. %. In an embodiment, the percent sericin in the solution is 3.0 wt. %. In an embodiment, the percent sericin in the solution is 4.0 wt. %. In an embodiment, the percent sericin in the solution is 5.0 wt. %. In an embodiment, the percent sericin in the solution is 10.0 wt. %. In an embodiment, the percent sericin in the solution is 25.0 wt. %. In some embodiments, the silk fibroin protein fragments of the present disclosure are shelf stable (they will not slowly or spontaneously gel when stored in an aqueous solution and there is no aggregation of fragments and therefore no increase in molecular weight over time), from 10 days to 3 years depending on storage conditions, percent SPF, and number of shipments and shipment conditions. Additionally, pH may be altered to extend shelf life and / or support shipping conditions by preventing premature folding and aggregation of the silk. In an embodiment, the stability of the LiBr-silk fragment solution is 0 to 1 year. In an embodiment, the stability of the LiBr-silk fragment solution is 0 to 2 years. In an embodiment, the stability of the LiBr-silk fragment solution is 0 to 3 years. In an embodiment, the stability of the LiBr-silk fragment solution is 0 to 4 years. In an embodiment, the stability of the LiBr-silk fragment solution is 0 to 5 years. In an DB1 / 158748174.5 116 embodiment, the stability of the LiBr-silk fragment solution is 1 to 2 years. In an embodiment, the stability of the LiBr-silk fragment solution is 1 to 3 years. In an embodiment, the stability of the LiBr-silk fragment solution is 1 to 4 years. In an embodiment, the stability of the LiBr-silk fragment solution is 1 to 5 years. In an embodiment, the stability of the LiBr-silk fragment solution is 2 to 3 years. In an embodiment, the stability of the LiBr-silk fragment solution is 2 to 4 years. In an embodiment, the stability of the LiBr-silk fragment solution is 2 to 5 years. In an embodiment, the stability of the LiBr-silk fragment solution is 3 to 4 years. In an embodiment, the stability of the LiBr-silk fragment solution is 3 to 5 years. In an embodiment, the stability of the LiBr-silk fragment solution is 4 to 5 years. In an embodiment, the stability of a composition of the present disclosure is 10 days to 6 months. In an embodiment, the stability of a composition of the present disclosure is 6 months to 12 months. In an embodiment, the stability of a composition of the present disclosure is 12 months to 18 months. In an embodiment, the stability of a composition of the present disclosure is 18 months to 24 months. In an embodiment, the stability of a composition of the present disclosure is 24 months to 30 months. In an embodiment, the stability of a composition of the present disclosure is 30 months to 36 months. In an embodiment, the stability of a composition of the present disclosure is 36 months to 48 months. In an embodiment, the stability of a composition of the present disclosure is 48 months to 60 months. In an embodiment, a composition of the present disclosure having SPF has non-detectable levels of LiBr residuals. In an embodiment, the amount of the LiBr residuals in a composition of the present disclosure is between 10 ppm and 1000 ppm. In an embodiment, the amount of the LiBr residuals in a composition of the present disclosure is between 10 ppm and 300 ppm. In an embodiment, the amount of the LiBr residuals in a composition of the present disclosure is less than 25 ppm. In an embodiment, the amount of the Li Br residuals in a composition of the present disclosure is less than 50 ppm. In an embodiment, the amount of the LiBr residuals in a composition of the present disclosure is less than 75 ppm. In an embodiment, the amount of the LiBr residuals in a composition of the present disclosure is less than 100 ppm. In an embodiment, the amount of the LiBr residuals in a composition of the present disclosure is less than 200 ppm. In an embodiment, the amount of the LiBr residuals in a composition of the present disclosure is less than 300 ppm. In an embodiment, the amount of the LiBr residuals in a composition of the present DB1 / 158748174.5 117 disclosure is less than 400 ppm. In an embodiment, the amount of the LiBr residuals in a composition of the present disclosure is less than 500 ppm. In an embodiment, the amount of the LiBr residuals in a composition of the present disclosure is less than 600 ppm. In an embodiment, the amount of the LiBr residuals in a composition of the present disclosure is less than 700 ppm. In an embodiment, the amount of the LiBr residuals in a composition of the present disclosure is less than 800 ppm. In an embodiment, the amount of the LiBr residuals in a composition of the present disclosure is less than 900 ppm. In an embodiment, the amount of the LiBr residuals in a composition of the present disclosure is less than 1000 ppm. In an embodiment, the amount of the LiBr residuals in a composition of the present disclosure is non- detectable to 500 ppm. In an embodiment, the amount of the LiBr residuals in a composition of the present disclosure is non-detectable to 450 ppm. In an embodiment, the amount of the LiBr residue in a composition of the present disclosure is non-detectable to 400 ppm. In an embodiment, the amount of the LiBr residuals in a composition of the present disclosure is non-detectable to 350 ppm. In an embodiment, the amount of the LiBr residuals in a composition of the present disclosure is non-detectable to 300 ppm. In an embodiment, the amount of the LiBr residuals in a composition of the present disclosure is non-detectable to 250 ppm. In an embodiment, the amount of the LiBr residuals in a composition of the present disclosure is non-detectable to 200 ppm. In an embodiment, the amount of the LiBr residuals in a composition of the present disclosure is non-detectable to 150 ppm. In an embodiment, the amount of the LiBr residuals in a composition of the present disclosure is non-detectable to 100 ppm. In an embodiment, the amount of the LiBr residuals in a composition of the present disclosure is 100 ppm to 200 ppm. In an embodiment, the amount of the LiBr residuals in a composition of the present disclosure is 200 ppm to 300 ppm. In an embodiment, the amount of the LiBr residuals in a composition of the present disclosure is 300 ppm to 400 ppm. In an embodiment, the amount of the LiBr residuals in a composition of the present disclosure is 400 ppm to 500 ppm. In an embodiment, a composition of the present disclosure having SPF, has non-detectable levels of Na2CO3 residuals. In an embodiment, the amount of the Na2CO3residuals in a composition of the present disclosure is less than 100 ppm. In an embodiment, the amount of the Na2CO3residuals in a composition of the present disclosure is less than 200 ppm. In an embodiment, the amount of the Na2CO3 DB1 / 158748174.5 118 residuals in a composition of the present disclosure is less than 300 ppm. In an embodiment, the amount of the Na2CO3 residuals in a composition of the present disclosure is less than 400 ppm. In an embodiment, the amount of the Na2CO3residuals in a composition of the present disclosure is less than 500 ppm. In an embodiment, the amount of the Na2CO3 residuals in a composition of the present disclosure is less than 600 ppm. In an embodiment, the amount of the Na2CO3residuals in a composition of the present disclosure is less than 700 ppm. In an embodiment, the amount of the Na2CO3 residuals in a composition of the present disclosure is less than 800 ppm. In an embodiment, the amount of the Na2CO3residuals in a composition of the present disclosure is less than 900 ppm. In an embodiment, the amount of the Na2CO3 residuals in a composition of the present disclosure is less than 1000 ppm. In an embodiment, the amount of the Na2CO3 residuals in a composition of the present disclosure is non-detectable to 500 ppm. In an embodiment, the amount of the Na2CO3 residuals in a composition of the present disclosure is non-detectable to 450 ppm. In an embodiment, the amount of the Na2CO3residuals in a composition of the present disclosure is non-detectable to 400 ppm. In an embodiment, the amount of the Na2CO3residuals in a composition of the present disclosure is non-detectable to 350 ppm. In an embodiment, the amount of the Na2CO3residuals in a composition of the present disclosure is non-detectable to 300 ppm. In an embodiment, the amount of the Na2CO3residuals in a composition of the present disclosure is non-detectable to 250 ppm. In an embodiment, the amount of the Na2CO3residuals in a composition of the present disclosure is non-detectable to 200 ppm. In an embodiment, the amount of the Na2CO3residuals in a composition of the present disclosure is non-detectable to 150 ppm. In an embodiment, the amount of the Na2CO3 residuals in a composition of the present disclosure is non-detectable to 100 ppm. In an embodiment, the amount of the Na2CO3residuals in a composition of the present disclosure is 100 ppm to 200 ppm. In an embodiment, the amount of the Na2CO3 residuals in a composition of the present disclosure is 200 ppm to 300 ppm. In an embodiment, the amount of the Na2CO3residuals in a composition of the present disclosure is 300 ppm to 400 ppm. In an embodiment, the amount of the Na2CO3 residuals in a composition of the present disclosure is 400 ppm to 500 ppm. A unique feature of the SPF compositions of the present disclosure are shelf stability (they will not slowly or spontaneously gel when stored in an aqueous solution and there is no aggregation of fragments and therefore no increase in DB1 / 158748174.5 119 molecular weight over time), from 10 days to 3 years depending on storage conditions, percent silk, and number of shipments and shipment conditions. Additionally pH may be altered to extend shelf-life and / or support shipping conditions by preventing premature folding and aggregation of the silk. In an embodiment, a SPF solution composition of the present disclosure has a shelf stability for up to 2 weeks at room temperature (RT). In an embodiment, a SPF solution composition of the present disclosure has a shelf stability for up to 4 weeks at RT. In an embodiment, a SPF solution composition of the present disclosure has a shelf stability for up to 6 weeks at RT. In an embodiment, a SPF solution composition of the present disclosure has a shelf stability for up to 8 weeks at RT. In an embodiment, a SPF solution composition of the present disclosure has a shelf stability for up to 10 weeks at RT. In an embodiment, a SPF solution composition of the present disclosure has a shelf stability for up to 12 weeks at RT. In an embodiment, a SPF solution composition of the present disclosure has a shelf stability ranging from about 4 weeks to about 52 weeks at RT. Table R below shows shelf stability test results for embodiments of SPF compositions of the present disclosure. sure In some embodiments, the water solubility of the silk film derived from silk fibroin protein fragments as described herein can be modified by solvent annealing (water annealing or methanol annealing), chemical crosslinking, enzyme crosslinking and heat treatment. In some embodiments, the process of annealing may involve inducing beta- sheet formation in the silk fibroin protein fragment solutions used as a coating material. Techniques of annealing (e.g., increase crystallinity) or otherwise promoting DB1 / 158748174.5 120 “molecular packing” of silk fibroin-protein based fragments have been described. In some embodiments, the amorphous silk film is annealed to introduce beta-sheet in the presence of a solvent selected from the group of water or organic solvent. In some embodiments, the amorphous silk film is annealed to introduce beta-sheet in the presence of water (water annealing process). In some embodiments, the amorphous silk fibroin protein fragment film is annealed to introduce beta-sheet in the presence of methanol. In some embodiments, annealing (e.g., the beta sheet formation) is induced by addition of an organic solvent. Suitable organic solvents include, but are not limited to methanol, ethanol, acetone, isopropanol, or combination thereof. In some embodiments, annealing is carried out by so-called “water-annealing” or “water vapor annealing” in which water vapor is used as an intermediate plasticizing agent or catalyst to promote the packing of beta-sheets. In some embodiments, the process of water annealing may be performed under vacuum. Suitable such methods have been described in Jin H-J et al. (2005), Water-stable Silk Films with Reduced Beta-Sheet Content, Advanced Functional Materials, 15: 1241- 1247; Xiao H. et al. (2011), Regulation of Silk Material Structure by Temperature- Controlled Water Vapor Annealing, Biomacromolecules, 12(5): 1686-1696. The important feature of the water annealing process is to drive the formation of crystalline beta-sheet in the silk fibroin protein fragment peptide chain to allow the silk fibroin self-assembling into a continuous film. In some embodiments, the crystallinity of the silk fibroin protein fragment film is controlled by controlling the temperature of water vapor and duration of the annealing. In some embodiments, the annealing is performed at a temperature ranging from about 65 °C to about 110 °C. In some embodiments, the temperature of the water is maintained at about 80 °C. In some embodiments, annealing is performed at a temperature selected from the group of about 65 °C, about 70 °C, about 75 °C, about 80 °C, about 85 °C, about 90 °C, about 95 °C, about 100 °C, about 105 °C, and about 110 °C. In some embodiments, the annealing process lasts a period of time selected from the group of about 1 minute to about 40 minutes, about 1 minute to about 50 minutes, about 1 minute to about 60 minutes, about 1 minute to about 70 minutes, about 1 minute to about 80 minutes, about 1 minute to about 90 minutes, about 1 minute to about 100 minutes, about 1 minute to about 110 minutes, about 1 minute to about 120 minutes, about 1 minute to about 130 minutes, about 5 minutes to about 40 minutes, about 5 minutes to about 50 minutes, about 5 minutes to about 60 DB1 / 158748174.5 121 minutes, about 5 minutes to about 70 minutes, about 5 minutes to about 80 minutes, about 5 minutes to about 90 minutes, about 5 minutes to about 100 minutes, about 5 minutes to about 110 minutes, about 5 minutes to about 120 minutes, about 5 minutes to about 130 minutes, about 10 minutes to about 40 minutes, about 10 minutes to about 50 minutes, about 10 minutes to about 60 minutes, about 10 minutes to about 70 minutes, about 10 minutes to about 80 minutes, about 10 minutes to about 90 minutes, about 10 minutes to about 100 minutes, about 10 minutes to about 110 minutes, about 10 minutes to about 120 minutes, about 10 minutes to about 130 minutes, about 15 minutes to about 40 minutes, about 15 minutes to about 50 minutes, about 15 minutes to about 60 minutes, about 15 minutes to about 70 minutes, about 15 minutes to about 80 minutes, about 15 minutes to about 90 minutes, about 15 minutes to about 100 minutes, about 15 minutes to about 110 minutes, about 15 minutes to about 120 minutes, about 15 minutes to about 130 minutes, about 20 minutes to about 40 minutes, about 20 minutes to about 50 minutes, about 20 minutes to about 60 minutes, about 20 minutes to about 70 minutes, about 20 minutes to about 80 minutes, about 20 minutes to about 90 minutes, about 20 minutes to about 100 minutes, about 20 minutes to about 110 minutes, about 20 minutes to about 120 minutes, about 20 minutes to about 130 minutes, about 25 minutes to about 40 minutes, about 25 minutes to about 50 minutes, about 25 minutes to about 60 minutes, about 25 minutes to about 70 minutes, about 25 minutes to about 80 minutes, about 25 minutes to about 90 minutes, about 25 minutes to about 100 minutes, about 25 minutes to about 110 minutes, about 25 minutes to about 120 minutes, about 25 minutes to about 130 minutes, about 30 minutes to about 40 minutes, about 30 minutes to about 50 minutes, about 30 minutes to about 60 minutes, about 30 minutes to about 70 minutes, about 30 minutes to about 80 minutes, about 30 minutes to about 90 minutes, about 30 minutes to about 100 minutes, about 30 minutes to about 110 minutes, about 30 minutes to about 120 minutes, about 30 minutes to about 130 minutes, about 35 minutes to about 40 minutes, about 35 minutes to about 50 minutes, about 35 minutes to about 60 minutes, about 35 minutes to about 70 minutes, about 35 minutes to about 80 minutes, about 35 minutes to about 90 minutes, about 35 minutes to about 100 minutes, about 35 minutes to about 110 minutes, about 35 minutes to about 120 minutes, about 35 minutes to about 130 minutes, about 40 minutes to about 50 minutes, about 40 minutes to about 60 DB1 / 158748174.5 122 minutes, about 40 minutes to about 70 minutes, about 40 minutes to about 80 minutes, about 40 minutes to about 90 minutes, about 40 minutes to about 100 minutes, about 40 minutes to about 110 minutes, about 40 minutes to about 120 minutes, about 40 minutes to about 130 minutes, about 45 minutes to about 50 minutes, about 45 minutes to about 60 minutes, about 45 minutes to about 70 minutes, about 45 minutes to about 80 minutes, about 45 minutes to about 90 minutes, about 45 minutes to about 100 minutes, about 45 minutes to about 110 minutes, about 45 minutes to about 120 minutes, and about 45 minutes to about 130 minutes. In some embodiments, the annealing process lasts a period of time ranging from about 1 minute to about 60 minutes. In some embodiments, the annealing process lasts a period of time ranging from about 45 minutes to about 60 minutes. The longer water annealing post-processing corresponded an increased crystallinity of silk fibroin protein fragments. In some embodiments, the annealed silk fibroin protein fragment film is immersing the wet silk fibroin protein fragment film in 100 % methanol for 60 minutes at room temperature. The methanol annealing changed the composition of silk fibroin protein fragment film from predominantly amorphous random coil to crystalline antiparallel beta-sheet structure. In some embodiments, the SPF as described herein can be used to prepare SPF microparticles by precipitation with methanol. Alternative flash drying, fluid-bed drying, spray drying or vacuum drying can be applied to remove water from the silk solution. The SPF powder can then be stored and handled without refrigeration or other special handling procedures. In some embodiments, the SPF powders comprise low molecular weight silk fibroin protein fragments. In some embodiments, the SPF powders comprise mid-molecular weight silk fibroin protein fragments. In some embodiments, the SPF powders comprise a mixture of low molecular weight silk fibroin protein fragments and mid-molecular weight silk fibroin protein fragment. As used herein, the terms “substantially sericin free” or “substantially devoid of sericin” refer to silk fibers in which a majority of the sericin protein has been removed. In an embodiment, silk fibroin that is substantially devoid of sericin refers to silk fibroin having from about 0.01 wt. % to about 10.0 wt. % sericin. In an embodiment, silk fibroin that is substantially devoid of sericin refers to silk fibroin having about 0.01 wt. % to about 9.0 wt. % sericin. In an embodiment, silk fibroin that is substantially devoid of sericin refers to silk fibroin having from about 0.01 wt. DB1 / 158748174.5 123 % to about 8.0 wt. % sericin. In an embodiment, silk fibroin that is substantially devoid of sericin refers to silk fibroin having from about 0.01 wt. % to about 7.0 wt. % sericin. In an embodiment, silk fibroin that is substantially devoid of sericin refers to silk fibroin having from about 0.01 wt. % to about 6.0 wt. % sericin. In an embodiment, silk fibroin that is substantially devoid of sericin refers to silk fibroin having from about 0.01 wt. % to about 5.0 wt. % sericin. In an embodiment, silk fibroin that is substantially devoid of sericin refers to silk fibroin having from about 0 wt. % to about 4.0 wt. % sericin. In an embodiment, silk fibroin that is substantially devoid of sericin refers to silk fibroin having from about 0.05 wt. % to about 4.0 wt. % sericin. In an embodiment, silk fibroin that is substantially devoid of sericin refers to silk fibroin having from about 0.1 wt. % to about 4.0 wt. % sericin. In an embodiment, silk fibroin that is substantially devoid of sericin refers to silk fibroin having from about 0.5 wt. % to about 4.0 wt. % sericin. In an embodiment, silk fibroin that is substantially devoid of sericin refers to silk fibroin having from about 1.0 wt. % to about 4.0 wt. % sericin. In an embodiment, silk fibroin that is substantially devoid of sericin refers to silk fibroin having from about 1.5 wt. % to about 4.0 wt. % sericin. In an embodiment, silk fibroin that is substantially devoid of sericin refers to silk fibroin having from about 2.0 wt. % to about 4.0 wt. % sericin. In an embodiment, silk fibroin that is substantially devoid of sericin refers to silk fibroin having from about 2.5 wt. % to about 4.0 wt. % sericin. In an embodiment, silk fibroin that is substantially devoid of sericin refers to silk fibroin having a sericin content from about 0.01 wt. % to about 0.1 wt. %. In an embodiment, silk fibroin that is substantially devoid of sericin refers to silk fibroin having a sericin content below about 0.1 wt. %. In an embodiment, silk fibroin that is substantially devoid of sericin refers to silk fibroin having a sericin content below about 0.05 wt. %. In an embodiment, when a silk source is added to a boiling (100 °C) aqueous solution of sodium carbonate for a treatment time of between about 30 minutes to about 60 minutes, a degumming loss of about 26.0 wt. % to about 31.0 wt. % is obtained. Following are non-limiting examples of suitable ranges for various parameters in and for preparation of the silk solutions of the present disclosure. The silk solutions of the present disclosure may include one or more, but not necessarily all, of these parameters and may be prepared using various combinations of ranges of such parameters. DB1 / 158748174.5 124 In an embodiment, the percent SPF in the solution is less than 30.0 wt. %. In an embodiment, the percent SPF in the solution is less than 25.0 wt. %. In an embodiment, the percent SPF in the solution is less than 20.0 wt. %. In an embodiment, the percent SPF in the solution is less than 19.0 wt. %. In an embodiment, the percent SPF in the solution is less than 18.0 wt. %. In an embodiment, the percent SPF in the solution is less than 17.0 wt. %. In an embodiment, the percent SPF in the solution is less than 16.0 wt. %. In an embodiment, the percent SPF in the solution is less than 15.0 wt. %. In an embodiment, the percent SPF in the solution is less than 14.0 wt. %. In an embodiment, the percent SPF in the solution is less than 13.0 wt. %. In an embodiment, the percent SPF in the solution is less than 12.0 wt. %. In an embodiment, the percent SPF in the solution is less than 11.0 wt. %. In an embodiment, the percent SPF in the solution is less than 10.0 wt. %. In an embodiment, the percent SPF in the solution is less than 9.0 wt. %. In an embodiment, the percent SPF in the solution is less than 8.0 wt. %. In an embodiment, the percent SPF in the solution is less than 7.0 wt. %. In an embodiment, the percent SPF in the solution is less than 6.0 wt. %. In an embodiment, the percent SPF in the solution is less than 5.0 wt. %. In an embodiment, the percent SPF in the solution is less than 4.0 wt. %. In an embodiment, the percent SPF in the solution is less than 3.0 wt. %. In an embodiment, the percent SPF in the solution is less than 2.0 wt. %. In an embodiment, the percent SPF in the solution is less than 1.0 wt. %. In an embodiment, the percent SPF in the solution is less than 0.9 wt. %. In an embodiment, the percent SPF in the solution is less than 0.8 wt. %. In an embodiment, the percent SPF in the solution is less than 0.7 wt. %. In an embodiment, the percent SPF in the solution is less than 0.6 wt. %. In an embodiment, the percent SPF in the solution is less than 0.5 wt. %. In an embodiment, the percent SPF in the solution is less than 0.4 wt. %. In an embodiment, the percent SPF in the solution is less than 0.3 wt. %. In an embodiment, the percent SPF in the solution is less than 0.2 wt. %. In an embodiment, the percent SPF in the solution is less than 0.1 wt. %. In an embodiment, the percent SPF in the solution is greater than 0.1 wt. %. In an embodiment, the percent SPF in the solution is greater than 0.2 wt. %. In an embodiment, the percent SPF in the solution is greater than 0.3 wt. %. In an embodiment, the percent SPF in the solution is greater than 0.4 wt. %. In an embodiment, the percent SPF in the solution is greater than 0.5 wt. %. In an DB1 / 158748174.5 125 embodiment, the percent SPF in the solution is greater than 0.6 wt. %. In an embodiment, the percent SPF in the solution is greater than 0.7 wt. %. In an embodiment, the percent SPF in the solution is greater than 0.8 wt. %. In an embodiment, the percent SPF in the solution is greater than 0.9 wt. %. In an embodiment, the percent SPF in the solution is greater than 1.0 wt. %. In an embodiment, the percent SPF in the solution is greater than 2.0 wt. %. In an embodiment, the percent SPF in the solution is greater than 3.0 wt. %. In an embodiment, the percent SPF in the solution is greater than 4.0 wt. %. In an embodiment, the percent SPF in the solution is greater than 5.0 wt. %. In an embodiment, the percent SPF in the solution is greater than 6.0 wt. %. In an embodiment, the percent SPF in the solution is greater than 7.0 wt. %. In an embodiment, the percent SPF in the solution is greater than 8.0 wt. %. In an embodiment, the percent SPF in the solution is greater than 9.0 wt. %. In an embodiment, the percent SPF in the solution is greater than 10.0 wt. %. In an embodiment, the percent SPF in the solution is greater than 11.0 wt. %. In an embodiment, the percent SPF in the solution is greater than 12.0 wt. %. In an embodiment, the percent SPF in the solution is greater than 13.0 wt. %. In an embodiment, the percent SPF in the solution is greater than 14.0 wt. %. In an embodiment, the percent SPF in the solution is greater than 15.0 wt. %. In an embodiment, the percent SPF in the solution is greater than 16.0 wt. %. In an embodiment, the percent SPF in the solution is greater than 17.0 wt. %. In an embodiment, the percent SPF in the solution is greater than 18.0 wt. %. In an embodiment, the percent SPF in the solution is greater than 19.0 wt. %. In an embodiment, the percent SPF in the solution is greater than 20.0 wt. %. In an embodiment, the percent SPF in the solution is greater than 25.0 wt. %. In an embodiment, the percent SPF in the solution ranges from about 0.1 wt. % to about 30.0 wt. %. In an embodiment, the percent SPF in the solution ranges from about 0.1 wt. % to about 25.0 wt. %. In an embodiment, the percent SPF in the solution ranges from about 0.1 wt. % to about 20.0 wt. %. In an embodiment, the percent SPF in the solution ranges from about 0.1 wt. % to about 15.0 wt. %. In an embodiment, the percent SPF in the solution ranges from about 0.1 wt. % to about 10.0 wt. %. In an embodiment, the percent SPF in the solution ranges from about 0.1 wt. % to about 9.0 wt. %. In an embodiment, the percent SPF in the solution ranges from about 0.1 wt. % to about 8.0 wt. %. In an embodiment, the percent SPF in the DB1 / 158748174.5 126 solution ranges from about 0.1 wt. % to about 7.0 wt. %. In an embodiment, the percent SPF in the solution ranges from about 0.1 wt. % to about 6.5 wt. %. In an embodiment, the percent SPF in the solution ranges from about 0.1 wt. % to about 6.0 wt. %. In an embodiment, the percent SPF in the solution ranges from about 0.1 wt. % to about 5.5 wt. %. In an embodiment, the percent SPF in the solution ranges from about 0.1 wt. % to about 5.0 wt. %. In an embodiment, the percent SPF in the solution ranges from about 0.1 wt. % to about 4.5 wt. %. In an embodiment, the percent SPF in the solution ranges from about 0.1 wt. % to about 4.0 wt. %. In an embodiment, the percent SPF in the solution ranges from about 0.1 wt. % to about 3.5 wt. %. In an embodiment, the percent SPF in the solution ranges from about 0.1 wt. % to about 3.0 wt. %. In an embodiment, the percent SPF in the solution ranges from about 0.1 wt. % to about 2.5 wt. %. In an embodiment, the percent SPF in the solution ranges from about 0.1 wt. % to about 2.0 wt. %. In an embodiment, the percent SPF in the solution ranges from about 0.1 wt. % to about 2.4 wt. %. In an embodiment, the percent SPF in the solution ranges from about 0.5 wt. % to about 5.0 wt. %. In an embodiment, the percent SPF in the solution ranges from about 0.5 wt. % to about 4.5 wt. %. In an embodiment, the percent SPF in the solution ranges from about 0.5 wt. % to about 4.0 wt. %. In an embodiment, the percent SPF in the solution ranges from about 0.5 wt. % to about 3.5 wt. %. In an embodiment, the percent SPF in the solution ranges from about 0.5 wt. % to about 3.0 wt. %. In an embodiment, the percent SPF in the solution ranges from about 0.5 wt. % to about 2.5 wt. %. In an embodiment, the percent SPF in the solution ranges from about 1.0 wt. % to about 4.0 wt. %. In an embodiment, the percent SPF in the solution ranges from about 1.0 wt. % to about 3.5 wt. %. In an embodiment, the percent SPF in the solution ranges from about 1.0 wt. % to about 3.0 wt. %. In an embodiment, the percent SPF in the solution ranges from about 1.0 wt. % to about 2.5 wt. %. In an embodiment, the percent SPF in the solution ranges from about 1.0 wt. % to about 2.4 wt. %. In an embodiment, the percent SPF in the solution ranges from about 1.0 wt. % to about 2.0 wt. %. In an embodiment, the percent SPF in the solution ranges from about 20.0 wt. % to about 30.0 wt. %. In an embodiment, the percent SPF in the solution ranges from about 0.1 wt. % to about 10.0 wt. %. In an embodiment, the percent SPF in the solution ranges from about 1.0 wt. % to about 10.0 wt. %. In an embodiment, the percent SPF in the solution ranges from about 2 wt. % to about 10.0 wt. %. In an embodiment, the percent SPF in the solution ranges from about 0.1 wt. % to about 6.0 DB1 / 158748174.5 127 wt. %. In an embodiment, the percent SPF in the solution ranges from about 6.0 wt. % to about 10.0 wt. %. In an embodiment, the percent SPF in the solution ranges from about 6.0 wt. % to about 8.0 wt. %. In an embodiment, the percent SPF in the solution ranges from about 6.0 wt. % to about 9.0 wt. %. In an embodiment, the percent SPF in the solution ranges from about 10.0 wt. % to about 20.0 wt. %. In an embodiment, the percent SPF in the solution ranges from about 11.0 wt. % to about 19.0 wt. %. In an embodiment, the percent SPF in the solution ranges from about 12.0 wt. % to about 18.0 wt. %. In an embodiment, the percent SPF in the solution ranges from about 13.0 wt. % to about 17.0 wt. %. In an embodiment, the percent SPF in the solution ranges from about 14.0 wt. % to about 16.0 wt. %. In an embodiment, the percent SPF in the solution is about 1.0 wt. %. In an embodiment, the percent SPF in the solution is about 1.5 wt. %. In an embodiment, the percent SPF in the solution is about 2.0 wt.%. In an embodiment, the percent SPF in the solution is about 2.4 wt. %. In an embodiment, the percent SPF in the solution is 3.0 wt. %. In an embodiment, the percent SPF in the solution is 3.5 wt. %. In an embodiment, the percent SPF in the solution is about 4.0 wt. %. In an embodiment, the percent SPF in the solution is about 4.5 wt. %. In an embodiment, the percent SPF in the solution is about 5.0 wt. %. In an embodiment, the percent SPF in the solution is about 5.5 wt. %. In an embodiment the percent SPF in the solution is about 6.0 wt. %. In an embodiment, the percent SPF in the solution is about 6.5 wt. %. In an embodiment, the percent SPF in the solution is about 7.0 wt. %. In an embodiment, the percent SPF in the solution is about 7.5 wt. %. In an embodiment, the percent SPF in the solution is about 8.0 wt. %. In an embodiment, the percent SPF in the solution is about 8.5 wt. %. In an embodiment, the percent SPF in the solution is about 9.0 wt. %. In an embodiment, the percent SPF in the solution is about 9.5 wt. %. In an embodiment, the percent SPF in the solution is about 10.0 wt. %. In an embodiment, the percent sericin in the solution is non-detectable to 25.0 wt. %. In an embodiment, the percent sericin in the solution is non-detectable to 5.0 wt. %. In an embodiment, the percent sericin in the solution is 1.0 wt. %. In an embodiment, the percent sericin in the solution is 2.0 wt. %. In an embodiment, the percent sericin in the solution is 3.0 wt. %. In an embodiment, the percent sericin in the solution is 4.0 wt. %. In an embodiment, the percent sericin in the solution is 5.0 wt. %. In an embodiment, the percent sericin in the solution is 10.0 wt. %. In an embodiment, the percent sericin in the solution is 25.0 wt. %. DB1 / 158748174.5 128 In some embodiments, the silk fibroin-based protein fragments of the present disclosure are shelf stable (they will not slowly or spontaneously gel when stored in an aqueous solution and there is no aggregation of fragments and therefore no increase in molecular weight over time), from 10 days to 3 years depending on storage conditions, percent SPF, and number of shipments and shipment conditions. Additionally, pH may be altered to extend shelf life and / or support shipping conditions by preventing premature folding and aggregation of the silk. In an embodiment, the stability of the LiBr-silk fragment solution is 0 to 1 year. In an embodiment, the stability of the LiBr-silk fragment solution is 0 to 2 years. In an embodiment, the stability of the LiBr-silk fragment solution is 0 to 3 years. In an embodiment, the stability of the LiBr-silk fragment solution is 0 to 4 years. In an embodiment, the stability of the LiBr-silk fragment solution is 0 to 5 years. In an embodiment, the stability of the LiBr-silk fragment solution is 1 to 2 years. In an embodiment, the stability of the LiBr-silk fragment solution is 1 to 3 years. In an embodiment, the stability of the LiBr-silk fragment solution is 1 to 4 years. In an embodiment, the stability of the LiBr-silk fragment solution is 1 to 5 years. In an embodiment, the stability of the LiBr-silk fragment solution is 2 to 3 years. In an embodiment, the stability of the LiBr-silk fragment solution is 2 to 4 years. In an embodiment, the stability of the LiBr-silk fragment solution is 2 to 5 years. In an embodiment, the stability of the LiBr-silk fragment solution is 3 to 4 years. In an embodiment, the stability of the LiBr-silk fragment solution is 3 to 5 years. In an embodiment, the stability of the LiBr-silk fragment solution is 4 to 5 years. In an embodiment, the stability of a composition of the present disclosure is 10 days to 6 months. In an embodiment, the stability of a composition of the present disclosure is 6 months to 12 months. In an embodiment, the stability of a composition of the present disclosure is 12 months to 18 months. In an embodiment, the stability of a composition of the present disclosure is 18 months to 24 months. In an embodiment, the stability of a composition of the present disclosure is 24 months to 30 months. In an embodiment, the stability of a composition of the present disclosure is 30 months to 36 months. In an embodiment, the stability of a composition of the present disclosure is 36 months to 48 months. In an embodiment, the stability of a composition of the present disclosure is 48 months to 60 months. In an embodiment, a selected property of the SPF coated articles that may be enhanced as compared to non-coated articles may include one or more of dimensional DB1 / 158748174.5 129 stability to laundering, dimensional stability to dry cleaning, appearance after laundering, appearance after dry cleaning, colorfastness to laundering, colorfastness to dry cleaning, colorfastness to non-chlorine bleach, seam torque / spirality (on knits), colorfastness to crocking, colorfastness to rubbing, colorfastness to water, colorfastness to light, colorfastness to perspiration, colorfastness to chlorinated pool water, colorfastness to sea water, tensile strength, seam slippage, tearing strength, seam breaking strength, abrasion resistance, pilling resistance, stretch recovery, bursting strength, colorfastness to die transfer in storage (labels), colorfastness to ozone, pile retention, bowing and skewing, colorfastness to saliva, snagging resistance, wrinkle resistance (e.g., appearance of apparel, retention of creases in fabrics, smooth appearance of fabrics), water repellency, water resistance, stain repellant (e.g., water repellency, oil repellency, water / alcohol repellency), vertical wicking, water absorption, dry rate, soil release, air permeability, wicking, antimicrobial properties, ultraviolet protection, resistance to torque, malodor resistant, biocompatibility, wetting time, absorption rate, spreading speed, accumulative one- way transport, flame retardant properties, coloring properties, fabric softening properties, a pH adjusting property, an antifelting property, and overall moisture management capability. In any of the foregoing embodiments, at least one property of the article is improved, wherein the property that is improved is dimensional stability to laundering, and wherein the property is improved by an amount relative to an uncoated article selected from the group consisting of at least 5%, at least 10%, at least 15%, at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 100%, at least 125%, at least 150%, at least 200%, at least 300%, at least 400%, and at least 500%. In any of the foregoing embodiments, at least one property of the article is improved, wherein the property that is improved is size retention on laundering, and wherein the property is improved by an amount relative to an uncoated article selected from the group consisting of at least 5%, at least 10%, at least 15%, at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 100%, at least 125%, at least 150%, a...

Claims

CLAIMS 1. A plurality of substantially solid particles comprising silk fibroin fragments and a stabilizer, the particles being characterized by at least one of: bulk density, surface area, pore size, pore volume, aspect ratio, and / or Hausner ratio.

2. The plurality of substantially solid particles of any one of claims 1 to 0, wherein the substantially solid particles are annealed.

3. The plurality of substantially solid particles of any one of claims 1 to 2, wherein the substantially solid particles are grounded.

4. The plurality of substantially solid particles of any one of claims 1 to 3, wherein the plurality of substantially solid particles comprise a pH modifier.

5. The plurality of substantially solid particles of claim 4, wherein the pH modifier is selected from sodium hydroxide and Ammonium hydroxide.

6. The plurality of substantially solid particles of claim 4 or 5, wherein the pH modifier is present in the pellet in an amount ranging from about 25 ppm to about 10,000.

7. The plurality of substantially solid particles of any one of claims 1 to 6, wherein the substantially solid particles have a bulk density of less than 0.03 g / ml, less than 0.04 g / ml, less than 0.05 g / ml, less than 0.06 g / ml, less than 0.07 g / ml, less than 0.08 g / ml, less than 0.09 g / ml, less than 0.10 g / ml, less than 0.11 g / ml, less than 0.12 g / ml, less than 0.13 g / ml, less than 0.14 g / ml, less than 0.15 g / ml, less than 0.16 g / ml, less than 0.17 g / ml, less than 0.18 g / ml, less than 0.19 g / ml, less than 0.20 g / ml, less than 0.21 g / ml, less than 0.22 g / ml, less than 0.23 g / ml, less than 0.24 g / ml, or less than 0.25 g / ml, less than 0.26 g / ml, less than 0.27 g / ml, less than 0.28 g / ml, less than 0.29 g / ml, less than 0.30 g / ml, less than 0.31 g / ml, less than 0.32 g / ml, less than 0.33 g / ml, less than 0.34 g / ml, or less than 0.35 g / ml. DB1 / 158748174.5 3448. The plurality of substantially solid particles of any one of claims 1 to 6, wherein the substantially solid particles have an average bulk density of about 0.03 g / ml, about 0.04 g / ml, or about 0.05 g / ml, about 0.03 g / ml, about 0.04 g / ml, about 0.05 g / ml, about 0.06 g / ml, about 0.07 g / ml, about 0.08 g / ml, about 0.09 g / ml, about 0.10 g / ml, about 0.11 g / ml, about 0.12 g / ml, about 0.13 g / ml, about 0.14 g / ml, about 0.15 g / ml, about 0.16 g / ml, about 0.17 g / ml, about 0.18 g / ml, about 0.19 g / ml, about 0.20 g / ml, about 0.21 g / ml, about 0.22 g / ml, about 0.23 g / ml, about 0.24 g / ml, about 0.25 g / ml, about 0.26 g / ml, about 0.27 g / ml, about 0.28 g / ml, about 0.29 g / ml, about 0.30 g / ml, about 0.31 g / ml, about 0.32 g / ml, about 0.33 g / ml, about 0.34 g / ml, or about 0.35 g / ml.

9. The plurality of substantially solid particles of any one of claims 1 to 8, wherein the substantially solid particles have a Hausner ratio of between 1.00 and 1.11, between 1.12 and 1.18, between 1.19 and 1.25, between 1.26 and 1.34, or between 1.35 and 1.

45.

10. The plurality of substantially solid particles of any one of claims 1 to 9, wherein the substantially solid particles have an average diameter of between about 3 mm and about 10 mm.

11. The plurality of substantially solid particles of any one of claims 1 to 9, wherein the substantially solid particles have an average diameter of about 3 mm, about 4 mm, about 5 mm, about 6 mm, about 7 mm, about 8 mm, about 9 mm, or about 10 mm.

12. The plurality of substantially solid particles of any one of claims 1 to 11, wherein the substantially solid particles have an aspect ratio between 1 and about 1.

45.

13. The plurality of substantially solid particles of any one of claims 1 to 11, wherein the substantially solid particles have an aspect ratio of 1, about 1.10, about 1.15, about 1.20, about 1.25, about 1.30, about 1.35, about 1.40, or about 1.

45. DB1 / 158748174.5 34514. The plurality of substantially solid particles of any one of claims 1 to 13, wherein the substantially solid particles are substantially spherical.

15. The plurality of substantially solid particles of any one of claims 1 to 14, wherein the substantially solid particles are mesoporous.

16. The plurality of substantially solid particles of any one of claims 1 to 14, wherein the substantially solid particles have a BET (Brunauer–Emmett–Teller) surface area between about 2.50 m2 / g and about 6.50 m2 / g.

17. The plurality of substantially solid particles of any one of claims 1 to 14, wherein the substantially solid particles have a BET (Brunauer–Emmett–Teller) surface area of between about 2.50 m2 / g and about 3.00 m2 / g, about 3.00 m2 / g and about 3.50 m2 / g, about 3.50 m2 / g and about 4.00 m2 / g, about 4.00 m2 / g and about 4.50 m2 / g, about 4.50 m2 / g and about 5.00 m2 / g, about 5.00 m2 / g and about 5.50 m2 / g, about 5.50 m2 / g and about 6.00 m2 / g, or about 6.00 m2 / g and about 6.50 m2 / g.

18. The plurality of substantially solid particles of any one of claims 1 to 17, wherein the substantially solid particles have an average pore size between about 25 Å and about 500 Å.

19. The plurality of substantially solid particles of any one of claims 1 to 17, wherein the substantially solid particles have an average pore size of about 25 Å to about 30 Å, about 30 Å to about 35 Å, about 35 Å to about 40 Å, about 40 Å to about 45 Å, about 45 Å to about 50 Å, about 50 Å to about 55 Å, about 55 Å to about 60 Å, about 60 Å to about 65 Å, about 65 Å to about 70 Å, about 70 Å to about 75 Å, about 75 Å to about 80 Å, about 80 Å to about 85 Å, about 85 Å to about 90 Å, about 90 Å to about 95 Å, about 95 Å to about 100 Å, about 100 Å to about 105 Å, about 105 Å to about 110 Å, about 110 Å to about 115 Å, about 115 Å to about 120 Å, about 120 Å to about 125 Å, about 125 Å to about 130 Å, about 130 Å to about 135 Å, about 135 Å to about 140 Å, about 140 Å to about 145 Å, or about 145 Å to about 150 Å. DB1 / 158748174.5 34620. The plurality of substantially solid particles of any one of claims 1 to 19, wherein the substantially solid particles comprise a plurality of radially orientated microchannels.

21. The plurality of substantially solid particles of any one of claims 1 to 20, wherein the substantially solid particles further comprise an emulsifier, a surfactant, a buffering agent, an amino acid, or a sugar.

22. The plurality of substantially solid particles of any one of claims 1 to 20, wherein the substantially solid particles further comprise a polysaccharide, a polysorbate, a glycoside, PBS, arginine, trehalose, glucose, or sucrose.

23. The plurality of substantially solid particles of any one of claims 1 to 20, wherein the substantially solid particles further comprise a surfactant selected from sucrose ester, cetearyl glucoside, caprylyl / capryl glucoside, sucrose laurate, sucrose palmitate, sucrose stearate, sucrose cocoate, sorbitan monostearate, and combinations thereof.

24. The plurality of substantially solid particles of any one of claims 1 to 20, wherein the substantially solid particles further comprise an additional protein or peptide, a C12-C24 fatty alcohol, a glycolipid, or a lipid.

25. The plurality of substantially solid particles of any one of claims 1 to 20, wherein the substantially solid particles further comprise a protein, a peptide, a sugar surfactant, a biosurfactant, a lipid, or a combination.

26. The plurality of substantially solid particles of any one of claims 1 to 20, wherein the substantially solid particles further comprise a sugar fatty acid ester, a sugar fatty acid monoester, a sugar fatty diester, a sugar fatty triester, or a sugar fatty and polyester.

27. The plurality of substantially solid particles of any one of claims 1 to 20, wherein the substantially solid particles further comprise a sucrose fatty acid ester, a DB1 / 158748174.5 347sorbitan or sorbitol fatty acid ester, an alkyl glucoside, an alkyl polyglucoside, or a combination thereof.

28. The plurality of substantially solid particles of any one of claims 1 to 20, wherein the substantially solid particles further comprise KCl, NaCl, MgCl2, CaCl2, PBS, Tris, Polysorbate 20, Polysorbate 80, Capryl Glucoside, Sucrose, Histidine, Glycine, or Arginine.

29. A silk fibroin nanoclay composite or film, comprising silk fibroin fragments a clay, and a stabilizer wherein the % (w / w) of clay in the composite is from about 1% to about 99%.

30. The nanoclay composite or film of claim 29, wherein the clay is a bentonite clay.

31. The nanoclay composite or film of claim 29 or 30, wherein the concentration of clay in the composite or film is from about 20% (w / w) to about 33% (w / w), from about 33% (w / w) to about 50% (w / w), or from about 50% (w / w) to about 67% (w / w).

32. The nanoclay composite or film of any one of claims 29 to 31, wherein the silk fibroin particles comprise a pH modifier.

33. The nanoclay composite or film of claim 32, wherein the pH modifier is selected from sodium hydroxide and Ammonium hydroxide.

34. The nanoclay composite or film of claim 32 or 33, wherein the pH modifier is present in the pellet in an amount ranging from about 25 ppm to about 10,000.

35. The nanoclay composite or film of any one of claims 29 to 34, wherein the water vapor permeance (WVP) of the composite is inversely proportional to the concentration of clay in the composite.

36. The nanoclay composite or film of any one of claims 29 to 34, wherein water vapor permeance (WVP, g / m2*Pa*24h) of the composite is from about 0.20 to about DB1 / 158748174.5 3480.30, from about 0.30 to about 0.35, from about 0.35 to about 0.40, from about 0.40 to about 0.45, from about 0.45 to about 0.50, from about 0.50 to about 0.55, from about 0.55 to about 0.60, from about 0.60 to about 0.65, from about 0.65 to about 0.70, from about 0.70 to about 0.75, from about 0.75 to about 0.80, or from about 0.80 to about 0.

85.

37. A stabilized silk fibroin solution comprising silk fibroin fragments and a stabilizer, wherein: i) the solution has a z-average value lower than a substantially similar silk fibroin solution comprising silk fibroin fragments but excluding the stabilizer; and / or ii) the solution has a z-average plateau value lower than a substantially similar silk fibroin solution comprising silk fibroin fragments but excluding the stabilizer.

38. The stabilized silk fibroin solution of claim 37, wherein the z-average is measured after a period of time after the silk fibroin fragments and the stabilizer are co-formulated, wherein the period time ranges from 1 hour to 250 hours, from 1 hour to 350 hours, from 1 hour to 450 hours, from 1 hour to 550 hours, from 1 hour to 650 hours, or from 1 hour to 1000 hours.

39. The stabilized silk fibroin solution of claim 37, wherein the z-average is measured after a period of time after the silk fibroin fragments and the stabilizer are co-formulated, wherein the period time ranges from 1 minute to 10 minutes, from 1 minute to 20 minutes, from 1 minute to 30 minutes, from 1 minute to 40 minutes, from 1 minute to 50 minutes, from 1 minute to 60 minutes, from 1 minute to 70 minutes, or from 1 minute to 80 minutes.

40. The plurality of substantially solid particles of any one of claims 1 to 28, the nanoclay composite or film of any one of claims 29 to 34, or the stabilized silk fibroin solution of any one of claims 37 to 39, wherein the stabilizer is an emulsifier, a surfactant, a buffering agent, an amino acid, or a sugar.

41. The plurality of substantially solid particles of any one of claims 1 to 28, the nanoclay composite or film of any one of claims 29 to 34, or the stabilized silk fibroin DB1 / 158748174.5 349solution of any one of claims 37 to 39, wherein the stabilizer is a polysaccharide, a polysorbate, a glycoside, PBS, arginine, trehalose, glucose, or sucrose.

42. The plurality of substantially solid particles of any one of claims 1 to 28, the nanoclay composite or film of any one of claims 29 to 34, or the stabilized silk fibroin solution of any one of claims 37 to 39, wherein the stabilizer is a surfactant selected from sucrose ester, cetearyl glucoside, caprylyl / capryl glucoside, sucrose laurate, sucrose palmitate, sucrose stearate, sucrose cocoate, sorbitan monostearate, and combinations thereof.

43. The plurality of substantially solid particles of any one of claims 1 to 28, the nanoclay composite or film of any one of claims 29 to 34, or the stabilized silk fibroin solution of any one of claims 37 to 39, wherein the stabilizer is an additional protein or peptide, a C12-C24 fatty alcohol, a glycolipid, or a lipid.

44. The plurality of substantially solid particles of any one of claims 1 to 28, the nanoclay composite or film of any one of claims 29 to 34, or the stabilized silk fibroin solution of any one of claims 37 to 39, wherein the stabilizer is a protein, a peptide, a sugar surfactant, a biosurfactant, a lipid, or a combination.

45. The plurality of substantially solid particles of any one of claims 1 to 28, the nanoclay composite or film of any one of claims 29 to 34, or the stabilized silk fibroin solution of any one of claims 37 to 39, wherein the stabilizer is a sugar fatty acid ester, a sugar fatty acid monoester, a sugar fatty diester, a sugar fatty triester, or a sugar fatty and polyester.

46. The plurality of substantially solid particles of any one of claims 1 to 28, the nanoclay composite or film of any one of claims 29 to 34, or the stabilized silk fibroin solution of any one of claims 37 to 39, wherein the stabilizer is a sucrose fatty acid ester, a sorbitan or sorbitol fatty acid ester, an alkyl glucoside, an alkyl polyglucoside, or a combination thereof.

47. The plurality of substantially solid particles of any one of claims 1 to 28, the nanoclay composite or film of any one of claims 29 to 34, or the stabilized silk fibroin DB1 / 158748174.5 350solution of any one of claims 37 to 39, wherein the stabilizer is KCl, NaCl, MgCl2, CaCl2, PBS, Tris, Polysorbate 20, Polysorbate 80, Capryl Glucoside, Sucrose, Histidine, Glycine, or Arginine.

48. The plurality of substantially solid particles of any one of claims 1 to 28, the nanoclay composite or film of any one of claims 29 to 34, or the stabilized silk fibroin solution of any one of claims 37 to 47, wherein the solution is sprayable.

49. A liquid in air suspension comprising a plurality of droplets comprising the stabilized silk fibroin solution of claim 48, wherein the droplets are sufficiently stable after being sprayed, for a period of time necessary to reach a surface.

50. A plurality of drops or droplets comprising the stabilized silk fibroin solution of any one of claims 37 to 47, wherein the droplets or drops are sufficiently stable after being formed, for a period of time necessary to reach a surface.

51. The plurality of substantially solid particles of any one of claims 1 to 28, the silk fibroin nanoclay composite or film of any one of claims 29 to 36, the stabilized silk fibroin solution of any one of claims 37 to 48, the liquid in air suspension of claim 49, or the plurality of drops or droplets of claim 50, wherein the silk fibroin fragments have a weight average molecular weight selected from between about 1 kDa and about 5 kDa, from between about 5 kDa and about 10 kDa, from between about 6 kDa and about 17 kDa, from between about 10 kDa and about 15 kDa, from between about 14 kDa and about 30 kDa, from between about 15 kDa and about 20 kDa, from between about 17 kDa and about 39 kDa, from between about 20 kDa and about 25 kDa, from between about 25 kDa and about 30 kDa, from between about 30 kDa and about 35 kDa, from between about 35 kDa and about 40 kDa, from between about 39 kDa and about 54 kDa, from between about 39 kDa and about 80 kDa, from between about 40 kDa and about 45 kDa, from between about 45 kDa and about 50 kDa, from between about 50 kDa and about 55 kDa, from between about 55 kDa and about 60 kDa, from between about 60 kDa and about 100 kDa, from between about 80 kDa and about 144 kDa, from between about 144 kDa and about 250 kDa, or from between about 250 kDa and about 350 kDa, and a polydispersity from 1 to about 5. DB1 / 158748174.5 35152. The plurality of substantially solid particles, the silk fibroin nanoclay composite or film, the stabilized silk fibroin solution, the liquid in air suspension, or the plurality of drops or droplets, of claim 51, wherein the polydispersity is from 1 to about 1.5, from about 1.5 to about 2.0, from about 2.0 to about 2.5, from about 2.5 to about 3.0, from about 3.0 to about 3.5, from about 3.5 to about 4.0, from about 4.0 to about 4.5, or from about 4.5 to about 5.

0.

53. The plurality of substantially solid particles, the silk fibroin nanoclay composite or film, the stabilized silk fibroin solution, the liquid in air suspension, or the plurality of drops or droplets, of claim 51, further comprising about 0.001% (w / w) to about 10% (w / w) sericin relative to the silk fibroin fragments.

54. The plurality of substantially solid particles, the silk fibroin nanoclay composite or film, the stabilized silk fibroin solution, the liquid in air suspension, or the plurality of drops or droplets, of any one of claims 51 to 53, wherein the silk fibroin fragments do not spontaneously or gradually gelate and do not visibly change in color or turbidity when in an aqueous solution for at least 10 days prior to being formulated into the substantially solid particles, the silk fibroin nanoclay composite or film, or the stabilized silk fibroin solution.

55. The plurality of substantially solid particles of any one of claims 1 to 28, the silk fibroin nanoclay composite or film of any one of claims 29 to 36, the stabilized silk fibroin solution of any one of claims 37 to 48, the liquid in air suspension of claim 49, or the plurality of drops or droplets of claim 50, wherein the silk fibroin fragments comprise a plurality of amino acids selected from M, R, V, K, T, F, I, L, C, A, Q, Y, N, D, E, G, S, H, P, and W, wherein at least one of the amino acids is modified, substituted, or replaced.

56. The plurality of substantially solid particles, the silk fibroin nanoclay composite or film, the stabilized silk fibroin solution, the liquid in air suspension, or the plurality of drops or droplets, of claim 55, wherein the fibroin is a fibroin heavy chain, a fibroin light chain, or a fibrohexamerin. DB1 / 158748174.5 35257. The plurality of substantially solid particles, the silk fibroin nanoclay composite or film, the stabilized silk fibroin solution, the liquid in air suspension, or the plurality of drops or droplets, of claim 55 or 56, wherein a silk fibroin fragment comprises between about 2 and about 100 amino acids.

58. The plurality of substantially solid particles, the silk fibroin nanoclay composite or film, the stabilized silk fibroin solution, the liquid in air suspension, or the plurality of drops or droplets, of claim 55 to 57, wherein a silk fibroin fragment comprises between one and five modifications, substitutions, and / or replacements.

59. The plurality of substantially solid particles, the silk fibroin nanoclay composite or film, the stabilized silk fibroin solution, the liquid in air suspension, or the plurality of drops or droplets, of any one of claims 55 to 58, wherein a modification, substitution, and / or replacement is selected from an asparagine to aspartic acid modification, substitution, and / or replacement, a glutamine to glutamic acid modification, substitution, and / or replacement, and a methionine to methionine oxide modification, substitution, and / or replacement.

60. The plurality of substantially solid particles, the silk fibroin nanoclay composite or film, the stabilized silk fibroin solution, the liquid in air suspension, or the plurality of drops or droplets, of any one of claims 55 to 59, wherein the fibroin is a fibroin heavy chain, and wherein a modification, substitution, and / or replacement is at a position corresponding to any one position from 1 to 5263 of the fibroin heavy chain.

61. The plurality of substantially solid particles, the silk fibroin nanoclay composite or film, the stabilized silk fibroin solution, the liquid in air suspension, or the plurality of drops or droplets, of claim 60, wherein a modification, substitution, and / or replacement is at Q58, M64, N68, N70, N77, M80, N93, M103, Q125, N132, Q139, Q275, N4191, Q5216, and / or N5262.

62. The plurality of substantially solid particles, the silk fibroin nanoclay composite or film, the stabilized silk fibroin solution, the liquid in air suspension, or the plurality of drops or droplets, of any one of claims 55 to 59, wherein the fibroin is DB1 / 158748174.5 353a fibroin light chain, and wherein a modification, substitution, and / or replacement is at a position corresponding to any one position from 1 to 262 of the fibroin light chain.

63. The plurality of substantially solid particles, the silk fibroin nanoclay composite or film, the stabilized silk fibroin solution, the liquid in air suspension, or the plurality of drops or droplets, of claim 62, wherein a modification, substitution, and / or replacement is at N23, Q24, N28, M69, N105, N108, N118, N136, N138, Q149, N186, N200, Q202, N204, N240, N248, and / or Q255.

64. The plurality of substantially solid particles, the silk fibroin nanoclay composite or film, the stabilized silk fibroin solution, the liquid in air suspension, or the plurality of drops or droplets, of any one of claims 55 to 59, wherein the fibroin is a fibrohexamerin (p25), and wherein a modification, substitution, and / or replacement is at a position corresponding to any one position from 1 to 220 of the fibrohexamerin (p25).

65. The plurality of substantially solid particles, the silk fibroin nanoclay composite or film, the stabilized silk fibroin solution, the liquid in air suspension, or the plurality of drops or droplets, of claim 64, wherein a modification, substitution, and / or replacement is at Q62, N93, M120, N149, N172, N174, and / or N202.

66. The plurality of substantially solid particles, the silk fibroin nanoclay composite or film, the stabilized silk fibroin solution, the liquid in air suspension, or the plurality of drops or droplets, of any one of claims 55 to 65, wherein each modification, substitution, and / or replacement is independently ranging between about 1% to about 99% in the silk fibroin fragments portion of the substantially solid particles, the silk fibroin nanoclay composite or film, or the stabilized silk fibroin solution composition.

67. The plurality of substantially solid particles, the silk fibroin nanoclay composite or film, the stabilized silk fibroin solution, the liquid in air suspension, or the plurality of drops or droplets, of claim 67, wherein a % modification, substitution, and / or replacement is defined as (number of peptide or protein fragments comprising DB1 / 158748174.5 354a modification, substitution, and / or replacement at a specific position, divided by the total number of peptide or protein fragments which include the specific position, whether comprising a modification, substitution, and / or replacement, or not) x 100.

68. The plurality of substantially solid particles of any one of claims 1 to 28, the silk fibroin nanoclay composite or film of any one of claims 29 to 36, the stabilized silk fibroin solution of any one of claims 37 to 48, the liquid in air suspension of claim 49, or the plurality of drops or droplets of claim 50, wherein the silk fibroin fragments are included in one or more fractions, each fraction independently comprising a plurality of fibroin heavy chain fragments, a plurality of fibroin light chain fragments, and / or a plurality of fibrohexamerin (p25) fragments.

69. The plurality of substantially solid particles, the silk fibroin nanoclay composite or film, the stabilized silk fibroin solution, the liquid in air suspension, or the plurality of drops or droplets, of claim 68, wherein the silk fibroin fragments have a weight average molecular weight (Mw) selected from between about 1 kDa and about 20 kDa, from between about 20 kDa and about 40 kDa, from between about 40 kDa and about 60 kDa, from between about 60 kDa and about 80 kDa, from between about 80 kDa and about 100 kDa, from between about 100 kDa and about 120 kDa, from between about 120 kDa and about 140 kDa, or from between about 140 kDa and about 160 kDa, from between about 160 kDa and about 180 kDa, from between about 180 kDa and about 200 kDa, or from between about 200 kDa and about 250 kDa, and a polydispersity between 1 and about 1.

7.

70. The plurality of substantially solid particles, the silk fibroin nanoclay composite or film, the stabilized silk fibroin solution, the liquid in air suspension, or the plurality of drops or droplets, of claim 68, wherein the silk fibroin fragments have a weight average molecular weight (Mw) selected from between about 10 kDa and about 20 kDa, from between about 20 kDa and about 40 kDa, from between about 40 kDa and about 60 kDa, from between about 60 kDa and about 80 kDa, from between about 80 kDa and about 100 kDa, from between about 100 kDa and about 120 kDa, from between about 120 kDa and about 140 kDa, from between about 140 kDa and about 160 kDa, or from between about 160 kDa and about 180 kDa, and a polydispersity between 1 and about 1.1, or 1 and about 1.

2. DB1 / 158748174.5 35571. The plurality of substantially solid particles, the silk fibroin nanoclay composite or film, the stabilized silk fibroin solution, the liquid in air suspension, or the plurality of drops or droplets, of claim 68, wherein the silk fibroin fragments in a fraction have a weight average molecular weight (Mw) selected from between about 10 kDa and about 20 kDa, from between about 20 kDa and about 40 kDa, from between about 40 kDa and about 60 kDa, from between about 60 kDa and about 80 kDa, from between about 80 kDa and about 100 kDa, from between about 100 kDa and about 120 kDa, or from between about 120 kDa and about 140 kDa, and a polydispersity between 1 and about 1.1, or 1 and about 1.

2.

72. The plurality of substantially solid particles, the silk fibroin nanoclay composite or film, the stabilized silk fibroin solution, the liquid in air suspension, or the plurality of drops or droplets, of claim 68, wherein the silk fibroin fragments in a fraction have a weight average molecular weight (Mw) selected from between about 60 kDa and about 80 kDa, from between about 80 kDa and about 100 kDa, or from between about 100 kDa and about 120 kDa, and a polydispersity between 1 and about 1.

1.

73. The plurality of substantially solid particles, the silk fibroin nanoclay composite or film, the stabilized silk fibroin solution, the liquid in air suspension, or the plurality of drops or droplets, of claim 68, wherein the silk fibroin fragments in a fraction have a weight average molecular weight (Mw) selected from between about 10 kDa and about 20 kDa, from between about 20 kDa and about 40 kDa, from between about 40 kDa and about 60 kDa, from between about 60 kDa and about 80 kDa, from between about 80 kDa and about 100 kDa, or from between about 100 kDa and about 110 kDa, and a polydispersity between 1 and about 1.1, or 1 and about 1.

2.

74. The plurality of substantially solid particles, the silk fibroin nanoclay composite or film, the stabilized silk fibroin solution, the liquid in air suspension, or the plurality of drops or droplets, of claim 68, wherein the silk fibroin fragments in a fraction have a weight average molecular weight (Mw) selected from between about 60 kDa and about 80 kDa, from between about 80 kDa and about 100 kDa, from DB1 / 158748174.5 356between about 100 kDa and about 120 kDa, or from between about 120 kDa and about 140 kDa, and a polydispersity between 1 and about 1.

1.

75. The plurality of substantially solid particles, the silk fibroin nanoclay composite or film, the stabilized silk fibroin solution, the liquid in air suspension, or the plurality of drops or droplets, of claim 68, wherein the silk fibroin fragments in a fraction have a weight average molecular weight (Mw) selected from between about 20 kDa and about 40 kDa, or from between about 40 kDa and about 60 kDa, and a polydispersity between 1 and about 1.1, or 1 and about 1.

2.

76. The plurality of substantially solid particles, the silk fibroin nanoclay composite or film, the stabilized silk fibroin solution, the liquid in air suspension, or the plurality of drops or droplets, of claim 68, wherein the one or more fractions are selected from AS77, AS78, AS79, AS80, and AS81.

77. The plurality of substantially solid particles, the silk fibroin nanoclay composite or film, the stabilized silk fibroin solution, the liquid in air suspension, or the plurality of drops or droplets, of claim 68, wherein the one or more fractions are selected from AS82, AS83, AS84, AS85, AS86, AS87, AS88, and AS89.

78. The plurality of substantially solid particles, the silk fibroin nanoclay composite or film, the stabilized silk fibroin solution, the liquid in air suspension, or the plurality of drops or droplets, of claim 68, wherein the one or more fractions are selected from AS90, AS91, AS92, AS93, and AS94.

79. The plurality of substantially solid particles, the silk fibroin nanoclay composite or film, the stabilized silk fibroin solution, the liquid in air suspension, or the plurality of drops or droplets, of claim 68, wherein the one or more fractions are selected from AS95, AS96, AS97, AS98, AS99, and AS100.

80. The plurality of substantially solid particles, the silk fibroin nanoclay composite or film, the stabilized silk fibroin solution, the liquid in air suspension, or the plurality of drops or droplets, of claim 68, wherein the silk fibroin fragments have a weight average molecular weight (Mw) selected from between about 40 kDa and DB1 / 158748174.5 357about 60 kDa, from between about 60 kDa and about 80 kDa, from between about 80 kDa and about 100 kDa, from between about 100 kDa and about 120 kDa, from between about 120 kDa and about 140 kDa, from between about 140 kDa and about 160 kDa, from between about 160 kDa and about 180 kDa, from between about 180 kDa and about 200 kDa, or from between about 200 kDa and about 220 kDa, and a polydispersity between 1 and about 1.

7.

81. The plurality of substantially solid particles, the silk fibroin nanoclay composite or film, the stabilized silk fibroin solution, the liquid in air suspension, or the plurality of drops or droplets, of claim 68, wherein the silk fibroin fragments in a fraction have a weight average molecular weight (Mw) selected from between about 40 kDa and about 60 kDa, from between about 60 kDa and about 80 kDa, from between about 80 kDa and about 100 kDa, from between about 100 kDa and about 120 kDa, from between about 120 kDa and about 140 kDa, from between about 140 kDa and about 160 kDa, from between about 160 kDa and about 180 kDa, from between about 180 kDa and about 200 kDa, or from between about 200 kDa and about 210 kDa, and a polydispersity between 1 and about 1.2, or 1 and about 1.

3.

82. The plurality of substantially solid particles, the silk fibroin nanoclay composite or film, the stabilized silk fibroin solution, the liquid in air suspension, or the plurality of drops or droplets, of claim 68, wherein the silk fibroin fragments in a fraction have a weight average molecular weight (Mw) selected from between about 40 kDa and about 60 kDa, from between about 60 kDa and about 80 kDa, from between about 80 kDa and about 100 kDa, or from between about 100 kDa and about 110 kDa, and a polydispersity between 1 and about 1.1, or 1 and about 1.2 83. The plurality of substantially solid particles, the silk fibroin nanoclay composite or film, the stabilized silk fibroin solution, the liquid in air suspension, or the plurality of drops or droplets, of claim 68, wherein the silk fibroin fragments in a fraction have a weight average molecular weight (Mw) selected from between about 60 kDa and about 80 kDa, from between about 80 kDa and about 100 kDa, from between about 100 kDa and about 120 kDa, from between about 120 kDa and about 140 kDa, from between about 140 kDa and about 160 kDa, from between about 160 kDa and about 180 kDa, from between about 180 kDa and about 200 kDa, or from DB1 / 158748174.5 358between about 200 kDa and about 210 kDa, and a polydispersity between 1 and about 1.2, or 1 and about 1.

3.

84. The plurality of substantially solid particles, the silk fibroin nanoclay composite or film, the stabilized silk fibroin solution, the liquid in air suspension, or the plurality of drops or droplets, of claim 68, wherein the one or more fractions are selected from AS101, AS102, AS103, AS104, and AS105.

85. The plurality of substantially solid particles, the silk fibroin nanoclay composite or film, the stabilized silk fibroin solution, the liquid in air suspension, or the plurality of drops or droplets, of claim 68, wherein the one or more fractions are selected from AS106, AS107, AS108, AS109, AS110, and AS111.

86. The plurality of substantially solid particles, the silk fibroin nanoclay composite or film, the stabilized silk fibroin solution, the liquid in air suspension, or the plurality of drops or droplets, of any one of claims 68 to 85, wherein the silk fibroin fragments comprise one or more amino acid modifications, substitutions, or replacements of an amino acid is selected from M, R, V, K, T, F, I, L, C, A, Q, Y, N, D, E, G, S, H, P, and W.

87. The plurality of substantially solid particles, the silk fibroin nanoclay composite or film, the stabilized silk fibroin solution, the liquid in air suspension, or the plurality of drops or droplets, of any one of claims 68 to 86, wherein the silk fibroin fragments comprise between about 2 and about 100 amino acids.

88. The plurality of substantially solid particles, the silk fibroin nanoclay composite or film, the stabilized silk fibroin solution, the liquid in air suspension, or the plurality of drops or droplets, of claim 86 or 87, wherein a silk fibroin fragment comprise between one and five modifications, substitutions, and / or replacements.

89. The plurality of substantially solid particles, the silk fibroin nanoclay composite or film, the stabilized silk fibroin solution, the liquid in air suspension, or the plurality of drops or droplets, of any one of claims 86 to 88, wherein the fibroin is a fibroin heavy chain, and wherein a modification, substitution, and / or replacement is DB1 / 158748174.5 359at a position corresponding to any one position from 1 to 5263 of the fibroin heavy chain.

90. The plurality of substantially solid particles, the silk fibroin nanoclay composite or film, the stabilized silk fibroin solution, the liquid in air suspension, or the plurality of drops or droplets, of any one of claims 86 to 88, wherein the fibroin is a fibroin light chain, and wherein a modification, substitution, and / or replacement is at a position corresponding to any one position from 1 to 262 of the fibroin light chain.

91. The plurality of substantially solid particles, the silk fibroin nanoclay composite or film, the stabilized silk fibroin solution, the liquid in air suspension, or the plurality of drops or droplets, of any one of claims 86 to 88, wherein the fibroin is a fibrohexamerin (p25) chain, and wherein a modification, substitution, and / or replacement is at a position corresponding to any one position from 1 to 220 of the fibrohexamerin (p25) chain.

92. The plurality of substantially solid particles, the silk fibroin nanoclay composite or film, the stabilized silk fibroin solution, the liquid in air suspension, or the plurality of drops or droplets, of any one of claims 86 to 91, wherein a modification, substitution, and / or replacement is selected from an asparagine to aspartic acid modification, substitution, and / or replacement, a glutamine to glutamic acid modification, substitution, and / or replacement, and a methionine to methionine oxide modification, substitution, and / or replacement.

93. The plurality of substantially solid particles, the silk fibroin nanoclay composite or film, the stabilized silk fibroin solution, the liquid in air suspension, or the plurality of drops or droplets, of any one of claims 86 to 92, wherein a modification, substitution, and / or replacement is at fibroin heavy chain position selected from Q58, M64, N68, N70, N77, M80, N93, M103, Q125, N132, Q139, Q275, N4191, Q5216, and / or N5262.

94. The plurality of substantially solid particles, the silk fibroin nanoclay composite or film, the stabilized silk fibroin solution, the liquid in air suspension, or DB1 / 158748174.5 360the plurality of drops or droplets, of any one of claims 86 to 92, wherein a modification, substitution, and / or replacement is at fibroin light chain position selected from N23, Q24, N28, M69, N105, N108, N118, N136, N138, Q149, N186, N200, Q202, N204, N240, N248, and / or Q255.

95. The plurality of substantially solid particles, the silk fibroin nanoclay composite or film, the stabilized silk fibroin solution, the liquid in air suspension, or the plurality of drops or droplets, of any one of claims 86 to 92, wherein a modification, substitution, and / or replacement is at fibrohexamerin (p25) position selected from Q62, N93, M120, N149, N172, N174, and / or N202.

96. The plurality of substantially solid particles, the silk fibroin nanoclay composite or film, the stabilized silk fibroin solution, the liquid in air suspension, or the plurality of drops or droplets, of any one of claims 86 to 95, wherein each modification, substitution, and / or replacement is independently ranging in the composition between about 1% to about 99%.

97. The plurality of substantially solid particles, the silk fibroin nanoclay composite or film, the stabilized silk fibroin solution, the liquid in air suspension, or the plurality of drops or droplets, of claim 96, wherein the % modification, substitution, and / or replacement is defined as (number of peptide or protein fragments comprising a modification, substitution, and / or replacement at a specific position, divided by the total number of peptide or protein fragments which include the specific position, whether comprising a modification, substitution, and / or replacement, or not) x 100.

98. The plurality of substantially solid particles, the silk fibroin nanoclay composite or film, the stabilized silk fibroin solution, the liquid in air suspension, or the plurality of drops or droplets, of any one of claims 51 to 97, wherein a molecular weight is determined by MALS.

99. A pouch or a laundry pod comprising the plurality of substantially solid particles of any one of claims 1 to 98. DB1 / 158748174.5 361100. The laundry pod of claim 99, wherein the plurality of substantially solid particles are compressed in a multi-particulate puck.

101. The laundry pod of claim 99 or 100, further comprising a dissolvable enclosure comprising polyvinylalcohol (PVA) or a derivative of PVA.

102. The pouch of claim 99, further comprising an enclosure comprising one or more of nylon, polyglycolide (PGA), polylactic acid (PLA), poly(lactide-co- glycolide) (PLGA), polycaprolactone (PCL), poly(butylene succinate) (PBS), polybutylene succinate adipate, poly(p-dioxanone) (PPDO), poly(butylene adipate-co- terephthalate) (PBAT), a copolyester of terephthalic acid and lactic acid, a copolyester of terephthalic acid and glycolic acid, a copolyester of terephthalic acid and succinic acid, poly(hydroxybutyrate), poly(hydroxyvalerate), polyhydroxyhexanoate, a poly(hydroxyalkanoate) (PHA), polymethylene adipate / terephthalate.

103. A method of making the plurality of substantially solid particles of any one of claims 1 to 98, the method comprising dripping a solution comprising a plurality of the silk fibroin fragments into liquid nitrogen.

104. The method of claim 103, further comprising a lyophilization step.

105. The method of claim 103 or 104, wherein the concentration of silk fibroin fragments in the solution is from about 3% (w / w) to about 50% (w / w).

106. The method of any one of claims 103 to 105, wherein the silk fibroin fragments comprise one or more of a molecular weight, polydispersity, and / or a modification, substitution, and / or replacement at a specific amino acid position, as defined in any one of claims 51 to 97.

107. The method of any one of claims 103 to 106, wherein the solution is stabilized as defined in any one of claims 37 to 47. DB1 / 158748174.5 362108. A method of reconstituting a silk fibroin fragments solution comprising dissolving the plurality of substantially solid particles of any one of claims 1 to 28 in a solvent, wherein the particles have a reconstitution yield of more than 90%.

109. The plurality of substantially solid particles of any one of claims 1 to 28, wherein the particles have a reconstitution yield in DI water of more than 90%.

110. The method of claim 108, or the plurality of substantially solid particles of claim 109, wherein a reconstitution rate of at least 90% is preserved after a stability testing comprising simulated ageing of a plurality of substantially solid particles of any one of claims 1 to 28, the ageing comprising storage a temperature between about 40 °C and about 60 °C, for a period of time ranging from about 400 days to about 650 days.

111. The method of claim 110, wherein the simulated age ranges from about 4 years to about 15 years. DB1 / 158748174.5 363

Images