Composite polymeric materials, and products and methods of preparing the same

Abstract

The disclosure provides leather articles having composite layer coatings including optional mechanically engineered topographical features.

Description

COMPOSITE POLYMERIC MATERIALS, AND PRODUCTS AND METHODS OF PREPARING THE SAME FIELD The disclosure relates to composite polymeric materials, including in part a cellulose- derivative coating composition, optionally including silk fibroin proteins or fragments thereof and various additional agents, for coating various substrates. 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. Silk fibers are lightweight, breathable, and hypoallergenic. SUMMARY Embodiments of the present disclosure provide a composite comprising a first polymeric macromolecular species or polymer and a second polymeric macromolecular species or polymer. In some embodiments, a portion of the first polymeric macromolecular species or polymer and a portion of the second polymeric macromolecular species or polymer are physically and / or chemically entangled. In some embodiments, a portion of the first polymeric macromolecular species or polymer are physically and / or chemically crosslinked. In some embodiments, a portion of the second polymeric macromolecular species or polymer are physically and / or chemically crosslinked. In some embodiments, a portion of the first polymeric macromolecular species or polymer are chemically and / or physically integrated into a portion of the second polymeric macromolecular species or polymer. In some embodiments, a portion of the first polymeric macromolecular species or polymer and a portion of the second polymeric macromolecular species or polymer are not separable. In some embodiments, a portion of the first polymeric macromolecular species or polymer and / or a portion of the second polymeric macromolecular species or polymer are cross-linked. In some embodiments, a portion of the first polymeric macromolecular species or polymer and / or a portion of the second polymeric macromolecular species or polymer are partially organized and / or crystallized. In some embodiments, a portion of the first polymeric macromolecular species or polymer and a portion of the second polymeric macromolecular species or polymer cannot be delaminated. In some embodiments, aportion of the first polymeric macromolecular species or polymer and a portion of the second polymeric macromolecular species or polymer are self-assembled. In some embodiments, a portion of the first polymeric macromolecular species or polymer in the composite has a second structure different than a first structure of the first polymeric macromolecular species or polymer. In some embodiments, a portion of the second polymeric macromolecular species or polymer in the composite has a second structure different than a first structure of the second polymeric macromolecular species or polymer. In some embodiments, a portion of the first polymeric macromolecular species or polymer in the composite has a second structure different than a first structure of the first polymeric macromolecular species or polymer, and a portion of the second polymeric macromolecular species or polymer in the composite has a second structure different than a first structure of the second polymeric macromolecular species or polymer. In some embodiments, the first polymeric macromolecular species or polymer comprises a protein component. In some embodiments, the protein component comprises one or more of silk fibroin proteins or fragments, collagen, elastin, gelatin, corn zein, wheat gluten, pectin, chitin, casein, and / or whey. In some embodiments, the first polymeric macromolecular species or polymer comprises a biodegradable polymer. In some embodiments, the first polymeric macromolecular species or polymer comprises one or more of a polyurethane component. In some embodiments, the first polymeric macromolecular species or polymer comprises a poly lactic acid (PLA) component, a poly(lactic-co-glycolic acid) (PLGA) component, or both. In some embodiments, the second polymeric macromolecular species or polymer comprises a cellulose and / or cellulose derivative component. In some embodiments, the cellulose derivative is selected from methyl cellulose, ethyl cellulose, ethyl methyl cellulose, hydroxyethyl methyl cellulose, hydroxypropyl methyl cellulose, ethyl hydroxyethyl cellulose, cellulose triacetate, cellulose propionate, cellulose nitrate, cellulose sulfate, carboxymethyl cellulose, hydroxyethyl cellulose, hydroxypropyl cellulose, cellulose acetate, cellulose acetate propionate, cellulose acetate butyrate, and microcrystalline cellulose. In some embodiments, the cellulose derivative is ethyl cellulose. In some embodiments, the ethoxyl content in ethyl cellulose is from 45.0% to 49.5%, from 45.0% to 46.0%, from 45.0% to 47.0%, from 47.0% to 48.0%, or from 48.0% to 49.5%. In some embodiments, the degree of substitution of the ethyl cellulose is 0.5 to 1, 1 to 1.5, 1.5 to 2, 2 to 2.5, or 2.5 to 3. In some embodiments, a second structure of the cellulose derivative comprises a degree of crystallinity of less than 100%. In some embodiments, a second structure of thecellulose derivative comprises a degree of crystallinity of between about 5% and less than about 100%. In some embodiments, a second structure of the cellulose derivative comprises a degree of crystallinity of between about 10% and about 20%, between about 20% and about 30%, between about 30% and about 40%, between about 40% and about 50%, between about 50% and about 60%, between about 60% and about 70%, between about 70% and about 80%, between about 80% and about 90%, between about 90% and about 99%, or between about 90% and about 100%. In some embodiments, a second structure of the cellulose derivative comprises a degree of crystallinity of less than about 99%, less than about 98%, less than about 97%, less than about 96%, less than about 95%, less than about 94%, less than about 93%, less than about 92%, less than about 91%, less than about 90%, less than about 89%, less than about 88%, less than about 87%, less than about 86%, less than about 85%, less than about 84%, less than about 83%, less than about 82%, less than about 81%, less than about 80%, less than about 79%, less than about 78%, less than about 77%, less than about 76%, less than about 75%, less than about 74%, less than about 73%, less than about 72%, less than about 71%, less than about 70%, less than about 69%, less than about 68%, less than about 67%, less than about 66%, less than about 65%, less than about 64%, less than about 63%, less than about 62%, less than about 61%, less than about 60%, less than about 59%, less than about 58%, less than about 57%, less than about 56%, less than about 55%, less than about 54%, less than about 53%, less than about 52%, less than about 51%, less than about 50% less than about 49%, less than about 48%, less than about 47%, less than about 46%, less than about 45%, less than about 44%, less than about 43%, less than about 42%, less than about 41%, less than about 40%, less than about 39%, less than about 38%, less than about 37%, less than about 36%, less than about 35%, less than about 34%, less than about 33%, less than about 32%, less than about 31%, less than about 30% less than about 29%, less than about 28%, less than about 27%, less than about 26%, less than about 25%, less than about 24%, less than about 23%, less than about 22%, less than about 21%, less than about 20% less than about 19%, less than about 18%, less than about 17%, less than about 16%, less than about 15%, less than about 14%, less than about 13%, less than about 12%, less than about 11%, or less than about 10%. In some embodiments, the w / w ratio between the first polymeric macromolecular species or polymer and the second polymeric macromolecular species polymer in the composite is between about 1:100 and about 100:1. In some embodiments, the w / w ratio between the first polymeric macromolecular species or polymer and the second polymericmacromolecular species polymer in the composite is about 99:1, about 98:2, about 97:3, about 96:4, about 95:5, about 94:6, about 93:7, about 92:8, about 91:9, about 90:10, about 89:11, about 88:12, about 87:13, about 86:14, about 85:15, about 84:16, about 83:17, about 82:18, about 81:19, about 80:20, about 79:21, about 78:22, about 77:23, about 76:24, about 75:25, about 74:26, about 73:27, about 72:28, about 71:29, about 70:30, about 69:31, about 68:32, about 67:33, about 66:34, about 65:35, about 64:36, about 63:37, about 62:38, about 61:39, about 60:40, about 59:41, about 58:42, about 57:43, about 56:44, about 55:45, about 54:46, about 53:47, about 52:48, about 51:49, about 50:50, about 49:51, about 48:52, about 47:53, about 46:54, about 45:55, about 44:56, about 43:57, about 42:58, about 41:59, about 40:60, about 39:61, about 38:62, about 37:63, about 36:64, about 35:65, about 34:66, about 33:67, about 32:68, about 31:69, about 30:70, about 29:71, about 28:72, about 27:73, about 26:74, about 25:75, about 24:76, about 23:77, about 22:78, about 21:79, about 20:80, about 19:81, about 18:82, about 17:83, about 16:84, about 15:85, about 14:86, about 13:87, about 12:88, about 11:89, about 10:90, about 9:91, about 8:92, about 7:93, about 6:94, about 5:95, about 4:96, about 3:97, about 2:98, or about 1:99. In some embodiments, the w / w ratio between the first polymeric macromolecular species or polymer and the second polymeric macromolecular species polymer in the composite is about 10:1, about 10:2, about 10:3, about 10:4, about 10:5, about 10:6, about 10:7, about 10:8, about 10:9, or about 10:10. In some embodiments, the first polymeric macromolecular species or polymer is distributed isotropically over a cross section of the composite. In some embodiments, the first polymeric macromolecular species or polymer is distributed anisotropically over a cross section of the composite. In some embodiments, a concentration of the first polymeric macromolecular species or polymer closer to a first surface of the composite is higher than a concentration of the first polymeric macromolecular species or polymer closer to a second surface of the composite. In some embodiments, the first polymeric macromolecular species or polymer is substantially undetectable at a second surface of the composite. In some embodiments, the second polymeric macromolecular species or polymer is distributed isotropically over a cross section of the composite. In some embodiments, the second polymeric macromolecular species or polymer is distributed anisotropically over a cross section of the composite. In some embodiments, a concentration of the second polymeric macromolecular species or polymer closer to a second surface of the composite is higher than a concentration of the second polymeric macromolecular species or polymer closer to a first surface of the composite. In someembodiments, the second polymeric macromolecular species or polymer is substantially undetectable at a first surface of the composite substrate-coating interface. In some embodiments, a first surface of the composite is adhesive. In some embodiments, a second surface of the composite is adhesive. In some embodiments, a first surface of the composite is adhesive, and a second surface of the composite is adhesive. In some embodiments, a first surface of the composite is adhesive, and a second surface of the composite is non-adhesive. In some embodiments, the composite has an increased water resistance compared to one of: i) a non-composite material comprising the first polymeric macromolecular species or polymer, but excluding the second polymeric macromolecular species or polymer, ii) a non-composite material comprising the second polymeric macromolecular species or polymer, but excluding the first polymeric macromolecular species or polymer, or iii) a non-composite material comprising the first polymeric macromolecular species or polymer and the second polymeric macromolecular species or polymer, wherein the polymeric macromolecular species or polymers are not physically and / or chemically molecularly entangled. In some embodiments, the composite has an increased water vapor permeability compared to one of: i) a non-composite material comprising the first polymeric macromolecular species or polymer, but excluding the second polymeric macromolecular species or polymer, ii) a non-composite material comprising the second polymeric macromolecular species or polymer, but excluding the first polymeric macromolecular species or polymer, or iii) a non-composite material comprising the first polymeric macromolecular species or polymer and the second polymeric macromolecular species or polymer, wherein the polymeric macromolecular species or polymers are not physically and / or chemically molecularly entangled. Embodiments of the present disclosure provide an article comprising a substrate and a coating, the coating comprising the composite as described in any of the embodiments above. In some embodiments, the substrate comprises an irregular surface. In some embodiments, the coating has a thickness between about 10 µm and about 1000 µm. In some embodiments, the amount of coating on the substrate is between about 0.01 g / ft2and about 25 g / ft2. In some embodiments, the amount of first polymeric macromolecular species or polymer in the coating on the substrate is between about 0.001 g / ft2and about 20 g / ft2. In some embodiments, the amount of second polymeric macromolecular species or polymer in the coating on the substrate is between about 0.001 g / ft2and about 15 g / ft2. In some embodiments, the substrate comprises a substantially flexible material. In someembodiments, the substrate comprises a leather material or a textile material. In some embodiments, the substrate comprises one or more of collagen, cellulose, and / or lignin. Embodiments of the present disclosure provide a method of coating a substrate, the method comprising applying to a surface of the substrate a first composition comprising a first polymeric macromolecular species or polymer, and a second composition comprising a second polymeric macromolecular species or polymer. In some embodiments, the first composition comprises an unstructured first polymeric macromolecular species or polymer, or a first structure of the first polymeric macromolecular species or polymer. In some embodiments, the first polymeric macromolecular species or polymer comprises a protein component. In some embodiments, the protein component comprises one or more of silk fibroin proteins or fragments, collagen, elastin, gelatin, corn zein, wheat gluten, pectin, chitin, casein, and / or whey. In some embodiments, the first polymeric macromolecular species or polymer comprises a biodegradable polymer. In some embodiments, the first polymeric macromolecular species or polymer comprises one or more of a polyurethane component. In some embodiments, the first polymeric macromolecular species or polymer comprises a poly lactic acid (PLA) component, a poly(lactic-co-glycolic acid) (PLGA) component, or both. In some embodiments, the second composition comprises an unstructured second polymeric macromolecular species or polymer, or a first structure of the second polymeric macromolecular species or polymer. In some embodiments, the second polymeric macromolecular species or polymer comprises a cellulose and / or cellulose derivative component. In some embodiments, the cellulose derivative is selected from methyl cellulose, ethyl cellulose, ethyl methyl cellulose, hydroxyethyl methyl cellulose, hydroxypropyl methyl cellulose, ethyl hydroxyethyl cellulose, cellulose triacetate, cellulose propionate, cellulose nitrate, cellulose sulfate, carboxymethyl cellulose, hydroxyethyl cellulose, hydroxypropyl cellulose, cellulose acetate, cellulose acetate propionate, cellulose acetate butyrate, and microcrystalline cellulose. In some embodiments, the cellulose derivative is ethyl cellulose. In some embodiments, the ethoxyl content in ethyl cellulose is from 45.0% to 49.5%, from 45.0% to 46.0%, from 45.0% to 47.0%, from 47.0% to 48.0%, or from 48.0% to 49.5%. In some embodiments, the degree of substitution of the ethyl cellulose is 0.5 to 1, 1 to 1.5, 1.5 to 2, 2 to 2.5, or 2.5 to 3. In some embodiments, the cellulose derivative comprises a first structure of the cellulose derivative having a degree of crystallinity lower than a second structure of the cellulose derivative comprising a degree of crystallinity of between about 5% and less than about 100%. In some embodiments, the second composition comprising a second polymeric macromolecular species or polymer further comprises a solventcomponent. In some embodiments, the solvent component comprises an alcohol and / or an alcohol derivative. In some embodiments, the solvent component comprises one or more of an alcohol, an ether, a ketone, an aldehyde, and / or a ketal. In some embodiments, the solvent component is from about 75% w / w to about 99% w / w of the composition, from about 80% w / w to about 98% w / w of the composition, from about 85% w / w to about 97.5% w / w of the composition, or from about 85% w / w to about 95% w / w of the composition. In some embodiments, the solvent component comprises one or more of methanol, ethanol, n- propanol, 2-propanol, n-butanol, 2-butanol, pentanol, hexanol, acetone, butanone, methoxypropanol, di-isopropylidene glycerol, 2,2-dimethyl-4-hydroxymethyl-1,3-dioxolane, 2,2-dimethyl-1,3-dioxolane-4-methanol, or any combination thereof. In some embodiments, a first composition comprising a first polymeric macromolecular species or polymer further comprises one or more of a polyethylene glycol (PEG) component, a polypropylene glycol (PPG) component, and / or a polyether component. In some embodiments, a first composition comprising a first polymeric macromolecular species or polymer further comprises one or more of fatty acid or fatty acid derived amide, and / or a monoglyceride, diglyceride, and / or triglyceride. In some embodiments, a first composition comprising a first polymeric macromolecular species or polymer further comprises one or more of a triethylene glycol monomethyl ether component, a diethylene glycol butyl ether component, a diethylene glycol ethyl ether component, a dimethyl tetradecanedioate component, an erucamide component, and / or a glyceryl stearate component. In some embodiments, a first composition comprising a first polymeric macromolecular species or polymer comprises one or more of an isocyanate component, a polyol component, a blocked isocyanate component, and / or a blocked polyol component. In some embodiments, a first composition comprising a first polymeric macromolecular species or polymer comprises a partially polymerized, partially crosslinked, and / or partially cured polyurethane component. In some embodiments, a first composition comprising a first polymeric macromolecular species or polymer further comprises a polyurethane prepolymer component. In some embodiments, a first composition comprising a first polymeric macromolecular species or polymer further comprises water. In some embodiments, a surface of the substrate is coated first with the first composition comprising a first polymeric macromolecular species or polymer, and the coated with the second composition comprising a second polymeric macromolecular species or polymer. In some embodiments, the method further comprises a drying or partial drying step between the two coating steps. In some embodiments, the first composition comprising a first polymeric macromolecular species or polymer is only partially polymerized, partially dried, and / orpartially cured before the second composition comprising a second polymeric macromolecular species or polymer is applied. In some embodiments, the second composition comprising a second polymeric macromolecular species or polymer is applied at a temperature above a glass transition temperature (Tg) of the first polymeric macromolecular species or polymer. In some embodiments, the second composition comprising a second polymeric macromolecular species or polymer is applied at a temperature above a glass transition temperature (Tg) of the second polymeric macromolecular species or polymer. In some embodiments, the first composition comprising a first polymeric macromolecular species or polymer is applied one or more times at a rate from about 0.5 mL / ft2to about 5 mL / ft2. In some embodiments, the second composition comprising a second polymeric macromolecular species or polymer is applied one or more times at a rate from about 0.5 mL / ft2to about 5 mL / ft2. Embodiments of the present disclosure provide an article comprising a substrate and a coating, the article made by a method as described in any of the embodiments above. In some embodiments, the first polymeric macromolecular species or polymer is distributed isotropically over a cross section of the coating from a substrate-coating interface to an external surface of the coating. In some embodiments, the first polymeric macromolecular species or polymer is distributed anisotropically over a cross section of the coating from a substrate-coating interface to an external surface of the coating. In some embodiments, a concentration of the first polymeric macromolecular species or polymer closer to a substrate- coating interface is higher than a concentration of the first macromolecular species or polymer closer to an external surface of the coating. In some embodiments, the first polymeric macromolecular species or polymer is substantially undetectable at an external surface of the coating. In some embodiments, the second polymeric macromolecular species or polymer is distributed isotropically over a cross section of the coating from a substrate- coating interface to an external surface of the coating. In some embodiments, the second polymeric macromolecular species or polymer is distributed anisotropically over a cross section of the coating from a substrate-coating interface to an external surface of the coating. In some embodiments, a concentration of the second polymeric macromolecular species or polymer closer to a substrate-coating interface is lower than a concentration of the second polymeric macromolecular species or polymer closer to an external surface of the coating. In some embodiments, the second polymeric macromolecular species or polymer is substantially undetectable at a substrate-coating interface.Embodiments of the present disclosure provide a composite of any one of the preceding embodiments, or a method of making thereof, comprising a mattifying agent and / or a plasticizer described herein. Embodiments of the present disclosure provide an article of any one of the preceding embodiments, or a method of making thereof, comprising a mattifying agent and / or a plasticizer described herein. Embodiments of the present disclosure provide composite or an article of any one of the preceding claims, or a method of making thereof, comprising modified fibroin fragments described herein. Embodiments of the present disclosure provide a plurality of fibroin fragments are modified, each comprising one or more amino acid residue modifications selected from an asparagine to aspartic acid modification, a glutamine to glutamic acid modification, and a methionine to methionine oxide modification. Embodiments of the present disclosure provide a plurality of modified fibroin fragment comprises one modification. Embodiments of the present disclosure provide a plurality of modified fibroin fragment comprises two modifications. Embodiments of the present disclosure provide a plurality of modified fibroin fragment comprises three modifications. Embodiments of the present disclosure provide an asparagine to aspartic acid modification is at one or more positions selected from N23, N28, N108, N118, N136, N186, N200, N204, N240, N248, N68, N70, N77, N5262, N93, N132, N149, N172, N174, N202, N105, N4191, Embodiments of the present disclosure provide a glutamine to glutamic acid modification is at one or more positions selected from Q24, Q149, Q202, Q58, Q139, Q275, Q5216, Q255, and Q125. Embodiments of the present disclosure provide a methionine to methionine oxide modification is at the M64 position. Embodiments of the present disclosure provide each modification is independently ranging in the composition between about 1% to about 99%. Embodiments of the present disclosure provide a % modification is defined as (number of modified fibroin fragments having a modification at a specific position divided by the total number of modified fibroin fragments which include the specific position, modified or unmodified) x 100. Embodiments of the present disclosure provide a coating system for coating a leather article comprising a basecoat layer comprising one or more of a polyurethane dispersion (PUD), a protein component, and a solvent, and a topcoat layer comprising one or more of a polyurethane dispersion (PUD), a cellulose derivative, an alcohol solvent, and a glycerin derivative. In some embodiments, the cellulose derivative is selected from methyl cellulose, ethyl cellulose, ethyl methyl cellulose, hydroxyethyl methyl cellulose, hydroxypropyl methylcellulose, ethyl hydroxyethyl cellulose, cellulose triacetate, cellulose propionate, cellulose nitrate, cellulose sulfate, carboxymethyl cellulose, hydroxyethyl cellulose, hydroxypropyl cellulose, cellulose acetate, cellulose acetate propionate, cellulose acetate butyrate, and microcrystalline cellulose. In some embodiments, the cellulose derivative is ethyl cellulose. In some embodiments, the ethoxyl content in ethyl cellulose is from 45.0% to 49.5%, from 45.0% to 46.0%, from 45.0% to 47.0%, from 47.0% to 48.0%, or from 48.0% to 49.5%. In some embodiments, the degree of substitution of the ethyl cellulose is 0.5 to 1, 1 to 1.5, 1.5 to 2, 2 to 2.5, or 2.5 to 3. In some embodiments, a second structure of the cellulose derivative comprises a degree of crystallinity of less than 100%. In some embodiments, a second structure of the cellulose derivative comprises a degree of crystallinity of between about 5% and less than about 100%. In some embodiments, a second structure of the cellulose derivative comprises a degree of crystallinity of between about 10% and about 20%, between about 20% and about 30%, between about 30% and about 40%, between about 40% and about 50%, between about 50% and about 60%, between about 60% and about 70%, between about 70% and about 80%, between about 80% and about 90%, between about 90% and about 99%, or between about 90% and about 100%. In some embodiments, a second structure of the cellulose derivative comprises a degree of crystallinity of less than about 99%, less than about 98%, less than about 97%, less than about 96%, less than about 95%, less than about 94%, less than about 93%, less than about 92%, less than about 91%, less than about 90%, less than about 89%, less than about 88%, less than about 87%, less than about 86%, less than about 85%, less than about 84%, less than about 83%, less than about 82%, less than about 81%, less than about 80%, less than about 79%, less than about 78%, less than about 77%, less than about 76%, less than about 75%, less than about 74%, less than about 73%, less than about 72%, less than about 71%, less than about 70%, less than about 69%, less than about 68%, less than about 67%, less than about 66%, less than about 65%, less than about 64%, less than about 63%, less than about 62%, less than about 61%, less than about 60%, less than about 59%, less than about 58%, less than about 57%, less than about 56%, less than about 55%, less than about 54%, less than about 53%, less than about 52%, less than about 51%, less than about 50% less than about 49%, less than about 48%, less than about 47%, less than about 46%, less than about 45%, less than about 44%, less than about 43%, less than about 42%, less than about 41%, less than about 40%, less than about 39%, less than about 38%, less than about 37%, less than about 36%, less than about 35%, less than about 34%, less than about 33%, less than about 32%, less than about 31%, less than about 30% less than about 29%, less than about 28%, less than about 27%, less than about 26%, less than about25%, less than about 24%, less than about 23%, less than about 22%, less than about 21%, less than about 20% less than about 19%, less than about 18%, less than about 17%, less than about 16%, less than about 15%, less than about 14%, less than about 13%, less than about 12%, less than about 11%, or less than about 10%. In some embodiments, the protein component comprises one or more of silk fibroin proteins or fragments, collagen, elastin, gelatin, corn zein, wheat gluten, pectin, chitin, casein, and / or whey. In some embodiments, the alcohol solvent is methanol, ethanol, acetone, isopropanol, n-Butanol, or a combination thereof. In some embodiments, the coating has a thickness between about 10 µm and about 1000 µm. In some embodiments, wherein the amount of coating on the substrate is between about 0.01 g / ft2 and about 25 g / ft2. Embodiments of the present disclosure provide a method of coating a leather article, the method comprising applying to a surface of the leather a basecoat layer comprising one or more of a polyurethane dispersion (PUD), a protein component, and a solvent, and a topcoat layer comprising one or more of a polyurethane dispersion (PUD), a cellulose derivative, an alcohol solvent, and a glycerin derivative. In some embodiments, the cellulose derivative is selected from methyl cellulose, ethyl cellulose, ethyl methyl cellulose, hydroxyethyl methyl cellulose, hydroxypropyl methyl cellulose, ethyl hydroxyethyl cellulose, cellulose triacetate, cellulose propionate, cellulose nitrate, cellulose sulfate, carboxymethyl cellulose, hydroxyethyl cellulose, hydroxypropyl cellulose, cellulose acetate, cellulose acetate propionate, cellulose acetate butyrate, and microcrystalline cellulose. In some embodiments, the cellulose derivative is ethyl cellulose. In some embodiments, the ethoxyl content in ethyl cellulose is from 45.0% to 49.5%, from 45.0% to 46.0%, from 45.0% to 47.0%, from 47.0% to 48.0%, or from 48.0% to 49.5%. In some embodiments, the degree of substitution of the ethyl cellulose is 0.5 to 1, 1 to 1.5, 1.5 to 2, 2 to 2.5, or 2.5 to 3. In some embodiments, a second structure of the cellulose derivative comprises a degree of crystallinity of less than 100%. In some embodiments, a second structure of the cellulose derivative comprises a degree of crystallinity of between about 5% and less than about 100%. In some embodiments, a second structure of the cellulose derivative comprises a degree of crystallinity of between about 10% and about 20%, between about 20% and about 30%, between about 30% and about 40%, between about 40% and about 50%, between about 50% and about 60%, between about 60% and about 70%, between about 70% and about 80%, between about 80% and about 90%, between about 90% and about 99%, or between about 90% and about 100%. In some embodiments, a second structure of the cellulose derivative comprises a degree of crystallinity of less than about 99%, less than about 98%, less than about 97%, less thanabout 96%, less than about 95%, less than about 94%, less than about 93%, less than about 92%, less than about 91%, less than about 90%, less than about 89%, less than about 88%, less than about 87%, less than about 86%, less than about 85%, less than about 84%, less than about 83%, less than about 82%, less than about 81%, less than about 80%, less than about 79%, less than about 78%, less than about 77%, less than about 76%, less than about 75%, less than about 74%, less than about 73%, less than about 72%, less than about 71%, less than about 70%, less than about 69%, less than about 68%, less than about 67%, less than about 66%, less than about 65%, less than about 64%, less than about 63%, less than about 62%, less than about 61%, less than about 60%, less than about 59%, less than about 58%, less than about 57%, less than about 56%, less than about 55%, less than about 54%, less than about 53%, less than about 52%, less than about 51%, less than about 50% less than about 49%, less than about 48%, less than about 47%, less than about 46%, less than about 45%, less than about 44%, less than about 43%, less than about 42%, less than about 41%, less than about 40%, less than about 39%, less than about 38%, less than about 37%, less than about 36%, less than about 35%, less than about 34%, less than about 33%, less than about 32%, less than about 31%, less than about 30% less than about 29%, less than about 28%, less than about 27%, less than about 26%, less than about 25%, less than about 24%, less than about 23%, less than about 22%, less than about 21%, less than about 20% less than about 19%, less than about 18%, less than about 17%, less than about 16%, less than about 15%, less than about 14%, less than about 13%, less than about 12%, less than about 11%, or less than about 10%. In some embodiments, the protein component comprises one or more of silk fibroin proteins or fragments, collagen, elastin, gelatin, corn zein, wheat gluten, pectin, chitin, casein, and / or whey. In some embodiments, the alcohol solvent is methanol, ethanol, acetone, isopropanol, n-Butanol, or a combination thereof. In some embodiments, the coating has a thickness between about 10 µm and about 1000 µm. In some embodiments, the amount of coating on the substrate is between about 0.01 g / ft2 and about 25 g / ft2. 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 is a flow chart showing various embodiments for producing pure silk fibroin-based protein fragments (SPFs) of the present disclosure.Figure 2 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. Figure 3 illustrates general steps used in leather processing. Figure 4 is a photograph of the felt pads (and associated leather samples) after 600 continuous cycles of Wet Veslic Rubbing, comparing silk fibroin fragment compositions (bottom sample – Entry B2) treated leather samples to polyurethane (top 2 samples) treated leather samples. Note the damage to the polyurethane samples and loss of dye from the leather to the felt after 600 cycles). Figure 5 is a photograph of the felt pads after 10 cycles of Wet Veslic Rubbing on Entries A1, A2, B1 and B2 (Table 1) treated leather samples. Figure 6 is a photograph of water droplets placed on samples treated either with silk fibroin fragments or a crosslinked polyurethane coating system after Wet Veslic Rubbing has been performed. In the case of silk fibroin fragments (Entry B2), the sample was exposed to 600 cycles of rubbing whereas the polyurethane samples only endured 10 cycles. The photograph was taken 5 minutes after placing the water droplets. Note the penetration of water into the leather matrix when using the commercial reference systems designed as top- coats. Figure 7A-7B is a graphical analysis illustrating the results of Water Vapor Transmission Test #1 on coated leather (7A) and uncoated leather (7B). Figure 8A-8B is a graphical analysis illustrating the results of Water Vapor Transmission Test #2 on coated leather (8A) and uncoated leather (8B). Figure 9A-9B is a graphical analysis illustrating the results of Water Vapor Transmission Test #3 on coated leather (9A) and uncoated leather (9B). Figure 10 is photographs of uncoated plain leather. Figure 11 show an FTIR analysis of uncoated plain leather. Figure 12 is photographs of leather treated with an adhesive coating of a coating system disclosed herein. Figure 13 shows an FTIR analysis of leather treated with an adhesive coating of a coating system disclosed herein. Figure 14A is photographs of treated leather finished with a top coat of a coating system disclosed herein. Figure 14B shows an FTIR analysis of treated leather finished with a top coat of a coating system disclosed herein.Figure 15A is an IR Spectra of leather samples treated with a coating system disclosed herein by LN-MCT Detector. Figure 15B shows Macro ATR Imaging of a leather sample treated with an adhesive base coat of a coating system disclosed herein. Figure 15C shows Macro ATR Imaging of a leather sample treated with a top coat of a coating system disclosed herein. Figures 16A- 16H are photographs illustrating the results of the soil release test with various stain sources on leather treated with a coating system disclosed herein.16A: Mud, 16B: Water, 16C: Mustard, 16D: Corn Oil, 16E: Wine, 16F: Ketchup, 16G: French Dressing, 16H: Coffee. Figure 17A- 17C are photographs of the leather samples treated with a coating system disclosed herein used in the Industrialization Trial. Figure 18A- 18I are photographs of the felt pads (and associated leather samples treated with a coating system disclosed herein) after 600 continuous cycles of Wet Veslic Rubbing (Note: Fig.18H was only subject to 360 cycles). Figure 19A- 19D are photographs illustrating the results of a Bally Flex Test conducted on various leather samples treated with a coating system disclosed herein. Figure 20A- 20I are photographs illustrating the results of an Adhesive Tape Test conducted on various leather samples treated with an adhesive coating system. Figure 21 is a photograph illustrating the difference between leather samples treated with an adhesive coating system disclosed herein before and after milling. Figures 22A- 22I are photographs illustrating the results of an Adhesive Tape Test conducted on various leather samples treated with an adhesive coating system disclosed herein. Figure 23 is a photograph illustrating the difference between leather samples treated with an adhesive coating system disclosed herein before and after milling. Figure 24A- 24B are photographs illustrating the difference in an Adhesive Tape Test conducted on a leather sample treated with an adhesive coating system disclosed herein before and after milling. Figure 25A- 25C are microscopic cross-sectional images of a leather surface treated with a coating system disclosed herein. Figure 26A- 26C are microscopic top view images of a leather surface treated with a coating system disclosed herein.Figure 27A- 27C are images showing a wet blue leather strip treated with a coating system disclosed herein under a digital microscope.27A: side view, 27B: top grain view, 27C: flesh view. Figure 28A- 28C are images showing a paper strip treated with a coating system disclosed herein under a digital microscope.28A: top view, 28B: side view, 28C: back view. Figure 29A- 29C are images showing a fabric strip treated with a coating system disclosed herein under a digital microscope.29A: top view, 29B: side view, 29C: back view. Figure 30A- 30C are images showing a fabric strip with blue tape treated with a coating system disclosed herein under a digital microscope.30A: top view, 30B: side view, 30C: back view. Figure 31 shows pictures of AS-104 + 2% Glycerol + 50 mM magnesium sulfate films tensile testing process. Figure 32 shows proposed formulation mechanism incorporating AS-104, 2% glycerol and salts at various concentrations. Figure 33A shows elongation at break of AS-104, 2% glycerol and guanidinium hydrochloride (5, 10, 25 and 50 mM). Figure 33B shows ultimate tensile strength of AS-104, 2% glycerol and guanidinium hydrochloride (5, 10, 25 and 50 mM). Figure 34A shows elongation at break of AS-104, 2% glycerol and sodium chloride (5, 10, 25 and 50 mM). Figure 34B shows ultimate tensile strength of AS-104, 2% glycerol and sodium chloride (5, 10, 25 and 50 mM). Figure 35A shows elongation at break of AS-104, 2% glycerol and urea (5, 10, 25 and 50 mM). Figure 35B shows ultimate tensile strength of AS-104, 2% glycerol and urea (5, 10, 25 and 50 mM). Figure 36A shows elongation at break of AS-104, 2% glycerol and L-Arginine hydrochloride (5, 10, 25 and 50 mM). Figure 36B shows ultimate tensile strength of AS-104, 2% glycerol and L-Arginine hydrochloride (5, 10, 25 and 50 mM). Figure 37A shows elongation at break of AS-104, 2% glycerol and magnesium sulfate heptahydrate (5, 10, 25 and 50 mM). Figure 37B shows ultimate tensile strength of AS-104, 2% glycerol and magnesium sulfate heptahydrate (5, 10, 25 and 50 mM).Figure 38A shows elongation at break of AS-104, 2% glycerol and ammonium sulfate (5, 10, 25 and 50 mM). Figure 38B shows ultimate tensile strength of AS-104, 2% glycerol and ammonium sulfate (5, 10, 25 and 50 mM). Figure 39A shows elongation at break of AS-104, 2% glycerol and calcium chloride (5, 10, 25 and 50 mM). Figure 39B shows ultimate tensile strength of AS-104, 2% glycerol and calcium chloride (5, 10, 25 and 50 mM). Figure 40A shows elongation at break of AS-104, 2% glycerol and magnesium chloride (5, 10, 25 and 50 mM). Figure 40B shows ultimate tensile strength of AS-104, 2% glycerol and magnesium chloride (5, 10, 25 and 50 mM). Figure 41A shows elongation at break of AS-104, 2% glycerol and calcium sulfate dihydrate (5, 10, 25 and 50 mM). Figure 41B shows ultimate tensile strength of AS-104, 2% glycerol and calcium sulfate dihydrate (5, 10, 25 and 50 mM). Figure 42A shows elongation at break of AS-104, 2% glycerol and calcium lactobionate (5, 10, 25 and 50 mM). Figure 42B shows ultimate tensile strength of AS-104, 2% glycerol and calcium lactobionate (5, 10, 25 and 50 mM). Figure 43 compiles all data on elongation at break. Figure 44 compiles all data on ultimate tensile strength. Figure 45 shows Veslic wet and dry testing results of Bodin Basic Black leather coated with 17% AS-104-5% Melio-9S11, 17% AS-104-5% Melio-9S11-10 mM CaCl2, 17% AS-104-5% Melio-9S11-50 mM MgSO4 and 17% AS-104-5% Melio-9S11-25 mM L- Arginine hydrochloride Figure 46 shows Veslic wet and dry Testing results of Bodin Brown leather coated with 17% AS-104-5% Melio-9S11, 17% AS-104-5% Melio-9S11-10 mM CaCl2, 17% AS- 104-5% Melio-9S11-50 mM MgSO4 and 17% AS-104-5% Melio-9S11-25 mM L-Arginine hydrochloride Figure 47 shows Veslic scores for Bodin Basic Black leather coated with 17% AS- 104-5% Melio-9S11, 17% AS-104-5% Melio-9S11-10 mM CaCl2, 17% AS-104-5% Melio- 9S11-50 mM MgSO4 and 17% AS-104-5% Melio-9S11-25 mM L-Arginine hydrochlorideFigure 48 shows Veslic scores for Bodin Brown leather coated with 17% AS-104-5% Melio-9S11, 17% AS-104-5% Melio-9S11-10 mM CaCl2, 17% AS-104-5% Melio-9S11-50 mM MgSO4 and 17% AS-104-5% Melio-9S11-25 mM L-Arginine hydrochloride Figure 49A and 49B illustrate before and after topography traces of a leather sample coated with GG- silk before (FIG.23A) and after (FIG.23B) coating with Silk + 0.5% wt. GG via point filling. Traces were captured using a Taylor Hobson CCI HD optical profilometer. Figure 50 shows a schematic of the preparation of a 2-part matting agent system. Figure 51A shows gray, brown, and black leathers with CAP-7. Figure 51B shows gray, brown, and black leathers with MHG. Figure 51C shows gray, brown, and black leathers with DPGDB. Figure 52 shows weight of the coated sample versus the diameter of the spray nozzle. Figure 53A shows 2.5% concentration ethyl cellulose in methoxy propanol on leather (not milled crust). Figure 53B shows 2.5% concentration ethyl cellulose in methoxy propanol on milled crust leather. Figure 53C shows 5% concentration ethyl cellulose in methoxy propanol on leather (not milled crust). Figure 53D shows 5% concentration ethyl cellulose in methoxy propanol on milled crust leather. Figure 53E shows 7% concentration ethyl cellulose in methoxy propanol on leather (not milled crust). Figure 53F shows 7% concentration ethyl cellulose in methoxy propanol on milled crust leather. Figure 54 shows test results from Formulation A matte testing. Figure 55A shows samples of Euroleather (top) and Fragopel (bottom) with Formulation A before ironing. Figure 55B shows samples of Euroleather (top) and Fragopel (bottom) with Formulation A before ironing. Figure 55C shows samples of Euroleather (top) and Fragopel (bottom) with Formulation A before ironing. Figure 55D shows samples of Euroleather (top) and Fragopel (bottom) with Formulation A before ironing.Figure 55E shows samples of Euroleather (top) and Fragopel (bottom) with Formulation A before ironing. Figure 55F shows samples of Euroleather (top) and Fragopel (bottom) with Formulation A before ironing. Figure 55G shows samples of Euroleather (top) and Fragopel (bottom) with Formulation A before ironing. Figure 55H shows samples of Euroleather (top) and Fragopel (bottom) with Formulation A after ironing. Figure 55I shows samples of Euroleather (top) and Fragopel (bottom) with Formulation A after ironing. Figure 55J shows samples of Euroleather (top) and Fragopel (bottom) with Formulation A after ironing. Figure 55K shows samples of Euroleather (top) and Fragopel (bottom) with Formulation A after ironing. Figure 55L shows samples of Euroleather (top) and Fragopel (bottom) with Formulation A after ironing. Figure 55M shows samples of Euroleather (top) and Fragopel (bottom) with Formulation A after ironing. Figure 55N shows samples of Euroleather (top) and Fragopel (bottom) with Formulation A after ironing. Figure 56A shows samples of Fragopel with Formulation A after (top) and before (bottom) milling. Figure 56B shows samples of Fragopel with Formulation A after (top) and before (bottom) milling. Figure 56C shows samples of Fragopel with Formulation A after (top) and before (bottom) milling. Figure 56D shows samples of Fragopel with Formulation A after (top) and before (bottom) milling. Figure 56E shows samples of Fragopel with Formulation A after (top) and before (bottom) milling. Figure 56F shows samples of Fragopel with Formulation A after (top) and before (bottom) milling. Figure 56G shows samples of Fragopel with Formulation A after (top) and before (bottom) milling.Figure 56H shows samples of Euroleather with Formulation A after (top) and before (bottom) milling. Figure 56I shows samples of Euroleather with Formulation A after (top) and before (bottom) milling. Figure 56J shows samples of Euroleather with Formulation A after (top) and before (bottom) milling. Figure 56K shows samples of Euroleather with Formulation A after (top) and before (bottom) milling. Figure 56L shows samples of Euroleather with Formulation A after (top) and before (bottom) milling. Figure 56M shows samples of Euroleather with Formulation A after (top) and before (bottom) milling. Figure 56N shows samples of Euroleather with Formulation A after (top) and before (bottom) milling. Figure 57A shows samples of Euroleather (left) and Fracopel (right) with Formulations A, B, C, and D before ironing. Figure 57B shows samples of Euroleather (left) and Fracopel (right) with Formulations A, B, C, and D before ironing. Figure 57C shows samples of Euroleather (left) and Fracopel (right) with Formulations A, B, C, and D before ironing. Figure 57D shows samples of Euroleather (left) and Fracopel (right) with Formulations A, B, C, and D before ironing. Figure 57E shows samples of Euroleather (left) and Fracopel (right) with Formulations A, B, C, and D after ironing. Figure 57F shows samples of Euroleather (left) and Fracopel (right) with Formulations A, B, C, and D after ironing. Figure 57G shows samples of Euroleather (left) and Fracopel (right) with Formulations A, B, C, and D after ironing. Figure 57H shows samples of Euroleather (left) and Fracopel (right) with Formulations A, B, C, and D after ironing. Figure 57I shows samples of Euroleather (left) and Fracopel (right) with Formulations A, B, C, and D after ironing (top) and after milling (bottom). Figure 57J shows samples of Euroleather (left) and Fracopel (right) with Formulations A, B, C, and D after ironing (top) and after milling (bottom).Figure 57K shows samples of Euroleather (left) and Fracopel (right) with Formulations A, B, C, and D after ironing (top) and after milling (bottom). Figure 57L shows samples of Euroleather (left) and Fracopel (right) with Formulations A, B, C, and D after ironing (top) and after milling (bottom). Figure 58A shows a vulcanization test after 2hrs @130C, which passes with a color change of 4 / 5. Figure 58B shows a sample forgotten in the oven after the vulcanization test overnight, which still passes with a color change of 4 / 5. Figure 59A shows finishing resistance when handling leather after spraying and before ironing of 072-1. Figure 59B shows finishing resistance when handling leather after spraying and before ironing of 072-2. Figures 59C shows finishing resistance when handling leather after spraying and before ironing of 072-3. Figure 60 shows IR spectra of the samples by LN-MCT detector. Figure 61 shows macro ATR imaging of the sample with an adhesive base coat. Figure 62 shows macro ATR imaging of the sample with the top coat. Figure 63 shows a cross-section of uncoated leather. Unevenness on the surface is visible. Figure 64 shows a cross-section of basecoat coated leather. Figure 65 shows coated leather with L1 system. Figure 66 shows further magnification of silver tagged silk in L1 system. Basecoat / topcoat composite indicated by silver tagged silk throughout the coating. Figure 67 shows a schematic of the layers formed. Figure 68. 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 69. 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 theUV-280 absorbance becomes less than 200 AU. The captured negatively charged silk / modified polypeptides are eluted with high salt concentration (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 70. 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. Figure 71. Analytical Size Exclusion Chromatography of the Low and Mid skid silk / modified peptide compositions and their components (see table 80 for more details). A, Molecular weight of the various Activated Silk new compositions described in this study. B, 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 80 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 80 for details). Figure 72. 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. Figure 73. Self-assembly reactions of the of the Low and Mid skid silk / modified peptide compositions and their components (see table 80 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. Figure 74. Self-assembly kinetics of the Low and Mid skid silk / modified peptide compositions and their components (see table 80 for more details). A, the Self-assembly Rate Factor shows how fast the self-assembly reaction proceeds once it is initiated and the self- assembly nuclei are organized. B, Maximum Gel Yield shows how dense the silk gel is after self-assembly is complete. C, Time required for the self-assembly reaction to produce half of the maximum gel amount. Figure 75. the Low and Mid skid silk / modified peptide compositions and their components (see table 80 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 76 is a graph of molecular weight plotted as a function of time for solubilized fibroin in 9.3 M LiBr at 100° C - 103° C. Figure 77 is a graph of molecular weight plotted as a function of time for solubilized fibroin in 9.3 M LiBr at 122° C - 125° C. Figure 78 is a graph illustrating percentage of amino acid modification in silk. Figures 79A-79C are graphs illustrating percentage of amino acid modifications in Low and Mid Skid silk. Fig.79A illustrates heavy chain modifications, Fig.79B illustrates light chain modifications, and Fig.79C illustrates fibrohexamerin modifications. N are Asparagines that become aspartic acid and Q are Glutamines that become deamidated. M corresponds to Methionies that become oxidized. Figures 80A- 80B are graphs illustrating percentage of amino acid modifications in Low and Mid Skid silk produced and lyophilized. Fig.80A illustrates heavy chain modifications and Fig.80B 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. Figures 81A- 81B are graphs illustrating percentage of amino acid modifications in Low Skid silk produced in two different facilities. Fig.81A illustrates heavy chain modifications and Fig.81B 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. Figure 82 are graphs illustrating percentage of amino acid modifications in Mid silk produced in Skid and Benchtop scale. N are Asparagines that become aspartic acid and Q are Glutamines that become deamidated. M corresponds to Methionies that become oxidized. Figure 83 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 84 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 85A and 85B 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.85A: 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 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.85B: 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 86A and 86B illustrates the Analytical Size Exclusion Chromatography of Low Skid silk / modified silk compositions and their constituent AS compositions. Fig.86A. Average molecular weight in kDa of Low Skid silk (LS) and AS77-AS81 are shown. Fig. 86B. Polydispersity (PDI) measurements are shown. The numerical data is presented in Table 86. Figure 87 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 88A and 88B 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.88A. 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 is3.668 h, and the FSAF is 3.08 (Abs / min). Fig.88B. 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 89A and 89B 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.89A. Illustrates intensity diameter particle size distribution measured for silk compositions AS77, AS78, AS79, AS80, and AS81. Fig.9B. Illustrate correlogram functions of silk compositions AS77, AS78, AS79, AS80, AS81. Figure 90 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 91 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 92A and 92B illustrate Analytical Size Exclusion Chromatography of Low Skid silk / modified silk compositions and their constituent AS compositions. Fig.92A. Illustrates average molecular weight in kDa of Low Skid silk (LS) and AS82-AS89 are shown. Fig.92B. Polydispersity (PDI) measurements are shown. The numerical data is presented in Table 88. Figure 93 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 94A and 94B 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.94A. 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.94B. 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 95A- 5C are graphs showing 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 particle size of each silk composition. Fig.95A. Shows intensity particle size distribution measured for silk compositions AS82, AS83, AS84, AS85, AS86, AS87, AS88, and AS89. Fig.95B. 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.95C. 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 96 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 negativelycharged 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 97A- 97E are chromatograms of anion exchange chromatography, hydrophobic interactions chromatography, and the following size exclusion chromatography of Low Skid silk / modified polypeptide compositions. Fig.97A. 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 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.97B. 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.97C. 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.97D. 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.97E. 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 98A- 98B are graphs showing analytical Size Exclusion Chromatography of Low Skid silk / modified silk compositions and their constituent AS compositions. Fig.98A. Average molecular weight in kDa of Low Skid silk (LS) and AS90-AS100 are shown. Fig.98B. Polydispersity (PDI) measurements are shown. The numerical data is presented in Table 90Figures 99A- 99B are SDS polyacrylamide gel electrophoresis of Low Skid silk / modified polypeptide compositions. Fig.99A. Q-HIC(elution) SEC fractions. Fig.99B. 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.99A, fraction 6 is AS90, fraction 7 is AS91, fraction 8 is AS92, fraction 9 is AS93, and fraction 10 is AS94. In Fig.99B, fraction 8 is AS95, fraction 9 is AS96, fraction 10 is AS97, fraction 11 is AS98, fraction 12 is AS99, and fraction 13 is AS100. Figure 100 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 101A- 101F 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.101A. 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.101B. Correlogram functions of silk compositions presented in (ZA). Fig. ZC. Intensity diameter particle size distribution measured for silk compositions AS90-AS94, derived from Q-HIC(elution)-SEC fractionation process. Fig.101D. Correlogram functions of silk compositions presented in (ZC). Fig.101E. Intensity diameter particle size distribution measured for silk compositions AS95-AS100, derived from Q-HIC(flowthrough)-SEC fractionation process. Fig.101F. Correlogram functions of silk compositions presented in (ZE). Figure 102. 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 103. Is a chromatogram of Mid Skid silk / modified polypeptide compositions loaded onto a Superdex 200 gel filtration column. Mid Skid silk / modified peptidecompositions 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 Mid Skid silk / modified peptide compositions by size. The relative elution volume of silk compositions AS107 and AS111 are indicated on the chromatogram. Figure 104A-104B. Illustrates analytical Size Exclusion Chromatography of Mid Skid silk / modified silk compositions and their constituent AS compositions. Fig.104A. Average molecular weight in kDa of Mid Skid silk (MS) and AS106-AS111 are shown. Fig. 104B. Polydispersity (PDI) measurements are shown. The numerical data is presented in Table 92. Figure 105. 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 106. 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 93. Low Skid silk (LS) was used as a negative control. LS, Low Skid silk; MS, Mid Skid silk. Figures 107A-107B. 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.107A. Intensity particle size distribution measured for silk compositions AS106, AS107, AS108, AS109, AS110, AS111, and Mid Skid (MS). Fig. 107B. Correlation functions of silk compositions presented in (A). Figure 108. 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 size exclusion chromatography as a second purification step, distinct populations of Mid Skid silk / modified polypeptidecompositions 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 109A-109B. 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.109A. 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.109B. 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 110A-110B. Illustrate analytical Size Exclusion Chromatography of Mid Skid silk / modified silk compositions and their constituent AS compositions. Fig.110A. Average molecular weight in kDa of Mid Skid silk (MS) and AS101-AS105 are shown. Fig. 110B. Polydispersity (PDI) measurements are shown. The numerical data is presented in Table 95. Figure 111. 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 112 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 96. Figures 113A-113C. 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.113A. Intensity diameter particle size distribution by intensity measured for silk compositions AS101, AS102, AS103, AS104, and AS105. Fig.113B. 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.113C. Correlogram functions of silk compositions AS101, AS102, AS103, AS104, AS105, and Mid Skid silk (MS). Figure 114. 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 115A- 115B are analytical SEC-MALS of Low, Mid and High Molecular Weight Silk. Fig.115A. Weight Average Molecular Weight in kDa of Low, Mid, and High Molecular Weight Silk. Fig.115B. Polydispersity Index (PDI) measurements of Low, Mid, and High Molecular Weight Silk are shown. Figures 116A- 116B. Are analytical SEC-MALS of Low, Mid and High Molecular Weight Silk organized by Silk Type. Individual data points are show and the mean is represented by the heigh of the box. The bars encompass one standard deviation. Fig.116A. Weight-Average Molecular Weight Ranges for Low, Mid, and High Molecular Weight Silk. Fig.116B. PDI Ranges for Low, Mid, and High Molecular Weight Silk. Figures 117A- 117B are nalytical SEC-MALS of Low Skid silk / modified silk compositions and the constituent AS compositions as separated by Q-SEC (Q-eluent). Fig. 117A. Average molecular weight in kDa of Low Skid silk (LS) and AS77-AS81 are shown. Fig.117B. Polydispersity (PDI) measurements are shown. The numerical data is presented in Table 103. Figures 118A- 118B are analytical SEC-MALS of Low Skid silk / modified silk compositions and the constituent AS compositions as separated by SEC. Fig.118A. Average molecular weight in kDa of Low Skid silk (LS) and AS82-AS89 are shown. Fig.118B. Polydispersity (PDI) measurements are shown. The numerical data is presented in Table 104. Figures 119A- 119B 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.119A. Average molecular weight in kDa of Low Skid silk (LS) and AS90-AS94 are shown. Fig. A119B. Polydispersity (PDI) measurements are shown. The numerical data is presented in Table 105. Figures 120A- 120B 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.120A. Average molecular weight in kDa of Low Skid silk (LS) and AS95-AS100 are shown. Fig.120B. Polydispersity (PDI) measurements are shown. The numerical data is presented in Table 105. Figures 121A- 121B 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.121A. Average molecular weight in kDa of Mid Skid silk (MS) and AS101-AS105 are shown. Fig.121B. Polydispersity (PDI) measurements are shown. The numerical data is presented in Table 106. Figures 122A- 122B are analytical SEC-MALS of Mid Skid silk / modified silk compositions and the constituent AS compositions as separated by SEC. Fig.122A. Average molecular weight in kDa of Mid Skid silk (MS) and AS106-AS111 are shown. Fig.122B. Polydispersity (PDI) measurements are shown. The numerical data is presented in Table 107. Figures 123A- 123B are SEM images of unfinished leather. Figures 124A- 124B are SEM images of a silver tagged basecoat on leather. The leather was sprayed with 4 gr / sf of silver tagged basecoat. Figures 125A- 125B are SEM images of a silver tagged basecoat only on leather. The leather was sprayed with 4 gr / sf of silver tagged basecoat at higher magnification. Figure 126 is an SEM image of a silver tagged full L1 finish (basecoat + topcoat). The leather was sprayed with 4 gr / sf of silver tagged basecoat and 6gr / sf topcoat. This is a 45° turned sideview. Figures 127A- 127B are SEM images of a silver tagged full L1 finish (basecoat + topcoat). The leather was sprayed with 4 gr / sf of silver tagged basecoat and 6gr / sf topcoat. This is a cross-section view. Figure 128 is a photograph illustrating an example of failed milled leather (left) and passed milled leather (right). Figures 129A and 129B illustrate the process for forming a pattern on leather using paper release. Figure 130 illustrates the process for forming a pattern on leather for a large defect or snuff leather. Figures 131A - 131B are illustrations of the final composition of a leather article made with Paper Release Transfer Leather with the Activated Silk™ Topcoat layer (Fig. 131A) vs. a traditional topcoat (Fig.131B). The Activated Silk™ Topcoat layer is lower in solids concentration than a traditional topcoat (1.5 – 3% vs.15- 35%). When applied to Activated Silk™ L1 basecoat, it creates a composite.Figure 132 is an image of Low Grade Leather prior to Activated Silk™ L1 Paper release processing. Figure 133 is an image of Low Grade Leather after Activated Silk™ L1 Paper Release Processing. Figure 134 is an image of Low Grade Leather after Activated Silk™ L1 Paper Release Processing Close up. Figure 135 is a cross section view of unfinished crust. Figure 136 is a cross section view of crust with laminated film (pre-skin and skin). Figure 137 is a cross section view of crust with laminated film and basecoat. Figure 138 is a cross section view of crust with laminated film (pre-skin and skin) and basecoat. Figure 139 is a cross section view of crust with laminated film (pre-skin and skin) and basecoat. Figure 140 is a cross section view of crust with laminated film (pre-skin and skin) and basecoat. Figure 141 is a cross section view of finished leather of laminated film, basecoat and topcoat after rotopress processing. 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. DETAILED DESCRIPTION In some embodiments, the disclosure provides a composition comprising a coating comprising two components. In some embodiments, the second component is impregnated onto the first component. In some embodiments, the second component goes through a phase change (e.g., and without limitation, Tg, polymerization, etc.). A first coating described herein may include without limitation a polymer or any protein disclosed herein, such as a biodegradable polyurethane, a silk protein, a collagen, casein, elastin, etc. A second coating described herein may include without limitation a cellulose derivative disclosed herein. A first coating and a second coating should not be limited in that order, as any coating disclosed herein may be interchanged with any other coating disclosed herein. While an ethyl cellulose may be usually brittle and can crack, in some embodiments, this disclosure provides for aflexible ethyl cellulose coating. Ten disclosure provides for coating any surface, without limitation, e.g., leather, fabric, wood, protective coating for food (fruit, vegetables, etc.). In some embodiments, a coating disclosed herein is made with two or more films (maybe starting from one film made of the two polymers) with a monolayer distribution for coating on substrates. As disclosed herein, a composite material and / or coating disclosed herein can be based, without limitation, on a \molecular entanglement whereby EC is free of crosslinker. In some embodiments, all the layers are fixed together with molecular interaction. In some embodiments, all molecular interactions are cured or set or polymerized. In some embodiments, a molecular interaction of the two layers whereby the film is cured and the molecules form larger polymeric structures. In some embodiments, an outer layer described herein comprises between 1% and 100% EC on the surface. In some embodiments, a first layer (in application against the surface to be coated): engages in molecular entanglement such as the first layer and the second layer became adhered; a first layer can adhere to uneven surface; a first layer is: thermoplastic, self-assembled, soluble in the solvent used for the second layer; first layer polymerize through crosslinking, self-assembly. In some embodiments, a first layer is resoluble and can be cured. In some embodiments, a polymer or protein, e.g., and without limitation, a silk protein, has a role in the first layer. In some embodiments, a second layer (deposited on top of the first layer and the outside layer): it is made by Ethyl Cellulose (EC) or a biomaterial or a polymer, in a dispersion of molecules; In some embodiments, this layer in solvent contains between about 1-5 gr / L by volume EC. In some embodiments, this layer can deliver dye, silk or other molecule to modify optical, haptics and mechanical properties. In some embodiments, EC is a protective barrier that can enhance the performance and characteristics of the first layer. In some embodiments, EC is mechanically resilient and enhance the water resistance properties. In some embodiments, EC can adhere to a dynamic first layer substrate. In some embodiments, EC can adhere to uneven first layer surface. In some embodiments, the majority of the EC faces outwardly to the external environment / forces. In some embodiments,, a protein or polymer, e.g., and without limitation, silk has a role in the second layer. Silk coated leather articles and methods of making thereof have been described in WO 2020 / 018821 and WO 2021 / 146654, each of which is incorporated herein by reference in its entirety. Leather is a material manufactured by treating the skin peeled off from an animal body with a series of physical mechanic and chemical methods, followed by tanning. The leather materials are composed of weaved collagen fiber bundles and trace amount of elasticfibers and reticular fibers, of which the collagen fiber is between 95 and 98 percent. The natural weaving structure of collagen fiber in natural leather is that the thicker fiber bundles sometimes are divided into several strands of thinner fiber bundles and the resulting thinner fiber bundles sometimes incorporate other fiber bundles to form another larger fiber bundle. Leather in its natural state is a nonwoven material where the fibrils of the fiber have grown together. The silk fibroin protein and collagen fibers in the leather are natural proteins composed of 22 proteinogenic amino acids. The silk protein has high affinity to the leather fibers (collagen fibers) resulted from the presence of hydrophilic amino acid residue in the silk fibroin protein (e.g., physical entanglement due to forming hydrogen bonding between silk protein fragments and leather fibers), for example, -OH group from serine, guanidine group from arginine, free amine group from lysine, -COOH group from aspartic acid and glutamic acid. Methods of coating leather including for examples a method including: • Leather crusts may first be treated with stucco and / or ground to prepare surface for basecoat application. Stucco is typically used with leather that has scars and deep defects and can be applied by rollers. Ground is typically used for buffed and / or split leather and can be applied via rollercoater or spray. • Separately, an appropriate grain release paper that bears the negative engraving of the print design is applied with the basecoat solution and dried. The two substrates, treated leather and coated release paper, are then stacked together with the coated sides facing each other. The stacked substrate is then laminated through high pressure and temperature. Once laminated, the release paper is removed, leaving the print design on the semi-finished leather. • To finish the leather, the topcoat is applied via spray or rollercoater and is dried and ironed. In some embodiments, herein described silk fibroin-based protein fragments and solutions may find application as color performance enhancer for leather or leather articles. In some embodiments, this disclosure provides silk treated leather or leather articles exhibiting good dyeability, excellent color fastness and enhanced color saturation. The treatment on the leather and leather articles with silk fibroin-based protein fragments and solutions enhances the quality and aesthetic properties of the natural leather using non-toxic, sustainable and natural silk based composition. The silk treatment process disclosed herein advances leather products while respecting its heritage and craft without disruption to the leather tanning and creating process.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 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 weightaverage 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 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 weightaverage 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 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 weightaverage 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 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 weightaverage 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 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 #2450, having weight average molecular weights selected from about 1 kDa to about 145 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: P (abou MW (about) 1 kD2 kD 3 kD 4 kD 5 kD 6 kD 7 kD 8 kD 9 kD 10 kD 11 kD 12 kD 13 kD 14 kD 15 kD 16 kD 17 kD 18 kD 19 kD 20 kD 21 kD 22 kD 23 kD 24 kD 25 kD 26 kD 27 kD 28 kD 29 kD 30 kD 31 kD 32 kD 33 kD 34 kD 35 kD 36 kD 37 kD 38 kD 39 kD 40 kD 41 kD 42 kD 43 kD 44 kD 45 kD 46 kD 47 kD48 kD 49 kD 50 kD 51 kD 52 kD 53 kD 54 kD 55 kD 56 kD 57 kD 58 kD 59 kD 60 kD 61 kD 62 kD 63 kD 64 kD 65 kD 66 kD 67 kD 68 kD 69 kD 70 kD 71 kD 72 kD 73 kD 74 kD 75 kD 76 kD 77 kD 78 kD 79 kD 80 kD 81 kD 82 kD 83 kD 84 kD 85 kD 86 kD 87 kD 88 kD 89 kD 90 kD 91 kD 92 kD 93 kD94 kD 95 kD 96 kD 97 kD 98 kD 99 kD 100 kD 101 kD 102 kD 103 kD 104 kD 105 kD 106 kD 107 kD 108 kD 109 kD 110 kD 111 kD 112 kD 113 kD 114 kD 115 kD 116 kD 117 kD 118 kD 119 kD 120 kD 121 kD 122 kD 123 kD 124 kD 125 kD 126 kD 127 kD 128 kD 129 kD 130 kD 131 kD 132 kD 133 kD 134 kD 135 kD 136 kD 137 kD 138 kD 139 kDIn some embodiments, the molecular weights described herein 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 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 thepresent 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 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 disclosurehave 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 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 Na2CO3at 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 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 silksolution. 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 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.FIG.1 is a flow chart showing various embodiments for producing pure silk fibroin 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.1, step A, cocoons (heat-treated or non-heat-treated), silk fibers, silk powder, spider silk or recombinant 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 Na2CO3is completely dissolved. The raw silk is added to the boiling water / Na2CO3(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 Na2CO3volume is maintained at 2.12 g / L. Subsequently, the water dissolved Na2CO3solution is drained and excess water / Na2CO3is 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 ofLithium 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. 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. 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 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 from 80 °C to 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 methodsdescribed 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 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 andpolydispersity 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 protein fragments and to create a solution of higher molecular weight silk with and / or without tighter polydispersity values. An assay for LiBr and Na2CO3detection can be 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 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. FIG.2 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 weightand polydispersity. It should be understood that not all of the steps illustrated are necessarily required to fabricate all silk solutions of the present disclosure. In an embodiment, silk protein fragment solutions useful for a wide variety of applications are prepared according to the following steps: forming pieces of silk cocoons from the Bombyx mori silkworm; extracting the pieces at about 100 °C in a Na2CO3 water solution for about 60 minutes, wherein a volume of the water equals about 0.4 × raw silk weight and the amount of Na2CO3 is about 0.848 × 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 × 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 1.0 wt. % 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 silk solution to a concentration of 2.0 wt. % silk in water. 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. Also without 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. The extraction step 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 thana convection oven, for example a stirred tank reactor. 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. 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. 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 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 sodiumcarbonate 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 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 bromidehaving 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 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 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 theaqueous 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 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 anantioxidant 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 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 silk fibroin protein fragment solutions with polydispersity equal to or lower than 2.5 at a variety of different molecular weight selected from between 5 kDa to 200 kDa, or between 10 kDa and 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 higher molecular weight silk film containing an ophthalmic drug may have a controlled slow release rate compared to a lower molecular weight film making it ideal for a delivery vehicle in eye care products. Additionally, the silk fibroin protein fragment solutions with a polydispersity of greater than 2.5 can be achieved. Further, two solutions with different average molecular weights and polydispersity can be mixed to create combination solutions. Alternatively, a liquid silk gland (100% sericin free silk protein) thathas been removed directly from a worm could be used in combination with any of the silk fibroin protein fragment solutions of the present disclosure. Molecular weight of the pure silk fibroin 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. Experiments were carried out to determine the effect of varying the extraction time. 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 – 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).Experiments were carried out to determine the effect of varying the extraction temperature. Table G 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.Experiments were carried out to determine the effect of varying the Lithium Bromide (LiBr) temperature when added to silk. Tables H-I 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 temperatureExperiments were carried out to determine the effect of v oven / dissolution temperature. Tables J-N 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.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 Na2CO3is 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 60minutes 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). 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.1262mL 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. The preparation of silk fibroin solutions with higher molecular weights is given in Table O.G FIG D G FISilk aqueous coating composition for application to fabrics are given in Tables P and Q below.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 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) 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 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:E) 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) polypeptides alternate. Dragline silk is the protein complex composed of majorampullate 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 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) polypeptides alternate in core domain. Specific secondary structures have been assigned to poly(A) / (GA), GGX and GPGXX 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 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: 1 to 3 of 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: 1 to 3 of U.S. Patent No. 9,051,453. 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. 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. Thetotal 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 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 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 ofeukaryotic 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 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 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 hexapeptide repeating units. The GAGAGS 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 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 hexapeptide repetitive fragment derived from H chain of B. mori silk heavy chain and mammalian elastin VPGVG motif produced by E. coli. In some embodiments, this disclosure provides fusion silk fibroin proteins composed of the GAGAGS hexapeptide repetitive fragment derived from H chain of B. mori silk heavy chain and GVGVP 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 repetitive fragment. In some embodiments, this disclosure provides recombinant proteins composed of the (GAGAGS)16repetitive fragment and the non-repetitive (GAGAGS)16 –F-COOH, (GAGAGS)16 –F-F-COOH, (GAGAGS)16 – F-F-F-COOH, (GAGAGS)16–F-F-F-F-COOH, (GAGAGS)16–F-F-F-F-F-F-F-F-COOH, (GAGAGS)16 –F-F-F-F–F-F-F-F-F-F-F-F-COOH produced by E. coli, where F has the following amino acid sequence SGFGPVANGGSGEASSESDFGSSGFGPVANASSGEASSESDFAG, 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 secondfibroin 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 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) or GPGQQ) 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 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, MaSpII, ADF-3 and / or ADF-4. 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, MaSpII, ADF-3 and / or ADF-4, 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, 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 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 motif forms turn spiral structures, which imparts elasticity to the silk polypeptide. Major ampullate and flagelliform silks both have a GPGXX 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 and GGRPSSSYG derived from Resilin. Resilin is an 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:1), ADF-4 (SEQ ID NO:2), NR3 (SEQ ID NO:41), NR4 (SEQ ID NO:42), ADF-4 of the spider Araneus diadematus as described in U.S. Pat. No.8,367,803, C16 peptide (spider silk protein eADF4, molecular weight of 47.7 kDa, AMSilk) comprising the 16 repeats of the sequence GSSAAAAAAAASGPGGYGPENQGPSGPGGYGPGGP, 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: 1 as described in U.S. Patent No.8288512. Besides the polypeptide sequence shown in SEQ ID NO:1, 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 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, 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, GPGSG, GPGGY, GPGGP, GPGGA, GPGQQ, GPGGG, GPGQG, GPGGS, GGY, GGP, GGA, GGR, GGS, GGT, GGN, GGQ, AAAAA, AAAAAA, AAAAAAA, AAAAAAAA, AAAAAAAAA, AAAAAAAAAA, GGRPSDTYG and GGRPSSSYG, (i) GPYGPGASAAAAAAGGYGPGSGQQ, (ii) GSSAAAAAAAASGPGGYGPENQGPSGPGGYGPGGP, (iii) GPGQQGPGQQGPGQQGPGQQ: (iv) GPGGAGGPYGPGGAGGPYGPGGAGGPY, (v) GGTTIIEDLDITIDGADGPITISEELTI, (vi) PGSSAAAAAAAASGPGQGQGQGQGQGGRPSDTYG, (vii)SAAAAAAAAGPGGGNGGRPSDTYGAPGGGNGGRPSSSYG, (viii) GGAGGAGGAGGSGGAGGS (SEQ ID NO: 27), (ix) GPGGAGPGGYGPGGSGPGGYGPGGSGPGGY, (x) GPYGPGASAAAAAAGGYGPGCGQQ, (xi) GPYGPGASAAAAAAGGYGPGKGQQ, (xii) GSSAAAAAAAASGPGGYGPENQGPCGPGGYGPGGP, (xiii) GSSAAAAAAAASGPGGYGPKNQGPSGPGGYGPGGP, (xiv) GSSAAAAAAAASGPGGYGPKNQGPSGPGGYGPGGP, or variants thereof as described in U.S. Pat. No.8,877,903, for example, a synthetic spider peptide having sequential order of GPGAS, GGY, GPGSG in the peptide chain, or sequential order of AAAAAAAA, GPGGY, GPGGP in the peptide chain, sequential order of AAAAAAAA, GPGQG, 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 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 is an integer and having any weight average molecular weight described herein, and / or [(GPG2YGPGQ2)a(X’)2S(A)b]p 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]pFormula (III) and / or [(GGX)n(GA)m(A)l]pFormula (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]p Formula (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 (SEQ ID NO: 43) or variants thereof, MaSpII (SEQ ID NO: 44) or variants thereof as described in U.S. Pat. No.8,367,803. 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, GKGGGGGG, GCGGSGGGGSGGGG, GKGGGGGGSGGGG, and GCGGGGGGSGGGG. 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. 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 or SAAAAAAAAGPGGGNGGRPSDTYGAPGGGNGGRPSSSYG, as described in U.S. Pat. No.8,367,803. In some embodiments, this disclosure provides recombinant spider proteins composed of the GPGGAGPGGYGPGGSGPGGYGPGGSGPGGY 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 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. Thelength 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 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 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 notprecipitate 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 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 medium of this step is 3 orhigher, 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 fiber assembly of NT-minispidroins, are due to surface electrostatic potential changes, and that clustering of acidic residues at one pole ofNT 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. 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: 1 of 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: 2 of U.S. Patent No. 9,051,453 is identical to an amino acid sequence represented by SEQ ID NO: 1 of 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: 3 of U.S. Patent No.9,051,453 is identical to an amino acid sequence represented by SEQ ID NO: 1 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: 1 to 3 or an amino acid sequence having a homology of 90% or more with the amino acid sequence represented by any of SEQ ID NOS: 1 to 3 of U.S. Patent No.9,051,453 is a polypeptide having an amino acid sequence represented by SEQ ID NO: 8 of U.S. Patent No.9,051,453. The polypeptide having the amino acid sequence represented by SEQ ID NO: 8 of 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: 5 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, 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: 8 of U.S. Patent No. 9,051,453, the C-terminal sequence is identical to the amino acid sequence represented by SEQ ID NO: 3. 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: 1 to 3 of 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: 1 to 3 of U.S. Patent No.9,051,453 may be a protein that has an amino acid sequence represented by SEQ ID NO: 8 of U.S. Patent No.9,051,453 in which one or aplurality 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: 15 of U.S. Patent No.9,051,453. The amino acid sequence represented by SEQ ID NO: 15 of U.S. Patent No. 9,051,453 is an amino acid sequence obtained by adding the amino acid sequence (SEQ ID NO: 5 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 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: 15 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. 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: 17 of U.S. Patent No.9,051,453. The amino acid sequence represented by SEQ ID NO: 17 of U.S. Patent No. 9,051,453 is an amino acid sequence obtained by adding the amino acid sequence (SEQ ID NO: 5 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: 17 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 weightof 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, 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: 19 of U.S. Patent No.9,051,453. The amino acid sequence represented by SEQ ID NO: 19 of U.S. Patent No.9,051,453 is an amino acid 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: 5 of 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: 19 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 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 naturalspider 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 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 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 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 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 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 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%, about36%, 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%, 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, inU.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 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 extendedperiod 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. 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 compositionof the present disclosure is soluble in an aqueous solution. In an 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 between a 99% crystalline portion and a 1% amorphous region, and 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, theextended 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 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. As used herein, in some embodiments the term “leather” and / or “leather substrate” refers to natural leather and may be derived from bovine skin, sheep skin, lamb skin, horse skin, crocodile skin, alligator skin, avian skin, or another known animal skin as would be appreciated by the art, or processed leather. Unprocessed, processed, coated, and / or repaired leather may include, without limitation, Altered leather, Aniline leather, Bonded leather, Brushed leather, Buffed leather, Bycast leather, Chamois leather, Chrome-tanned leather, Combination tanned leather, Cordovan leather, Corrected grain leather, Crockproof leather, Drummed leather, Embossed leather, Enhanced grain leather, Grained leather, Metallized leather, Naked leather, Natural grain leather, Nubuck leather, Patent leather, Pearlized leather, Plated leather, Printed leather, Protected leather, Pure Aniline leather, Tanned / Retanned leather, Round Hand leather, Saddle leather, Semi-Aniline leather Shrunken grain leather, Side leather, Split leather, Suede leather, and Wet blue. In some embodiments, the term “leather” may refer to synthetic or reconstituted leather, including, but not limited to, leather partially / fully constituted with cellulose, mushroom-based material, synthetic materials such as vinyl, synthetic materials such as polyamide or polyester.As used herein, the term hand refers to the feel of a material, which may be further described as the feeling of softness, crispness, dryness, silkiness, smoothness, and combinations thereof. Material hand is also referred to as “drape.” A material with a hard hand is coarse, rough, and generally less comfortable for the wearer. A material with a soft hand is fluid and smooth and generally more comfortable for the wearer. Material hand can be determined by comparison to collections of material samples, or by use of methods such as the Kawabata Evaluation System (KES) or the Fabric Assurance by Simple Testing (FAST) methods. Behera and Hari, Ind. J. Fibre & Textile Res., 1994, 19, 168-71. In some embodiments, and as described herein, silk can change the hand of leather, as may be evaluated by SynTouch Touch-Scale methodology or another methodology as described herein. As used herein, a “coating” refers to a material, or combination of materials, that form a substantially continuous layer or film on an exterior surface of a substrate, such as leather or leather article. In some embodiments, a portion of the coating may penetrate at least partially into the substrate. In some embodiments, the coating may penetrate at least partially into the interstices of a substrate. In some embodiments, the coating may be infused into a surface of the substrate such that the application of the coating, or coating process, may include infusing (at the melting temperature of the substrate) at least one coating component at least partially into a surface of the substrate. A coating may be applied to a substrate by one or more of the processes described herein. In embodiments described where the coating may be infused into a surface of the substrate, the coating may be codissolved in a surface of the substrate such that a component of the coating may be intermixed in the surface of the substrate to a depth of at least about 1 nm, or at least about 2 nm, or at least about 3 nm, or at least about 4 nm, or at least about 5 nm, or at least about 6 nm, or at least about 7 nm, or at least about 8 nm, or at least about 9 nm, or at least about 10 nm, or at least about 20 nm, or at least about 30 nm, or at least about 40 nm, or at least about 50 nm, or at least about 60 nm, or at least about 70 nm, or at least about 80 nm, or at least about 90 nm, or at least about 100 nm. In some embodiments, the coating may be infused into a surface of the substrate where the substrate includes leather or a leather article. As used herein, the term “bath coating” encompasses coating a material in a bath, immersing a material in a bath, and submerging a material in a bath. Concepts of bath coating are set forth in U.S. Patent No.4,521,458, the entirety of which is incorporated by reference.As used herein, and unless more specifically described, the term drying may refer to drying a coated material as described herein at a temperature greater than room temperature (i.e., 20 °C). Without wishing to be bound by any particular theory, any and all solutions described herein can be further used or processed to obtain a variety of silk and / or SPF compositions, including, but not limited to, silk non-Newtonian fluids, silk materials that can sustain a shear stress network spanning the system, silk solutions containing water or another solvent trapped inside a loose silk polymer network, silk materials that transition from a liquid form via bond percolation transition such as gels, silk immobile network entrapping a mobile solvent, silk materials forming reversible or irreversible crosslinks, silk materials that exhibit a shear modulus, silk elastomers or silk materials exhibiting thermoplastic behavior, silk materials formed by the processes of either glass formation, gelation, or colloidal aggregation, silk crystals, and / or silk crystals polish, glues, gels, pastes, putties, and / or waxes. As used herein when referring to a number or a numerical range, the term “about” means that the stated number or numerical range is included together with numbers or numerical ranges within experimental variability, or within statistical experimental error from the stated number or numerical range, wherein the variation or error is from 0% to 15%, or from 0% to 10%, or from 0% to 5% of the stated number or numerical range. As used herein, “silk based proteins or fragments thereof” includes silk fibroin-based proteins or fragments thereof, natural silk based proteins or fragments thereof, recombinant silk based proteins or fragments thereof, and combinations thereof. Natural silk based proteins or fragments thereof include spider silk based proteins or fragments thereof, silkworm silk based proteins or fragments thereof, and combinations thereof. Silkworm based proteins or fragments thereof may include Bombyx mori silk based proteins or fragments thereof. The SPF mixture solutions described herein may include silk based proteins or fragments thereof. Moreover, SFS, as described herein, may be replaced with SPF mixture solutions. The silk based proteins or fragments thereof, silk solutions or mixtures (e.g., SPF or SFS solutions or mixture), and the like, may be prepared according to the methods described in U.S. Patent Nos.9,187,538, 9,522,107, 9,522,108, 9,511, 012, 9,517,191, and 9,545,369, and U.S. Patent Publication Nos.2016 / 0222579 and 2016 / 0281294, and International Patent Publication Nos. WO 2016 / 090055 and WO 2017 / 011679, the entirety of which are incorporated herein by reference. In some embodiments, the silk based proteins or fragments thereof may be provided as a silk composition, which may be an aqueous solution or mixture of silk, a silk gel, and / or a silk wax as described herein.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 between about 0.01% (w / w) and about 10.0% (w / w) sericin. In an embodiment, silk fibroin that is substantially devoid of sericin refers to silk fibroin having a sericin content below about 0.05 % (w / w). 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 wt. % to about 31 wt.% is obtained. As used herein, the term “substantially homogeneous” may refer to pure 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 an additive, for example a pigment, throughout a composition of the present disclosure. As used herein, “residuals” refer to materials related to one or more process steps in the manufacturing of silk fibroin solutions, silk fibroin fragments solutions, or concentrates thereof. In some embodiments, 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 in some embodiments 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 managementprocess. 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. In some embodiments, compositions and articles described herein, and methods of preparing the same, include silk coated leather or leather article. The leather or leather article may be a polymeric material such as those described elsewhere herein. The terms “infused” and / or “partially dissolved” includes mixing to form a dispersion of, e.g., a portion of leather or leather article with a portion of the silk based coating. In some embodiments, the dispersion may be a solid suspension (i.e., a dispersion comprising domains on the order of 10 nm) or a solid solution (i.e., a molecular dispersion) of silk. In some embodiments, the dispersion may be localized at the surface interface between the silk coating and the leather or leather article, and may have a depth of 1 nm, 2 nm, 5 nm, 10 nm, 25 nm, 50 nm, 75 nm, 100 nm, or greater than 100 nm, depending on the method of preparation. In some embodiments, the dispersion may be a layer sandwiched between the leather or leather article and the silk coating. In some embodiments, the dispersion may be prepared by coating silk, including silk fibroin with the characteristics described herein, onto the leather or leather article, and then performing an additional process to form the dispersion, including heating at a temperature of 100 °C, 125 °C, 150 °C, 175 °C, 200 °C, 225 °C, or 250 °C for a time period selected from the group consisting of 1 minute, 2 minutes, 5 minutes, 10 minutes, 15 minutes, 20 minutes, 30 minutes, 1 hour, 2 hours, 4 hours, 8 hours, 16 hours, or 24 hours. In some embodiments, heating may be performed at or above the glass transition temperature (Tg) of silk and / or the polymeric fabric or textile, which may be assessed by methods known in the art. In some embodiments, the dispersion may be formed by coating silk, including silk fibroin with the characteristics described herein, onto the leather or leather article, and then performing an additional process to impregnate the silk coating into the leather or leather article, including treatment with an organic solvent. Methods for characterizing the properties of polymers dissolved in one another are well known in the art and include differential scanning calorimetry and surface analysis methods capable of depth profiling, including spectroscopic methods. In some embodiments, 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 isabout 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. In some embodiments, where aqueous solutions are used to prepare SPF compositions or SPF containing coatings, the aqueous solutions are prepared using any type of water. In some embodiments, water may be DI water, tap water, or naturally available water. As used herein, “tap water” refers to potable water provided by public utilities and water of comparable quality, regardless of the source, without further refinement such as by reverse osmosis, distillation, and / or deionization. Therefore, the use of “DI water,” “RODI water,” or “water,” as set forth herein, may be understood to be interchangeable with “tap water” according to the processes described herein without deleterious effects to such processes. Leather and Leather Articles Processed, Coated, and / or Repaired with Silk Fibroin-Based Protein Fragments In one aspect, the present disclosure provides a coating composition comprising silk fibroin proteins or fragments thereof. In an embodiment, the silk fibroin proteins or fragments thereof have an average weight average molecular weight in a range selected from between about 1 kDa and about 5 kDa, between about 5 kDa and about 10 kDa, between about 6 kDa and about 17 kDa, between about 10 kDa and about 15 kDa, between about 14 kDa and about 30 kDa, between about 15 kDa and about 20 kDa, between about 17 kDa and about 39 kDa, between about 20 kDa and about 25 kDa, between about 25 kDa and about 30 kDa, between about 30 kDa and about 35 kDa, between about 35 kDa and about 40 kDa, between about 39 kDa and about 80 kDa, between about 40 kDa and about 45 kDa, between about 45 kDa and about 50 kDa, between about 60 kDa and about 100 kDa, and between about 80 kDa and about 144 kDa, and a polydispersity between 1 and about 5. In some embodiments, the silk fibroin proteins or fragments thereof have any average weight average molecular weight described herein. In some embodiments, the silk fibroin proteins or fragments thereof have a polydispersity between 1 and about 1.5. In some embodiments, the silk fibroin proteins or fragments thereof have a polydispersity between about 1.5 and about 2. In some embodiments, the silk fibroin proteins or fragments thereof have a polydispersity betweenabout 2 and about 2.5. In some embodiments, the silk fibroin proteins or fragments thereof have a polydispersity between about 2.5 and about 3. In some embodiments, the silk fibroin proteins or fragments thereof have a polydispersity between about 3 and about 3.5. In some embodiments, the silk fibroin proteins or fragments thereof have a polydispersity between about 3.5 and about 4. In some embodiments, of claim 1, wherein the silk fibroin proteins or fragments thereof have a polydispersity between about 4 and about 4.5. In some embodiments, the silk fibroin proteins or fragments thereof have a polydispersity between about 4.5 and about 5. In an embodiment, the silk fibroin proteins or fragments thereof have any average weight average molecular weight and polydispersity described herein, and optionally any other limitations described herein, and about 0.001% (w / w) to about 10% (w / w) sericin relative to the silk fibroin proteins or fragments thereof. In some embodiments, the w / w ratio between silk fibroin proteins or fragments thereof and sericin is about 99:1, about 98:2, about 97:3, about 96:4, about 95:5, about 94:6, about 93:7, about 92:8, about 91:9, about 90:10, about 89:11, about 88:12, about 87:13, about 86:14, about 85:15, about 84:16, about 83:17, about 82:18, about 81:19, about 80:20, about 79:21, about 78:22, about 77:23, about 76:24, or about 75:25. In some embodiments, the relative w / w amount of sericin to the silk fibroin proteins or fragments thereof is about 10%, about 9%, about 8%, about 7%, about 6%, about 5%, about 4%, about 3%, about 2%, about 1%, about 0.9%, about 0.8%, about 0.7%, about 0.6%, about 0.5%, 0.4%, about 0.3%, about 0.2%, about 0.1%, about 0.01%, or about 0.001%. In an embodiment, the silk fibroin proteins or fragments thereof have any average weight average molecular weight and polydispersity described herein, and optionally any other limitations described herein, wherein the silk fibroin proteins or fragments thereof 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 coated onto the article. In some embodiments, the silk fibroin proteins or fragments thereof do not spontaneously or gradually gelate and do not visibly change in color or turbidity when in an aqueous solution for at least 1 day, 2 days, 3 days, 4 days, 5 days, 6 days, 7 days, 8 days, 9 days, 10 days, 11 days, 12 days, 13 days, 14 days, 15 days, 16 days, 17 days, 18 days, 19 days, 20 days, 21 days, 4 weeks, or 1 month prior to being coated on the article. In one aspect, the present disclosure provides an article coated with the coating composition described elsewhere herein.In an embodiment, the article is a leather article such as a leather substrate. Some methods for adding a protein to a substrate, including a leather substrate, are described in U.S. Pat. No.8,993,065, incorporated herein by reference in its entirety. The disclosure also provides an article including a leather substrate and silk fibroin proteins or fragments thereof having any average weight average molecular weight and polydispersity described herein, and optionally any other limitations described herein, wherein: 1) a portion of the silk fibroin proteins or fragments thereof is coated on a surface of the leather substrate; or 2) a portion of the silk fibroin proteins or fragments thereof is infused into a layer of the leather substrate, in some embodiments, such layers having a thickness as described herein; or 3) a portion of the silk fibroin proteins or fragments thereof is in a recessed portion of the leather substrate selected from an opening, a crevice, and a defect in the leather substrate; or 4) any combination of the above. Referring to FIGS.22A and 22B, the manner in which a portion of the silk fibroin proteins or fragments thereof is coated on a surface of the leather substrate, or the manner in which a portion of the silk fibroin proteins or fragments thereof is in a recessed portion of the leather substrate, can be described by way of a cross-section index, wherein a cross-section index is defined as the ratio between the area above the curve up to a baseline and the length of the cross section across which the area above the curve is determined. The cross-section index is reflected herein as a unitless value. The curve may reflect the leather surface (if uncoated or unfilled) along a cross-section, or a surface of a silk fibroin proteins or fragments thereof coating or filling along a cross-section. The baseline may reflect a horizontal plane approximating the surface of the leather substrate across the segment through which the cross-section index is determined. As shown in FIG.49A, a recessed portion is for example between the cross-section x1 = about 210 µm, and x2 = about 600 µm, and the cross-section index of this recessed portion can be calculated as described herein. In some embodiments, a recessed portion of the leather substrate has a cross-section index of about 6.50, about 6.75, about 7, about 7.25, about 7.50, about 7.75, about 8, about 8.25, about 8.50, about 8.75, about 9, about 9.25, about 9.50, about 9.75, or about 10. In some embodiments, a recessed portion of the leather substrate can have another cross-section index, for example about 5, about 5.1, about 5.2, about 5.3, about 5.4, about 5.5, about 5.6, about 5.7, about 5.8, about 5.9, about 6, about 6.1, about 6.2, bout 6.3, about 6.4, about 6.5, about 6.6, about 6.7, about 6.8, about 6.9, about 7, about 7.1, about 7.2, about 7.3, about 7.4, about 7.5, about 7.6, about 7.7, about 7.8, about 7.9, about 8, about 8.1, about 8.2, bout 8.3, about 8.4, about 8.5, about 8.6, about 8.7, about 8.8, about 8.9, about 9,about 9.1, about 9.2, about 9.3, about 9.4, about 9.5, about 9.6, about 9.7, about 9.8, about 9.9, or about 10. Also as shown in FIG.49A, a substantially non-recessed portion of the leather substrate is for example between the cross-section x1 = 0 µm, and x2 = about 210 µm, and the cross-section index of this substantially non-recessed portion can be calculated as described herein. In some embodiments, a substantially non-recessed portion of the leather substrate has a cross-section index of about 1.1, about 1.2, about 1.3, about 1.4, about 1.5, about 1.6, about 1.7, about 1.8, about 1.9, or about 2.0. In some embodiments, a substantially non-recessed portion of the leather substrate can have another cross-section index, for example about 0.1, about 0.2, about 0.3, about 0.4, about 0.5, about 0.6, about 0.7, about 0.8, about 0.9, about 1, about 1.1, about 1.2, bout 1.3, about 1.4, about 1.5, about 1.6, about 1.7, about 1.8, about 1.9, about 2, about 2.1, about 2.2, about 2.3, about 2.4, about 2.5, about 2.6, about 2.7, about 2.8, about 2.9, or about 3. As shown in FIG.22B, a recessed portion filled with silk fibroin proteins or fragments thereof is for example between the cross-section x1 = about 210 µm, and x2 = about 395 µm, and the cross-section index of this filled recessed portion can be calculated as described herein. In some embodiments, a filled recessed portion of the leather substrate can have a cross-section index of about 0.25, about 0.50, about 0.75, about 1, about 1.25, about 1.27, about 1.50, about 1.75, or about 2. In some embodiments, a filled recessed portion of the leather substrate can have any other cross-section index, for example about 0.1, about 0.2, about 0.3, about 0.4, about 0.5, about 0.6, about 0.7, about 0.8, about 0.9, about 1, about 1.1, about 1.2, bout 1.3, about 1.4, about 1.5, about 1.6, about 1.7, about 1.8, about 1.9, about 2, about 2.1, about 2.2, about 2.3, about 2.4, about 2.5, about 2.6, about 2.7, about 2.8, about 2.9, or about 3. Also as shown in FIG.22B, a substantially non-recessed portion of the leather substrate coated with silk fibroin proteins or fragments thereof is for example between the cross-section x1 = 0 µm, and x2 = about 210 µm, and the cross-section index of this recessed portion can be calculated as described herein. In some embodiments, a coated substantially non-recessed portion of the leather substrate has a cross-section index of about 0.05, about 0.1, about 0.15, about 0.2, about 0.25, about 0.50, about 0.75, about 1, about 1.25, about 1.27, about 1.50, about 1.75, or about 2. In some embodiments, a coated substantially non-recessed portion of the leather substrate can have any other cross-section index, for example about 0.1, about 0.2, about 0.3, about 0.4, about 0.5, about 0.6, about 0.7, about 0.8, about 0.9, about 1, about 1.1, about 1.2, bout 1.3, about 1.4, about 1.5, about 1.6, about 1.7, about 1.8, about 1.9, about 2, about 2.1, about 2.2, about 2.3, about 2.4, about 2.5, about 2.6, about 2.7, about 2.8, about 2.9, or about 3.In some embodiments, a coated substantially non-recessed portion of the leather substrate may have a cross-section index lower than a substantially non-recessed portion of the leather substrate before coating. In some embodiments, a coated substantially non- recessed portion of the leather substrate has a cross-section index lower than a substantially non-recessed portion of the leather substrate before coating, wherein the cross-section index of the coated substantially non-recessed portion of the leather substrate is higher than 0. In some embodiments, a coated substantially non-recessed portion of the leather substrate has a cross-section index lower than a substantially non-recessed portion of the leather substrate before coating by a factor between 1% and 99%. In some embodiments, a coated substantially non-recessed portion of the leather substrate may have a cross-section index lower than a substantially recessed portion of the leather substrate before filling. In some embodiments, a coated substantially non-recessed portion of the leather substrate has a cross-section index lower than a substantially recessed portion of the leather substrate before filling, wherein the cross-section index of the coated substantially non-recessed portion of the leather substrate is higher than 0. In some embodiments, a coated substantially non-recessed portion of the leather substrate has a cross- section index lower than a substantially recessed portion of the leather substrate before filling by a factor between 1% and 99%. In some embodiments, a filled recessed portion of the leather substrate may have a cross-section index lower than a substantially non-recessed portion of the leather substrate before coating. In some embodiments, a filled recessed portion of the leather substrate may have a cross-section index lower than a substantially non-recessed portion of the leather substrate before coating, wherein the cross-section index of the filled recessed portion of the leather substrate is higher than 0. In some embodiments, a filled recessed portion of the leather substrate may have a cross-section index lower than a substantially non-recessed portion of the leather substrate before coating by a factor between 1% and 99%. In some embodiments, a filled recessed portion of the leather substrate may have a cross-section index lower than a substantially non-recessed portion of the leather substrate before filling. In some embodiments, a filled recessed portion of the leather substrate may have a cross-section index lower than a substantially non-recessed portion of the leather substrate before filling, wherein the cross-section index of the filled recessed portion of the leather substrate is higher than 0. In some embodiments, a filled recessed portion of the leather substrate may have a cross-section index lower than a substantially non-recessed portion of the leather substrate before filling by a factor between 1% and 99%.The disclosure also provides an article including a leather substrate and silk fibroin proteins or fragments thereof having any average weight average molecular weight and polydispersity described herein, and optionally any other limitations described herein, the article further including one or more polysaccharides selected from starch, cellulose, gum arabic, guar gum, xanthan gum, alginate, pectin, chitin, chitosan, carrageenan, inulin, and gellan gum. In some embodiments, the polysaccharide is gellan gum. In some embodiments, the gellan gum comprises low-acyl content gellan gum. The disclosure also provides an article including a leather substrate and silk fibroin proteins or fragments thereof having any average weight average molecular weight and polydispersity described herein, and optionally any other limitations described herein, the article further including one or more polyols, and / or one or more polyethers. In some embodiments, the polyols include one or more of glycol, glycerol, sorbitol, glucose, sucrose, and dextrose. The disclosure also provides an article including a leather substrate and silk fibroin proteins or fragments thereof having any average weight average molecular weight and polydispersity described herein, and optionally any other limitations described herein, the article further including one or more of a silicone, a dye, a pigment, and a polyurethane as described herein. In an embodiment, an aqueous coating composition described elsewhere herein is applied directly to the article. In an embodiment, a silk coating described elsewhere herein can be coated on the article to form a pattern or design on the article. In an embodiment, a coating composition described elsewhere herein is applied to a leather or leather article under tension and / or lax to vary penetration into the leather or leather article. In an embodiment, the disclosure provides leather and leather articles coated with a silk composition described herein. In an embodiment, the disclosure provides leather and leather articles repaired with a silk composition described herein, for example by filling, masking, or hiding a defect in the surface or structure of the leather. In an embodiment, the disclosure provides leather and leather articles processed with any one of herein described silk compositions and a dye to provide colored leather and leather articles exhibiting enhanced color-saturation and excellent color-fixation properties. In some embodiments, the silk composition may be applied currently with the dye. In some embodiments, the silk composition may be applied prior to the dyeing process. In some embodiments, the silk composition may be applied post the dyeing process. In some embodiments, the leather may include nubuck skin in crust, nubuck skin finished in black orblue color, suede skin fined in brown or turquoise color, bottom split suede, or top split wet blue suede. The disclosure provides generally to methods and articles related to filling a recessed portion of a leather, such as, without limitation, an opening, a crevice, or a defect in a leather substrate, with silk fibroin proteins and / or fragments thereof. As used herein, the term “defect” or “leather defect,” refers to any imperfection in or on the surface, and / or the underlying structure of the leather. For example, removal of a hair and / or hair follicle may leave a visible void or gap in the surface or structure of the leather or hide. This disclosure is not limited to repairing visible defects, and thus it is contemplated that any defects can be repaired as described herein. This disclosure is likewise not limited to repairing defects of a certain size, and defects of any size can be repaired and / or filled. For example, silk and / or SPFs, and any and all compositions described herein, can be used to fill in or mask the appearance of larger defects occurring over larger areas of a defective skin surface. As used herein, “repaired” or “repairing” leather refers to filling a defect with a composition including silk and / or SPF, wherein as a result of such repairing the defect is substantially eliminated. For example, a void or gap which is fully or partially filled with a composition as described herein may be a repaired defect. In an embodiment, the disclosure provides a leather or leather article processed, coated, and / or repaired with silk fibroin-based proteins or fragments thereof. In an embodiment, the disclosure provides a leather or leather article processed, coated, or repaired with silk fibroin-based proteins or fragments thereof, wherein the leather or leather article is a leather or leather article used for human apparel, including apparel. In an embodiment, the disclosure provides a leather or leather article processed, coated, or repaired with silk fibroin- based proteins or fragments thereof, wherein the leather or leather article is used for automobile upholstery. In an embodiment, the disclosure provides a leather or leather article processed, coated, or repaired with silk fibroin-based proteins or fragments thereof, wherein the leather or leather article is used for aircraft upholstery. In an embodiment, the disclosure provides a leather or leather article processed, coated, or repaired with silk fibroin-based proteins or fragments thereof, wherein the leather or leather article is used for upholstery in transportation vehicles for public, commercial, military, or other use, including buses and trains. In an embodiment, the disclosure provides a leather or leather article processed, coated, or repaired with silk fibroin-based proteins or fragments thereof, wherein the leather or leather article is used for upholstery of a product that requires a high degree of resistance to wear as compared to normal upholstery.In an embodiment, a leather or leather article is treated with a polymer, such as polyglycolide (PGA), polyethylene glycols, copolymers of glycolide, glycolide / L-lactide copolymers (PGA / PLLA), glycolide / trimethylene carbonate copolymers (PGA / TMC), polylactides (PLA), stereocopolymers of PLA, poly-L-lactide (PLLA), poly-DL-lactide (PDLLA), L-lactide / DL-lactide copolymers, co-polymers of PLA, lactide / tetramethylglycolide copolymers, lactide / trimethylene carbonate copolymers, lactide / δ-valerolactone copolymers, lactide / ε-caprolactone copolymers, polydepsipeptides, PLA / polyethylene oxide copolymers, unsymmetrically 3,6-substituted poly-1,4-dioxane-2,5- diones, poly-β-hydroxybutyrate (PHBA), PHBA / β-hydroxyvalerate copolymers (PHBA / HVA), poly-β-hydroxypropionate (PHPA), poly-p-dioxanone (PDS), poly-δ- valerolactone, poly-ε-caprolactone, methylmethacrylate-N-vinyl pyrrolidine copolymers, polyesteramides, polyesters of oxalic acid, polydihydropyrans, polyalkyl-2-cyanoacrylates, polyurethanes (PU), polyvinylalcohols (PVA), polypeptides, poly-β-malic acid (PMLA), poly-β-alkanoic acids, polyvinylalcohol (PVA), polyethyleneoxide (PEO), chitine polymers, polyethylene, polypropylene, polyasetal, polyamides, polyesters, polysulphone, polyether ether ketone, polyethylene terephthalate, polycarbonate, polyaryl ether ketone, and polyether ketone ketone. In an embodiment, an aqueous solution of pure silk fibroin-based protein fragments of the present disclosure is used to process and / or coat a leather or leather article. In an embodiment, the concentration of silk in the solution ranges from about 0.1% to about 20.0%. In an embodiment, the concentration of silk in the solution ranges from about 0.1% to about 15.0%. In an embodiment, the concentration of silk in the solution ranges from about 0.5% to about 10.0%. In an embodiment, the concentration of silk in the solution ranges from about 1.0% to about 5.0%. In an embodiment, an aqueous solution of pure silk fibroin-based protein fragments of the present disclosure is applied directly to a leather or leather article. Alternatively, silk microsphere and any additives may be used for processing and / or coating a leather or leather article. In an embodiment, additives can be added to an aqueous solution of pure silk fibroin-based protein fragments of the present disclosure before coating (e.g., alcohols) to further enhance material properties. In an embodiment, a silk coating of the present disclosure can have In an embodiment, a composition of pure silk fibroin-based protein fragments of the present disclosure is used to repair a leather or leather article. In some embodiments, the composition is viscous. In some embodiments, the composition is thixotropic. In some embodiments, the composition is a gel, a putty, a wax, a paste, or the like. In someembodiments, the composition is shaped as a repairing bar, for example a repairing crayon. In some embodiments, the composition is delivered from a syringe, a delivery gun, a brush-type applicator, a roller-type applicator, a pen or marker-type applicator, or the like. In some embodiments, the composition is co-delivered from a multiple syringe, for example a double syringe, or a double delivery gun, along a different composition designed to harden, initiate curing of, or otherwise modify the SPF composition. In an embodiment, the concentration of silk in the composition ranges from about 0.1% to about 50.0%. In an embodiment, the concentration of silk in the solution ranges from about 0.1% to about 35.0%. In an embodiment, the concentration of silk in the solution ranges from about 0.5% to about 30.0%. In an embodiment, the concentration of silk in the solution ranges from about 1.0% to about 25.0%. In an embodiment, a composition of pure silk fibroin-based protein fragments of the present disclosure is applied directly to a leather or leather article, for example to a leather defect. Alternatively, silk microsphere and any additives may be used for repairing a leather or leather article. In an embodiment, additives can be added to the composition of pure silk fibroin-based protein fragments of the present disclosure before coating (e.g., alcohols) to further enhance material properties. In an embodiment, a composition is applied to a leather or leather article under tension and / or lax to vary penetration in to the leather, leather article, or leather defect. In an embodiment, the disclosure provides a leather or leather article coated with the coating composition describe elsewhere herein. In an embodiment, the leather or leather article is an aniline leather or leather article. In an embodiment, the leather or leather article is used for human apparel, automobile upholstery, aircraft upholstery, or upholstery in transportation vehicles for public, commercial, military, or other use, including buses and trains. In an embodiment, the disclosure provides a leather or leather article coated with the mattifying coating composition described elsewhere herein, wherein the leather or leather article is used for a product wherein a matte effect is desired. In another embodiment, the disclosure provides an aniline leather or aniline leather article coated with the water soluble dye fixing coating composition described elsewhere herein. In an embodiment, the aniline leather or aniline leather article is coated with a water soluble dye fixing coating composition described herein comprising a water soluble aniline leather dye. In an embodiment, the water soluble dye fixing coating composition described herein comprising a water soluble aniline leather dye fixes the aniline leather dye during aniline leather finishing, providing a dyed leather with a natural look and / or feel. In an embodiment, the concentration of the water soluble dye and / or water soluble aniline leather dye can be tuned to provide a deeper color of the dyed leather or a lighter color of the dyed leather.Methods of Coating an Article with the Coating Composition In yet another aspect, the present disclosure provides a method of coating an article with a coating composition, the method comprising applying the coating composition to one or more surfaces of the article. The coating composition is described elsewhere herein. In an embodiment, the coating composition comprises silk fibroin proteins or fragments thereof and a mattifying silica and / or starch. In another embodiment, the coating composition comprises silk fibroin proteins or fragments thereof and a water soluble dye. In another embodiment, the coating composition is a two part coating composition wherein the first part comprises a water soluble dye and the second part comprises silk fibroin proteins or fragments thereof. In an embodiment, the coating composition is a liquid, a gel, a paste, a wax, or a cream. In an embodiment, the coating composition is a liquid. In one embodiment, the coating composition comprises an aqueous solvent. In one embodiment wherein the coating composition is a liquid, the method further comprises the step of drying the article. The coating composition described herein may be applied to the article using any method known to a person of skill in the art. Exemplary application methods include, but are not limited to, hand-spraying, spraying using a mechanical spray setup, applying by brush, rubbing, wet-mixing, washing, drumming, soaking, injecting, plastering, smearing, or the like. In an embodiment wherein the coating composition comprises silk fibroin proteins or fragments thereof and a water soluble dye, the coating composition is sprayed onto the article in one application of about 4 g / sqft. In an embodiment, the coating composition comprising silk fibroin proteins or fragments thereof and a water soluble dye is sprayed onto a leather article in one application of about 4 g / sqft. In some embodiments, a coating composition described herein may be applied to an article alone, mixed with one or several chemicals (e.g., chemical agents), as one coat, multiple coats, or at multiple times using varied application methods. In an embodiment, the thickness of the coating is described elsewhere herein. In embodiments wherein the coating composition is a two part coating composition, the step of applying the coating composition to one or more surfaces of the article comprises (a) applying the first part of the coating composition to one or more surfaces of the article. In an embodiment, a first part of the coating composition comprising a water soluble dye is applied to one or more surfaces of the article. In an embodiment, a first part of the coating composition comprising a water soluble dye is applied to one or more surfaces of a leather article. In an embodiment, the first part of the coating composition is applied to the leatherarticle by spraying. In an embodiment, the first part of the coating composition is applied to the leather article by spraying a first layer at about 2 g / sqft onto the article. In an embodiment, the method further comprises the step (b) of drying the leather article after the first layer of the first part of the coating composition is applied. In an embodiment, the method further comprises (c) applying a second layer of the first part of the coating composition to one or more surfaces of the dried leather article. In an embodiment, the first part of the coating composition is applied to the dried leather article by spraying. In an embodiment, the first part of the coating composition is applied to the dried leather article by spraying a second layer at about 2 g / sqft onto the article. In some embodiments, the method further comprises (d) drying the leather article after the second layer of the first part of the coating composition is applied to the article. In an embodiment, the method further comprises (e) applying the second part of the coating composition to one or more surfaces of the article. In an embodiment, a second part of the coating composition comprising silk fibroin proteins or fragments thereof is applied to one or more surfaces of the article. In an embodiment, a second part of the coating composition comprising silk fibroin proteins or fragments thereof is applied to one or more surfaces of a leather article. In an embodiment, the second part of the coating composition is applied to the leather article by spraying. In an embodiment, the second part of the coating composition is applied to the leather article by spraying a layer of the second part of the coating composition at about 4 g / sqft onto the article. In an embodiment, only one layer of the second part of the coating composition is applied to the leather article. In an embodiment, the method further comprises (f) drying the leather article after the second part of the coating composition is applied to the article. In an embodiment, the coating composition comprising silk fibroin proteins or fragments thereof and a water soluble dye as a one part coating composition has a comparable performance to the two part coating composition when applied as a coating on an article. In an embodiment, the one part coating composition has a similar ability to maintain colorfastness to rubbing as the two part coating composition. Paper Transfer Process In some embodiments, a layer or coating described herein can be applied by paper transfer or paper release process. See for example Figure 129 and Figure 130. Description of a paper release process can also be found in Internation Publication No. WO2020209717, which is incorporated by reference herein. The paper release process may be useful forimprinting a grain pattern on a substrate (ex. Leather), maintaining texture integrity, imparting patterns, or textile nobilitation. Coating with Topographical Features Embodiments of the present disclosure provide an article comprising a substrate and a coating, wherein the coating comprises a base layer comprising a first polymeric macromolecular species or polymer and a top layer comprising a second polymeric macromolecular species or polymer, wherein the base layer comprises mechanically engineered topographical features on a surface opposite to the substrate, wherein the engineered topographical features have width and / or depth dimensions on a scale of from about 0 µm to about 250 µm, wherein a portion of the base layer and a portion of the top layer form a composite layer which substantially represents and / or retains the topographical features of the base layer. In some embodiments, the engineered topographical features have width and / or depth dimensions on a scale of from about 0 µm to about 50 µm, from about 50 µm to about 100 µm, from about 100 µm to about 150 µm, from about 150 µm to about 200 µm, or from about 200 µm to about 250 µm. In some embodiments, the article further comprises one or more additional layers disposed between the substrate and the base layer, the additional layers selected from a preground layer, a ground layer, and an adhesive layer. In some embodiments, the base layer topographical features are substantially different from any non-engineered topographical features of the substrate, the preground layer, the ground layer, and / or the adhesive layer. In some embodiments, the composite layer topographical features are substantially different from any non-engineered topographical features of the substrate, the preground layer, the ground layer, and / or the adhesive layer. In some embodiments, the composite layer comprises a portion of the first polymeric macromolecular species or polymer and a portion of the second polymeric macromolecular species or polymer. In some embodiments, the mechanically engineered topographical features comprise one or more of mechanically engineered embossed features, mechanically engineered relieved features, mechanically engineered recessed features, mechanically engineered imprinted features, and / or mechanically engineered repetitive features. In some embodiments, the mechanically engineered topographical features comprise one or more of mechanically engineered imprinted features and / or mechanically engineered imparted patterns. In some embodiments, the mechanically engineered topographical features comprise one or more of mechanically engineered imprinted grain patterns.In some embodiments, the mechanically engineered topographical features comprise one or more mechanically engineered imprinted fine grain features having a grain depth between 0 μm to 100 μm. In some embodiments, the mechanically engineered topographical features comprise one or more mechanically engineered imprinted fine grain features having a grain depth of between about 0 μm to about 10 μm, between about 10 μm to about 20 μm, between about 20 μm to about 30 μm, between about 30 μm to about 40 μm, between about 40 μm to about 50 μm, between about 50 μm to about 60 μm, between about 60 μm to about 70 μm, between about 70 μm to about 80 μm, between about 80 μm to about 90 μm, between about 90 μm to about 100 μm, between about 100 μm to about 110 μm, between about 110 μm to about 120 μm, between about 120 μm to about 130 μm, between about 130 μm to about 140 μm, or between about 140 μm to about 150 μm. In some embodiments, the mechanically engineered topographical features comprise one or more mechanically engineered imprinted coarse grain features having a grain depth between 100 μm to 150 μm, or between 150 μm to 500 μm. In some embodiments, the mechanically engineered topographical features comprise one or more mechanically engineered imprinted coarse grain features having a grain depth of between about 100 μm to about 110 μm, between about 110 μm to about 120 μm, between about 120 μm to about 130 μm, between about 130 μm to about 140 μm, between about 140 μm to about 150 μm, between about 150 μm to about 160 μm, between about 160 μm to about 170 μm, between about 170 μm to about 180 μm, between about 180 μm to about 190 μm, or between about 190 μm to about 200 μm. In some embodiments, the composite layer comprises a portion of the base layer and a portion of the top layer which are physically and / or chemically entangled, and / or physically and / or chemically crosslinked, and / or chemically and / or physically integrated. In some embodiments, the adhesive layer comprises and / or is generated by one or more of an acrylic dispersion, a polyurethane dispersion, a waterborne urethane-acrylic hybrid dispersion (HPDS), a wax, an oil in water emulsion, and / or a polysiloxane. In some embodiments, the first polymeric macromolecular species or polymer comprises a protein component. In some embodiments, the protein component comprises one or more of silk fibroin proteins or fragments, collagen, elastin, gelatin, corn zein, wheat gluten, pectin, chitin, casein, and / or whey. In some embodiments, the base layer comprises and / or is generated by one or more of a polyurethane dispersion, a wax, an oil in water emulsion, and / or a protein binder. In some embodiments, the first polymeric macromolecular species or polymer comprises a poly lactic acid (PLA) component, and / or a poly(lactic-co-glycolic acid) (PLGA) component. In someembodiments, the first polymeric macromolecular species or polymer comprises a biodegradable polymer. In some embodiments, the base layer has a thickness between about 10 µm and about 35 µm. In some embodiments, the base layer has a thickness between about 35 µm and about 100 µm. In some embodiments, the base layer has a thickness between about 100 µm and about 250 µm. In some embodiments, the base layer has a thickness between about 5 µm and 15 µm, between about 15 µm and 20 µm, between about 20 µm and 25 µm, between about 25 µm and 35 µm, between about 30 µm and 35 µm, or between about 35 µm and 40 µm. In some embodiments, the base layer has a thickness of about 10 µm, about 15 µm, about 20 µm, about 25 µm, about 30 µm, or about 35 µm. In some embodiments, the second polymeric macromolecular species or polymer comprises one or more of a cellulose derivative, an aliphatic or aromatic polyurethane, a silanol / amino-polysiloxane emulsions, a crosslinked PU, treated silicas, and / or a protein component. In some embodiments, the protein component comprises one or more of silk fibroin proteins or fragments, collagen, elastin, gelatin, corn zein, wheat gluten, pectin, chitin, casein, and / or whey. In some embodiments, the second polymeric macromolecular species or polymer comprises a biodegradable polymer. In some embodiments, the second polymeric macromolecular species or polymer comprises a cellulose and / or cellulose derivative component. In some embodiments, the cellulose derivative is selected from methyl cellulose, ethyl cellulose, ethyl methyl cellulose, hydroxyethyl methyl cellulose, hydroxypropyl methyl cellulose, ethyl hydroxyethyl cellulose, cellulose triacetate, cellulose propionate, cellulose nitrate, cellulose sulfate, carboxymethyl cellulose, hydroxyethyl cellulose, hydroxypropyl cellulose, cellulose acetate, cellulose acetate propionate, cellulose acetate butyrate, and microcrystalline cellulose. In some embodiments, the cellulose derivative is ethyl cellulose. In some embodiments, the ethoxyl content in ethyl cellulose is from 45.0% to 49.5%, from 45.0% to 46.0%, from 45.0% to 47.0%, from 47.0% to 48.0%, or from 48.0% to 49.5%. In some embodiments, the degree of substitution of the ethyl cellulose is 0.5 to 1, 1 to 1.5, 1.5 to 2, 2 to 2.5, or 2.5 to 3. In some embodiments, a second structure of the cellulose derivative comprises a degree of crystallinity of less than 100%, of between about 5% and less than about 100%, of between about 10% and about 20%, between about 20% and about 30%, between about 30% and about 40%, between about 40% and about 50%, between about 50% and about 60%, between about 60% and about 70%, between about 70% and about 80%, between about 80% and about 90%, between about 90% and about 99%, or between about 90% and about 100%. In some embodiments, a second structure of the cellulose derivativecomprises a degree of crystallinity of less than about 99%, less than about 98%, less than about 97%, less than about 96%, less than about 95%, less than about 94%, less than about 93%, less than about 92%, less than about 91%, less than about 90%, less than about 89%, less than about 88%, less than about 87%, less than about 86%, less than about 85%, less than about 84%, less than about 83%, less than about 82%, less than about 81%, less than about 80%, less than about 79%, less than about 78%, less than about 77%, less than about 76%, less than about 75%, less than about 74%, less than about 73%, less than about 72%, less than about 71%, less than about 70%, less than about 69%, less than about 68%, less than about 67%, less than about 66%, less than about 65%, less than about 64%, less than about 63%, less than about 62%, less than about 61%, less than about 60%, less than about 59%, less than about 58%, less than about 57%, less than about 56%, less than about 55%, less than about 54%, less than about 53%, less than about 52%, less than about 51%, less than about 50% less than about 49%, less than about 48%, less than about 47%, less than about 46%, less than about 45%, less than about 44%, less than about 43%, less than about 42%, less than about 41%, less than about 40%, less than about 39%, less than about 38%, less than about 37%, less than about 36%, less than about 35%, less than about 34%, less than about 33%, less than about 32%, less than about 31%, less than about 30% less than about 29%, less than about 28%, less than about 27%, less than about 26%, less than about 25%, less than about 24%, less than about 23%, less than about 22%, less than about 21%, less than about 20% less than about 19%, less than about 18%, less than about 17%, less than about 16%, less than about 15%, less than about 14%, less than about 13%, less than about 12%, less than about 11%, or less than about 10%. In some embodiments, the top layer has a thickness between about 5 µm and about 10 µm. In some embodiments, the top layer has a thickness between about 1 µm and about 10 µm. In some embodiments, the top layer has a thickness between about 10 µm and about 25 µm. In some embodiments, the top layer has a thickness between about 25 µm and about 50 µm. In some embodiments, the top layer has a thickness between about 5 µm and about 6 µm, between about 6 µm and about 7 µm, between about 7 µm and about 8 µm, between about 8 µm and about 9 µm, or between about 9 µm and about 10 µm. In some embodiments, the top layer has a thickness of about 5 µm, about 6 µm, about 7 µm, about 8 µm, aboubt 9 µm, or about 10 µm. In some embodiments, the thickness ratio between the base layer and the top layer ranges from about 10:1 to about 1:1. In some embodiments, the thickness ratio between the base layer and the top layer is about 10:1, about 9:1, about 8:1, about 7:1, about 6:1, about 5:1, about 4:1, about 3:1, about 2:1, or about 1:1. In some embodiments, thethickness ratio between the base layer and the top layer is between about 10:1 and about 9:1, between about 9:1 and about 8:1, between about 8:1 and about 7:1, between about 7:1 and about 6:1, between about 6:1 and about 5:1, between about 5:1 and about 4:1, between about 4:1 and about 3:1, between about 3:1 and about 2:1, or between about 2:1 and about 1:1. In some embodiments, the top layer does not include an adhesive material or cross- linker. In some embodiments, the first polymeric macromolecular species or polymer is distributed anisotropically over a cross section of the composite layer. In some embodiments, the second polymeric macromolecular species or polymer is distributed anisotropically over a cross section of the composite layer. In some embodiments, the substrate comprises an irregular surface. In some embodiments, the substrate comprises topographical features which are not mechanically engineered. In some embodiments, the coating has a thickness between about 10 µm and about 1000 µm. In some embodiments, the coating has a thickness between about 10 µm and about 100 µm, between about 100 µm and about 200 µm, between about 200 µm and about 300 µm, between about 300 µm and about 400 µm, between about 400 µm and about 500 µm, between about 500 µm and about 600 µm, between about 600 µm and about 700 µm, between about 700 µm and about 800 µm, between about 800 µm and about 900 µm, or between about 900 µm and about 1000 µm. In some embodiments, the amount of coating on the substrate is between about 0.01 g / ft2and about 25 g / ft2. In some embodiments, the amount of coating on the substrate is between about 0 g / ft2and about 5 g / ft2, between about 5 g / ft2and about 10 g / ft2, between about 10 g / ft2and about 15 g / ft2, between about 15 g / ft2and about 20 g / ft2, between about 20 g / ft2and about 25 g / ft2, between about 25 g / ft2and about 30 g / ft2, between about 30 g / ft2and about 35 g / ft2m, or between about 30 g / ft2and about 40 g / ft2, In some embodiments, the substrate comprises a substantially flexible material. In some embodiments, the substrate comprises a leather material or a textile material. In some embodiments, the substrate comprises one or more of collagen, fibroin, keratin, cellulose, and / or lignin. In some embodiments, the coating comprises one or more mattifying agent. In some embodiments, the coating comprises one or more plasticizer. In some embodiments, the coating comprises a plurality of modified fibroin fragments, each comprising one or more amino acid residue modifications selected from an asparagine to aspartic acid modification, a glutamine to glutamic acid modification, and a methionine to methionine oxide modification. In some embodiments, a plurality of modified fibroin fragments comprises one modification. In some embodiments, a plurality of modifiedfibroin fragments comprises two modifications. In some embodiments, a plurality of modified fibroin fragments comprises three modifications. In some embodiments, an asparagine to aspartic acid modification is at one or more positions selected from N23, N28, N108, N118, N136, N186, N200, N204, N240, N248, N68, N70, N77, N5262, N93, N132, N149, N172, N174, N202, N105, N4191, In some embodiments, a glutamine to glutamic acid modification is at one or more positions selected from Q24, Q149, Q202, Q58, Q139, Q275, Q5216, Q255, and Q125, In some embodiments, a methionine to methionine oxide modification is at the M64 position. In some embodiments, each modification is independently ranging in the composition between about 1% to about 99%. In some embodiments, a % modification is defined as (number of modified fibroin f...

Claims

CLAIMS1. An article comprising a substrate and a coating, wherein the coating comprises a base layer comprising a first polymeric macromolecular species or polymer and a top layer comprising a second polymeric macromolecular species or polymer, wherein the base layer comprises mechanically engineered topographical features on a surface opposite to the substrate, wherein the engineered topographical features have width and / or depth dimensions on a scale of from about 0 pm to about 250 pm. wherein a portion of the base layer and a portion of the top layer form a composite layer which substantially represents and / or retains the topographical features of the base layer.

2. The article of claim 1, further comprising one or more additional layers disposed between the substrate and the base layer, the additional layers selected from a preground layer, a ground layer, and an adhesive layer.

3. The article of claim 2, wherein the base layer topographical features are substantially different from any non-engineered topographical features of the substrate, the preground layer, the ground layer, and / or the adhesive layer.

4. The article of claim 2 or 3, wherein the composite layer topographical features are substantially different from any non-engineered topographical features of the substrate, the preground layer, the ground layer, and / or the adhesive layer.

5. The article of any one of claims 1 to 4, wherein the composite layer comprises a portion of the first polymeric macromolecular species or polymer and a portion of the second polymeric macromolecular species or polymer.

6. The article of any one of claims 1 to 5, wherein the mechanically engineered topographical features comprise one or more of mechanically engineered embossed features, mechanically engineered relieved features, mechanically engineered recessed features, mechanically engineered imprinted features, and / or mechanically engineered repetitive features.

7. The article of any one of claims 1 to 5, wherein the mechanically engineered topographical features comprise one or more of mechanically engineered imprinted features and / or mechanically engineered imparted patterns.

8. The article of any one of claims 1 to 5, wherein the mechanically engineered topographical features comprise one or more of mechanically engineered imprinted grain patterns.

9. The article of any one of claims 1 to 5, wherein the mechanically engineered topographical features comprise one or more mechanically engineered imprinted fine grain features having a grain depth between 0-100 μm.

10. The article of any one of claims 1 to 5, wherein the mechanically engineered topographical features comprise one or more mechanically engineered imprinted coarse grain features having a grain depth between 100-150 μm.

11. The article of any one of claims 1 to 10, wherein the composite layer comprises a portion of the base layer and a portion of the top layer which are physically and / or chemically entangled, and / or physically and / or chemically crosslinked, and / or chemically and / or physically integrated.

12. The article of any one of claims 4 to 11, wherein the adhesive layer comprises and / or is generated by one or more of an acrylic dispersion, a polyurethane dispersion, a waterborne urethane-acrylic hybrid dispersion (HPDS), a wax, an oil in water emulsion, and / or a poly siloxane.

13. The article of any one of claims 1 to 12, wherein the first polymeric macromolecular species or polymer compnses a protein component.

14. The article of claim 13, wherein the protein component comprises one or more of silk fibroin proteins or fragments, collagen, elastin, gelatin, com zein, wheat gluten, pectin, chitin, casein, and / or whey.

15. The article of any one of claims 1 to 13, wherein the base layer comprises and / or is generated by one or more of a polyurethane dispersion, a wax, an oil in water emulsion, and / or a protein binder.

16. The article of any one of claims 1 to 13, wherein the first polymeric macromolecular species or polymer comprises a poly lactic acid (PLA) component, and / or a poly(lactic-co-gly colic acid) (PLGA) component.

17. The article of any one of claims 1 to 16, wherein the first polymeric macromolecular species or polymer comprises a biodegradable polymer.

18. The article of any one of claims 1 to 17, wherein the base layer has a thickness between about 10 pm and about 35 pm.

19. The article of any one of claims 1 to 18, wherein the second polymeric macromolecular species or polymer comprises one or more of a cellulose derivative, an aliphatic or aromatic polyurethane, a silanol / amino-poly siloxane emulsions, a crosslinked PU, treated silicas, and / or a protein component.

20. The article of claim 19. wherein the protein component comprises one or more of silk fibroin proteins or fragments, collagen, elastin, gelatin, com zein, wheat gluten, pectin, chitin, casein, and / or whey.

21. The article of any one of claims 1 to 20, wherein the second polymeric macromolecular species or polymer comprises a biodegradable polymer.

22. The article of any one of claims 1 to 21, wherein the second polymeric macromolecular species or polymer comprises a cellulose and / or cellulose derivative component.

23. The article of claim 22, wherein the cellulose derivative is selected from methyl cellulose, ethyl cellulose, ethyl methyl cellulose, hydroxyethyl methyl cellulose, hydroxypropyl methyl cellulose, ethyl hydroxyethyl cellulose, cellulose triacetate, cellulose propionate, cellulose nitrate, cellulose sulfate, carboxymethyl cellulose, hydroxyethyl cellulose, hydroxypropyl cellulose, cellulose acetate, cellulose acetate propionate, cellulose acetate butyrate, and microcrystalline cellulose.

24. The article of claim 23, wherein the cellulose derivative is ethyl cellulose.

25. The article of claim 23 or 24. wherein the ethoxyl content in ethyl cellulose is from 45.0% to 49.5%, from 45.0% to 46.0%, from 45.0% to 47.0%, from 47.0% to 48.0%, or from 48.0% to 49.5%.

26. The article of claim 24 or 25, wherein the degree of substitution of the ethyl cellulose is 0.5 to 1, 1 to 1.

5. 1.5 to 2, 2 to 2.5, or 2.5 to 3.

27. The article of any one of claims 24 to 26, wherein a second structure of the cellulose derivative comprises a degree of crystallinity of less than 100%, of between about 5% and less than about 100%, of between about 10% and about 20%, between about 20% and about 30%. between about 30% and about 40%. between about 40% and about 50%, between about 50% and about 60%, between about 60% and about 70%, between about 70% and about 80%, between about 80% and about 90%, between about 90% and about 99%, or between about 90% and about 100%.

28. The article of any one of claims 24 to 26, wherein a second structure of the cellulose derivative comprises a degree of crystallinity of less than about 99%. less than about 98%, less than about 97%, less than about 96%, less than about 95%, less than about 94%, less than about 93%, less than about 92%, less than about 91%, less than about 90%, less than about 89%, less than about 88%, less than about 87%, less than about 86%, less than about 85%. less than about 84%. less than about 83%. less than about 82%, less than about 81%, less than about 80%, less than about 79%, less than about 78%, less than about 77%,less than about 76%, less than about 75%, less than about 74%, less than about 73%, less than about 72%. less than about 71%. less than about 70%. less than about 69%, less than about 68%, less than about 67%, less than about 66%, less than about 65%, less than about 64%, less than about 63%, less than about 62%, less than about 61%, less than about 60%, less than about 59%, less than about 58%, less than about 57%, less than about 56%, less than about 55%, less than about 54%, less than about 53%, less than about 52%, less than about 51%, less than about 50% less than about 49%, less than about 48%, less than about 47%, less than about 46%, less than about 45%, less than about 44%, less than about 43%, less than about 42%, less than about 41%, less than about 40%, less than about 39%, less than about 38%, less than about 37%, less than about 36%, less than about 35%, less than about 34%, less than about 33%. less than about 32%. less than about 31%. less than about 30% less than about 29%, less than about 28%, less than about 27%, less than about 26%, less than about 25%, less than about 24%, less than about 23%, less than about 22%, less than about 21%, less than about 20% less than about 19%, less than about 18%, less than about 17%, less than about 16%, less than about 15%, less than about 14%, less than about 13%, less than about 12%, less than about 11%. or less than about 10%.

29. The article of any one of claims 1 to 28, wherein the top layer has a thickness between about 5 μm and about 10 μm.

30. The article of any one of claims 1 to 29, wherein the thickness ratio between the base layer and the top layer ranges from about 10: 1 to about 1:1.

31. The article of any one of claims 1 to 30, wherein the top layer does not include an adhesive material or cross-linker.

32. The article of any one of claims 1 to 31, wherein the first polymeric macromolecular species or polymer is distributed anisotropically over a cross section of the composite layer.

33. The article of any one of claims 1 to 31, wherein the second polymeric macromolecular species or polymer is distributed anisotropically over a cross section of the composite layer.

34. The article of any one of claims 1 to 33, wherein the substrate comprises an irregular surface.

35. The article of any one of claims 1 to 33, wherein the substrate comprises topographical features which are not mechanically engineered.

36. The article of any one of claims 1 to 35, wherein the coating has a thickness between about 10 μm and about 1000 μm.

37. The article of any one of claims 1 to 36, wherein the amount of coating on the substrate is between about 0.01 g / ft2and about 25 g / ft2.

38. The article of any one of claims 1 to 37, wherein the substrate comprises a substantially flexible material.

39. The article of any one of claims 1 to 38, wherein the substrate comprises a leather material or a textile material.

40. The article of any one of claims 1 to 39, wherein the substrate comprises one or more of collagen, fibroin, keratin, cellulose, and / or lignin.

41. The article of any one of claims 1 to 40, wherein the coating comprises one or more mattifying agent.

42. The article of any one of claims 1 to 40, wherein the coating comprises one or more plasticizer.

43. The article of any one of claims 1 to 42, wherein the coating comprises a plurality of modified fibroin fragments, each comprising one or more amino acid residue modifications selected from an asparagine to aspartic acid modification, a glutamine to glutamic acid modification, and a methionine to methionine oxide modification.

44. The article of claim 43, wherein a plurality of modified fibroin fragments comprises one modification.

45. The article of claim 43, wherein a plurality of modified fibroin fragments comprises two modifications.

46. The article of claim 43, wherein a plurality of modified fibroin fragments comprises three modifications.

47. The article of any one of claims 43 to 46, wherein an asparagine to aspartic acid modification is at one or more positions selected from N23. N28, N 108, N 118, N 136, N 186, N200, N204, N240, N248, N68, N70, N77, N5262, N93, N132, N149, N172, N174, N202, N105, N4191,48. The article of any one of claims 43 to 46, wherein a glutamine to glutamic acid modification is at one or more positions selected from Q24, Q149, Q202. Q58, Q139, Q275, Q5216. Q255, and Q 125,49. The article of any one of claims 43 to 46, wherein a methionine to methionine oxide modification is at the M64 position.

50. The article of any one of claims 43 to 49, wherein each modification is independently ranging in the composition between about 1% to about 99%.

51. The article of any one of claims 43 to 50, wherein a % modification is defined as (number of modified fibroin fragments having a modification at a specific position divided by the total number of modified fibroin fragments which include the specific position, modified or unmodified) x 100.

52. A method of coating a substrate with a composite coat, the method comprising applying to the substrate a base layer coating composition through a release paper method, wherein the release paper forms a plurality of mechanically engineered topographical features on the base layer opposite to a surface applied to the substrate, wherein the engineered topographical features have width and / or depth dimensions on a scale of from about 0 pm to about 250 μm, and applying atop layer coating composition.

53. The method of claim 52, further comprising applying to the substrate one or more additional layers coating compositions prior to applying the base layer coating composition, the additional layers selected from a preground layer, a ground layer, and an adhesive layer.

54. The method of claim 52 or 53, wherein an adhesive layer coating composition comprises one or more of an acrylic dispersion, a polyurethane dispersion, a waterborne urethane-acrylic hybrid dispersion (HPDS), a wax, an oil in water emulsion, and / or a polysiloxane55. The method of any one of claims 52 to 54, wherein a base layer coating composition comprises a protein component.

56. The method of claim 55, wherein the protein component comprises one or more of silk fibroin proteins or fragments, collagen, elastin, gelatin, com zein, wheat gluten, pectin, chitin, casein, and / or whey.

57. The method of any one of claims 52 to 56, wherein a base layer coating composition comprises one or more of a polyurethane dispersion, a wax, an oil in water emulsion, and / or a protein binder.

58. The method of any one of claims 52 to 56, wherein a base layer coating composition comprises a poly lactic acid (PLA) component, and / or a poly(lactic-co-glycolic acid) (PLGA) component.

59. The method of any one of claims 52 to 56. wherein a base layer coating composition comprises a biodegradable polymer.

60. The method of any one of claims 52 to 59, wherein a top layer coating composition comprises one or more of a cellulose derivative, an aliphatic or aromatic polyurethane, a silanol / amino-polysiloxane emulsions, a crosslinked PU, treated silicas, and / or a protein component.

61. The method of claim 60, wherein a top layer coating composition comprises one or more of silk fibroin proteins or fragments, collagen, elastin, gelatin, com zein, wheat gluten, pectin, chitin, casein, and / or whey.

62. The method of any one of claims 52 to 61, wherein a top layer coating composition a biodegradable polymer.

63. The method of any one of claims 52 to 61, wherein a top layer coating composition comprises a cellulose and / or cellulose derivative component.

64. The method of claim 63, wherein the cellulose derivative is selected from methyl cellulose, ethyl cellulose, ethyl methyl cellulose, hydroxyethyl methyl cellulose, hydroxypropyl methyl cellulose, ethyl hydroxyethyl cellulose, cellulose triacetate, cellulose propionate, cellulose nitrate, cellulose sulfate, carboxymethyl cellulose, hydroxyethyl cellulose, hydroxypropyl cellulose, cellulose acetate, cellulose acetate propionate, cellulose acetate butyrate, and microcrystalline cellulose.

65. The method of claim 63, wherein the cellulose derivative is ethyl cellulose.

66. The method of claim 64 or 65. wherein the ethoxyl content in ethyl cellulose is from 45.0% to 49.5%, from 45.0% to 46.0%, from 45.0% to 47.0%, from 47.0% to 48.0%. or from 48.0% to 49.5%.

67. The method of claim 65 or 66, wherein the degree of substitution of the ethyl cellulose is 0.5 to 1, 1 to 1.

5. 1.5 to 2, 2 to 2.5, or 2.5 to 3.

68. The method of any one of claims 65 to 67. wherein a second structure of the cellulose derivative comprises a degree of crystallinity of less than 100%, of between about 5% and less than about 100%, of between about 10% and about 20%, between about 20% and about 30%. between about 30% and about 40%, between about 40% and about 50%, between about 50% and about 60%, between about 60% and about 70%. between about 70% and about 80%, between about 80% and about 90%, between about 90% and about 99%, or between about 90% and about 100%.

69. The method of any one of claims 65 to 67, wherein a second structure of the cellulose derivative comprises a degree of crystallinity’ of less than about 99%, less than about 98%. less than about 97%. less than about 96%. less than about 95%. less than about 94%, less than about 93%, less than about 92%, less than about 91%, less than about 90%, less than about 89%, less than about 88%, less than about 87%, less than about 86%, less than about 85%. less than about 84%. less than about 83%. less than about 82%. less than about 81%. less than about 80%. less than about 79%. less than about 78%. less than about 77%. less than about 76%, less than about 75%, less than about 74%, less than about 73%, less thanabout 72%. less than about 71%. less than about 70%. less than about 69%. less than about 68%. less than about 67%. less than about 66%. less than about 65%. less than about 64%. less than about 63%, less than about 62%, less than about 61%, less than about 60%, less than about 59%, less than about 58%, less than about 57%, less than about 56%, less than about 55%, less than about 54%, less than about 53%, less than about 52%, less than about 51%, less than about 50% less than about 49%, less than about 48%, less than about 47%, less than about 46%. less than about 45%. less than about 44%. less than about 43%. less than about 42%, less than about 41%, less than about 40%, less than about 39%, less than about 38%, less than about 37%, less than about 36%, less than about 35%, less than about 34%, less than about 33%. less than about 32%. less than about 31%. less than about 30% less than about 29%. less than about 28%. less than about 27%. less than about 26%. less than about 25%. less than about 24%, less than about 23%, less than about 22%, less than about 21%, less than about 20% less than about 19%, less than about 18%, less than about 17%, less than about 16%, less than about 15%, less than about 14%, less than about 13%, less than about 12%, less than about 11%, or less than about 10%.

70. The method of any one of claims 52 to 69. wherein the substrate comprises a substantially flexible material.

71. The method of any one of claims 52 to 69, wherein the substrate comprises a leather material or a textile material.

72. The method of any one of claims 52 to 69. wherein the substrate comprises one or more of collagen, fibroin, keratin, cellulose, and / or lignin.

73. The method of any one of claims 52 to 72, wherein a coating composition comprises a mattifying agent.

74. The method of any one of claims 52 to 72. wherein a coating composition comprises a plasticizer.

75. The method of any one of claims 52 to 74, wherein a coating composition comprises a plurality of modified fibroin fragments, each comprising one or more amino acid residue modifications selected from an asparagine to aspartic acid modification, a glutamine to glutamic acid modification, and a methionine to methionine oxide modification.

76. The method of claim 75, wherein a plurality of modified fibroin fragments comprises one modification.

77. The method of claim 75, wherein a plurality of modified fibroin fragments comprises two modifications.

78. The method of claim 75, wherein a plurality of modified fibroin fragments comprises three modifications.

79. The method of any one of claims 75 to 78, wherein an asparagine to aspartic acid modification is at one or more positions selected from N23, N28, N108, N118, N136, N186, N200, N204, N240, N248, N68, N70, N77, N5262, N93, N132, N149, N172, N174, N202, N105, N4191.

80. The method of any one of claims 75 to 78. wherein a glutamine to glutamic acid modification is at one or more positions selected from Q24, Q149, Q202, Q58, Q139, Q275, Q5216, Q255, and Q125.

81. The method of any one of claims 75 to 78, wherein a methionine to methionine oxide modification is at the M64 position.

82. The method of any one of claims 75 to 81, wherein each modification is independently ranging in the composition between about 1% to about 99%.

83. The method of any one of claims 75 to 82, wherein a % modification is defined as (number of modified fibroin fragments having a modification at a specific position divided by the total number of modified fibroin fragments which include the specific position, modified or unmodified) x 100.

84. The method of any one of claims 52 to 83, wherein a coating composition further comprises a solvent component.

85. The method of claim 84, wherein the solvent component comprises an alcohol and / or an alcohol derivative.

86. The method of claim 84 or 85, wherein the solvent component comprises one or more of an alcohol, an ether, a ketone, an aldehyde, and / or a ketal.

87. The method of any one of claims 84 to 86. wherein the solvent component is from about 75% w / w to about 99% w / w of the coating composition, from about 80% w / w to about 98% w / w of the coating composition, from about 85% w / w to about 97.5% w / w of the coating composition, or from about 85% w / w to about 95% w / w of the coating composition.

88. The method of any one of claims 84 to 87, wherein the solvent component comprises one or more of methanol, ethanol, n-propanol, 2-propanol. n-butanol, 2-butanoL pentanol, hexanol, acetone, butanone, methoxypropanol, di-isopropylidene glycerol, 2,2- dimethyl-4-hydroxymethyl- 1,3 -dioxolane, 2,2-dimethyl-1,3-dioxolane-4-methanol, or any combination thereof.

89. The method of any one of claims 52 to 88, wherein a coating composition comprises one or more of a polyethylene glycol (PEG) component, a polypropylene glycol (PPG) component, and / or a polyether component.

90. The method of any one of claims 52 to 88, wherein a coating composition comprises one or more of fatty acid or fatty acid derived amide, and / or a monoglyceride, diglyceride, and / or triglyceride.

91. The method of any one of claims 52 to 88. wherein a coating composition comprises one or more of a triethylene glycol monomethyl ether component, a diethylene glycol butyl ether component, a diethylene glycol ethyl ether component, a dimethyl tetradecanedi oate component, an erucamide component, and / or a glyceryl stearate component.

92. The method of any one of claims 52 to 91, wherein a coating composition comprises water.

93. The method of any one of claims 52 to 92, wherein a coating composition comprises a mattifying agent.

94. The method of any one of claims 52 to 92. wherein a coating composition comprises a plasticizer.

95. The method of any one of claims 52 to 94, further comprising one or more pressing steps, and / or one or more drying or partial drying steps.

96. The method of any one of claims 52 to 95. wherein a first coating composition is partially polymerized, partially dried, and / or partially cured before a second coating composition is applied.

97. The method of any one of claims 52 to 96, wherein a coating composition is applied at a rate from about 0.5 mL / ft2to about 5 mL / ft2.

98. An article comprising a substrate and a coating, the article made by a method of any one of claims 52 to 97.

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