Methods for cosmetic skin remodeling

Abstract

The methods described herein provide self-assembling macromolecular networks within human skin. These methods provide immediate and cumulative physical properties within the skin, resulting in cosmetic benefits including plumping / filling, strengthening, smoothing, firming, and lifting, as well as enhanced optical properties, radiance, and other cosmetic appearance characteristics. This disclosure also provides methods for reconstructing skin without cellular biogenesis by generating macrostructures within the skin. These methods include achieving intradermal self-assembly by topically applying a composition comprising at least one self-assembly material to form functional macrostructures within the skin, and achieving in vivo self-assembly of at least one self-assembly material while substantially preventing self-assembly prior to topical application or treatment.

Description

Method for aesthetic skin remodeling Priority Information This application claims priority to U.S. Provisional Patent Application No. 62 / 914,201, filed on October 11, 2019, the content of which is incorporated herein by reference in its entirety. This disclosure relates to the field of aesthetic or dermatological compositions. More particularly, this disclosure relates to the field of aesthetic compositions comprising at least one self-assembling material that self-assembles into macroscopic structures within the skin layers. Self-assembly is an elegant and advantageous "bottom-up" approach towards the design of ordered, three-dimensional and biocompatible nanobiomaterials. Due to the highly specific interactions between structural units, reproducible macromolecular nanostructures can be obtained. These intermolecular associations organize supramolecular structures and are mainly non-covalent electrostatic interactions, hydrogen bonds, van der Waals forces, etc. Supramolecular chemistry or biology aggregates a large number of two-dimensional or three-dimensional (2D or 3D) complex structures and entities formed by the association of chemical or biological substances. These associations are governed by the principles of molecular complementarity or molecular recognition and self-assembly. Knowledge of the rules of intermolecular association can be used to design multi-molecular assemblies in the form of membranes, thin films, layers, micelles, nanotubes or gels for various biomedical or technological applications. In biological systems, these self-assembling molecules are usually lipids, peptides, proteins, sugars and nucleic acids. Peptides are versatile building blocks for fabricating supramolecular structures. Their ability to adopt specific secondary structures, as dictated by the amino acid sequence, provides a unique platform for the design of self-assembling biomaterials with hierarchical 3D macromolecular structures, nano-scale to macro-scale features and tunable physical properties. For example, peptides are able to assemble into nanotubes (U.S. Patent No. 7,179,784) or into supramolecular hydrogels consisting of a 3D scaffold with a large amount of immobilized water or aqueous solution of about 98 - 99%. Peptide-based biomaterials are powerful tools for potential applications in biotechnology, medicine and other technological applications. Depending on their respective properties, these peptide-based hydrogels are considered for the development of new materials for tissue engineering, regenerative medicine, as drug and vaccine delivery vehicles or as peptide chips for drug research and diagnostics. There is also strong interest in using peptide-based self-assembling biomaterials such as gels for the development of molecular electronics. A variety of "intelligent peptide hydrogels" have been generated that respond to external manipulations such as temperature, pH, mechanical influences or other stimuli with a dynamic behavior of swelling, shrinking or decomposing. However, these biomaterials are still not "developed" enough to mimic natural tissues such as the extracellular matrix (ECM) or cartilage tissue or other biological differences. The challenge for the meaningful use of peptide hydrogels is to mimic and replace natural tissues, not only as "space fillers" or mechanical scaffolds, but also to understand and address the biochemical signals and physiological requirements for keeping the contained cells in the correct position and under "in vivo" conditions. To rationally design suitable hydrogels, many efforts have been made to understand and control the relationship between peptide sequence and structure. Generally, hydrogels contain macroscopic structures such as fibers that tangle and form a network. Most peptide-based hydrogels utilize β-sheet sheets assembled into fibers as building blocks. In addition to materials based on β-sheet structures, self-assembling hydrogels can also be obtained from α-helical peptides. However, currently known peptide hydrogels are in most cases associated with low rigidity, sometimes unfavorable physiological properties and / or complexity, and are associated with a large amount of processing thereof, which results in high production costs.Accordingly, there is a widely recognized need for peptide hydrogels that are easy to form, non-toxic, and have a rigidity high enough for standard applications. The hydrogel should also be suitable for delivering bioactive moieties (such as nucleic acids, small molecule therapeutics, cosmeceuticals, and antimicrobials) and / or used as a biomimetic scaffold that supports in vivo and in vitro cell growth and promotes the regeneration of native tissues and / or used for 2D and / or 3D biomanufacturing. Self-assembly is a powerful design paradigm for generating complex molecular assemblies from a limited number of structural units. Little or no reports have utilized self-assembling networks for topical application to the skin and scalp with the intention of generating systems that form supramolecular structures in a specified space within or on the skin tissue. These applications have complex requirements for any self-assembling system, including personal care, cosmetic methods and formulations, their compatibility and stability, application outside the target tissue, penetration into the correct site or layer in the skin or scalp, the inherent physicochemical properties within the skin layer, and the need to control where self-assembly occurs on the packaging surface, between formulations, on the skin surface, or within the skin. The methods described herein provide macromolecular networks that self-assemble within human skin. The methods provide physical properties based on accumulation within the skin that cause cosmetic benefits, including swelling / plumping, filling, strengthening, smoothing, tightening, and lifting, as well as enhancing the optical properties, luminance, and other cosmetic appearance characteristics of the skin. The present disclosure provides methods for restructuring the skin without cell biogenesis by affecting the macroscopic structure within the skin. The methods include achieving self-assembly within the skin layer by applying a cosmetic composition comprising at least one self-assembling material, wherein the self-assembling material forms a functional macroscopic structure within the skin. The methods further include achieving self-assembly of the at least one self-assembling material in vivo while substantially preventing self-assembly of the at least one self-assembling material in the composition prior to topical application or treatment. The self-assembling material comprises at least one oligomer. The self-assembling material further comprises more than one oligomer capable of self-assembling with each other in the skin. The methods provide at least one cosmetic skin care, hair care, or cosmetic benefit. The cosmetic benefits include improving wrinkles, fine lines, pores, sagging, anti-aging, swelling / plumping, filling, barrier strengthening, smoothing, tightening, the optical properties of the skin, lifting, luminance, or gloss. The functional macroscopic structure is 3D, and the oligomers form a functional macroscopic structure within the skin after triggering. The triggering is temperature, ionic strength, concentration, pH, solvent, or a combination thereof, or the application of a second composition before or after topical application or treatment. Specifically, the triggering includes a pH in the range of about 3-9, a pH change of 0.001-5 pH units, a gradient of temperature, pH, salt, or ions present in the skin layer, a change in salt concentration, or a change in the concentration of the self-assembling material. Specifically, the pH triggering is a change in the pH value within the skin layer from a non-physiological pH to a physiological pH value. The self-assembly is achieved within 6 hours after topical application of the cosmetic composition. Unless otherwise specified, all percentages and ratios used herein are by weight of the total composition, and all measurements are made at 25 °C. All numerical ranges include narrower ranges; the upper and lower limits depicted are interchangeable to generate other ranges not explicitly depicted. The compositions can contain the essential components and optional ingredients described herein, consist essentially of, or consist of them. As used herein, "consisting essentially of" means that the composition or component can include additional ingredients, but only if the additional ingredients do not substantially alter the basic and novel characteristics of the claimed composition or method. The terms "apply" or "application" as used with respect to a composition mean contacting or spreading the composition onto a substrate, such as the surface of human skin or the epidermis. As used herein, the term "dermatologically or cosmetically acceptable" means that the composition or component is suitable for contact with human skin tissue without undue toxicity, incompatibility, instability, allergic reaction, etc. As used herein, the term "facial skin surface" means one or more of the forehead, periorbital, cheek, perioral, chin, and nasal skin surfaces. While the facial skin surface is of interest and is exemplified herein, other skin surfaces can also be treated with the composition, e.g., surfaces that are not normally covered by clothing, such as the facial skin surface, hand and arm skin surfaces, foot and leg skin surfaces, and neck and chest skin surfaces (e.g., décolletage). As used herein, the term "keratinized tissue" means the keratin-containing layer that is the outermost protective covering of a mammal, including but not limited to skin, scalp, mucous membranes, lips, hair, toenails, fingernails, stratum corneum, hooves, etc. As used herein, the terms "topical application", "topically", and "topical" mean applying (e.g., spreading, spraying) the composition onto the surface of the keratinized tissue. As used herein, the term "effective amount" means an amount of a compound or composition sufficient to significantly induce a positive keratinized tissue benefit, including independently or in combination with other benefits disclosed herein. This means that the content and / or concentration of the agent in the formulation is sufficient such that when the formulation is applied at a normal frequency and normal amount, the formulation can result in the treatment of one or more undesirable keratinized tissue conditions (e.g., skin wrinkles). For example, the amount can be sufficient to inhibit or enhance some biochemical functions occurring within the keratinized tissue. Such an amount of a skin care agent can vary depending on the type of product, the type of keratinized tissue condition to be treated, etc. As used herein, the term "self-assembly" means that materials (e.g., but not limited to molecules, biomolecules, DNA, polysaccharides, polymers, colloids, or macroscopic particles) organize and assemble into an ordered and / or functional and well-defined 2D or 3D macroscopic structure or pattern due to specific local interactions. Such 2D or 3D macroscopic structures or assemblies can directly confer benefits, including but not limited to the physical properties of tissues, skin layers, such as volume, turgor, elasticity, light scattering, etc.Although external guidance is not required to physically sort materials, external conditions (such as temperature, pressure, ionic strength, salt strength, pH, and other factors) can affect whether the self-assembly of certain materials can occur. In certain cases, for example, the self-assembly of molecules is defined as the ability of specific molecules (such as, but not limited to, oligomers of macromolecules) to spontaneously non-covalently bind to themselves under appropriate conditions and form large, ordered, well-defined 3D functional macroscopic structures within the skin layer or on or within body tissues. The macroscopic structures can range within the nanoscale or millimeter scale. As used herein, the term "co-assembly" refers to the organization of molecules, biomolecules, or materials (such as, but not limited to, molecules, polymers, DNA, polysaccharides, colloids, or macroscopic particles) into ordered and / or functional and well-defined 2D or 3D macroscopic structures or patterns due to specific local interactions between the components themselves. In certain cases, specific molecules (such as oligomers of macromolecules) spontaneously non-covalently bind to other complementary oligomers under appropriate conditions and form a binary system with a larger 3D structure. In addition, the term "self-assembly" is meant to include the term "co-assembly" as it relates to the formation of such self-directed ordered systems. As used herein, the term "self-assembling peptide" refers to a peptide or combination of peptides formed by a chain of at least two amino acids (α-amino acid residues) connected by covalent bonds (such as peptide bonds), wherein the peptide self-assembles upon contact with body tissues within, on, or in skin tissue to form a matrix. Self-assembling peptides can be branched, in which case they will contain at least two chains of amino acids connected by non-peptide bonds. In addition, the length of self-assembling peptides can vary as long as they can self-assemble in vivo. Although the amino acid sequences of self-assembling peptides can vary, in certain cases, the sequences can include those that provide amphiphilic properties to the self-assembling peptides. For example, self-assembling peptides can include (but not necessarily) approximately equal numbers of hydrophobic and hydrophilic amino acids. The term "macroscopic" refers to dimensions large enough to be visible at a magnification of 10-fold or greater. Macroscopic structures can be two-dimensional or three-dimensional. As used herein, the term "skin active agent" refers to an active ingredient that provides cosmetic and / or dermatological effects to the application area on the skin. As used herein, the terms "stable" and "stability" refer to the chemical state, physical homogeneity, and / or color of a composition remaining substantially unchanged when the composition is at a temperature of about 4°C to about 50°C, with and / or without humidity conditions. As used herein, the term "subcutaneous" refers to within or penetrating the epidermis. As used herein, the term "transdermal" refers to the application of a material or composition through the skin surface. Human skin is divided into three layers: the epidermis, the dermis, and the subcutaneous tissue or hypodermis. The epidermis includes an outer layer and an inner layer. At the base of the epidermis, there are cells called melanocytes (about 5% of epidermal cells). The dermis or middle layer contains collagen and other materials essential for skin strength and its self-repair ability. The subcutaneous layer or hypodermis serves to insulate the body.The present disclosure relates to methods and cosmeceutical and dermatological formulations or compositions comprising materials that self-assemble within the skin following topical administration. The compositions comprise self-assembling molecules including, but not limited to, lipids, peptides, polysaccharides, nucleic acids, surfactants and their derivatives and other molecules including derivatives, alone or in combination to form one or more highly ordered structures within skin tissue or on skin tissue present within the skin layers by non-invasive topical application. Thus, such topical administration achieves skin effects and cosmetic benefits such as, but not limited to, lifting, tightening and plumping, etc. Self-assembly Self-assembly is the arrangement or organization of molecules into structurally well-defined arrangements under certain conditions. Such organization can occur spontaneously or can occur subsequent to conditions that favor such self-assembly. The self-assembly of molecules is caused by non-covalent interactions and physical bonds. Non-covalent interactions include hydrogen bonds, ionic bonds and van der Waals forces, etc., which are necessary to assemble molecules into well-defined organized structures with complementarity and structural compatibility. Self-assembling materials are molecules including, but not limited to, oligomers of peptides, DNA, polysaccharides, sugars, polymers and carbohydrates, which can self-assemble into organized structures within the skin upon triggering. Due to the conditions present in the formulation, self-assembly is substantially prevented from occurring in the composition prior to administration or processing; however, when an appropriate trigger is applied, or appropriate conditions or molecules are present in the skin layers and induce assembly, self-assembly occurs in vivo. Due to the self-arrangement of the molecules within the skin layers, various physical effects occur in the target layer of the skin, resulting in cosmetic benefits such as skin lifting, tightening, reduction of fine lines, effect on pores on the skin, wrinkles, thickening of the epidermal layer, etc. In addition, the methods and compositions also provide enhanced delivery of active agents within the skin layers, thereby providing structural and physical enhancement to the skin by topical application. Another object of the present disclosure is to provide a method of topical administration that utilizes a new, self-spreading mechanism that adds new structures to the skin that alter the physical and mechanical properties within the skin and tissue layers without involving the induction of new biogenesis by skin cells, including tissue or cell biogenesis. Specifically, a physical phenomenon is described herein that enables the human skin to be reconfigured by altering the physical and mechanical properties of the human skin within the skin layers without participating in cell biogenesis and via topical application. The physical self-assembly phenomenon provides at least one skin benefit that is perceived soon after or subsequent to treatment, preferably immediately or subsequent to topical application. The physical self-assembly phenomenon also enables the skin to be macroscopically reconfigured by altering the mechanical properties of the skin at a desired location within the skin layers. The macroscopic structure or element can be 2D or 3D. If 2D, the macroscopic structure comprises more than one monolayer of molecules, such as, but not limited to, at least two or more layers of molecules contributing to the structural change. The size of the macroscopic structure assembly can range from nanometers to millimeters. Macroscopic 2D assemblies or structures include, for example, nanoribbons or belts, etc. Self-assembly of self-assembling materials is the ability of oligomers of macromolecules (e.g., peptides, peptidomimetics, proteins, carbohydrates, oligonucleotides, DNA, RNA, lipids and their derivatives, etc.) to non-covalently bind to themselves spontaneously under appropriate conditions and form ordered well-defined 2D or 3D structures. Self-assembling materials include molecules such as, but not limited to, oligomers of peptides, DNA, carbohydrates, lipids, synthetic hybrids, and / or combinations thereof, which can self-assemble into organized structures in the skin upon triggering. When a self-assembling material (e.g., a peptide) is topically applied to the skin, the material migrates through the tissue under controlled conditions (i.e., a selected trigger) and self-assembles within the skin layers. Selected triggers include gradient conditions present within the skin layers; changes in conditions between the formulation and the skin layers, e.g., changes in the values of temperature, pH, salinity, ionic strength, or peptide concentration between the composition and the skin layers; conditions present within the skin layers, including body temperature, pH, ions, salinity, ionic strength, enzyme concentration, peptide amount; or molecules within the skin, such as elastin, fibronectin, collagen, hyaluronic acid, etc. Similarly, mixtures of materials can also be applied, such as oligomers of peptides, multiple peptides, multiple types of peptides, or multiple oligomers, to achieve an effect. In some specific cases, when delivered within the skin layers, multiple peptides of different classes or types start to co-aggregate, causing self-assembly, otherwise the multiple peptides do not bind to each other. Thus, self-assembly is induced in vivo within the skin, caused by a selected trigger, while substantially preventing self-assembly from occurring in the composition prior to application or treatment. When the composition is topically applied to the skin, the material migrates through the skin, and when the material is delivered within the skin layers, self-assembly is triggered and induced by a selected trigger as described herein. The trigger can be applied as a subsequent application of different compositions or through gradient conditions within the skin layers (including pH, temperature, salinity, ionic strength, enzyme concentration, etc.), or through changes in the values of such conditions (i.e., not limited to changes in the values of pH, ionic strength, salinity, solvent, enzyme concentration, light, or temperature between the composition and the skin layers), or through molecules present within the skin layers. This physical phenomenon achieves the remodeling of the skin by changing its mechanical properties at the desired location within the skin, without participating in new cell or tissue biogenesis. Thus, the methods and compositions provide cosmetic or dermatological benefits by achieving self-assembly within the skin and by achieving the mechanical and physical properties of the skin, e.g., reducing fine lines and wrinkles, reducing pores, increasing skin tightness, elasticity, and smoothness, increasing plumpness, brightness, etc. A. Self-assembling peptides disclose a composition comprising oligomers, i.e., peptides, capable of self-assembling within the skin. As used herein, the term "peptide" includes "polypeptide", "oligopeptide", and "protein", and refers to a string of at least two α-amino acid residues linked together by covalent bonds (such as peptide bonds). The length of such peptides can vary as long as they retain the ability to self-assemble to an extent useful for one or more of the purposes described herein. Peptides having as few as two α-amino acid residues or as many as about 200 residues may be suitable, and those peptides identified as self-assembling typically have lengths within this range (e.g., 4-200, 8-36, 8-24, 8-16, 12-20, 6-64, 4-8, 5-10, 2-6, 1-8, 16-20, 2-42, 5-40, 10-40 amino acid residues, including all ranges and sub-ranges therein). "Peptide" can refer to a single peptide or a collection of peptides having the same or different sequences, any of which may include only naturally occurring α-amino acid residues, non-naturally occurring α-amino acid residues, or both. α-Amino acid analogs are also known in the art and can alternatively be used. In particular, D-forms of α-amino acid residues can be used. Additionally, one or more amino acid residues in the self-assembling peptide can be altered or derivatized by the addition of chemical entities such as acyl, alkyl, glycosyl, glycan, phosphate, farnesyl, geranylgeranyl, fatty acid groups, or linkers for conjugation or functionalization. Useful peptides can also be branched, in which case they will contain at least two amino acid residues, each amino acid residue consisting of at least three amino acid residues linked by peptide bonds. In some cases, the two amino acid residues themselves may not be linked by a peptide bond. The amino acid residues in the self-assembling peptide can be naturally occurring or non-naturally occurring amino acid residues. Naturally occurring amino acids can include amino acid residues encoded by the standard genetic code as well as non-standard amino acids (e.g., amino acids having a D-configuration rather than an L-configuration), and those amino acids that can be formed by modification of standard amino acids. Atypical or non-naturally occurring amino acids have not been found in nature but can be incorporated into the peptide chain. Self-assembling peptides can be chemically synthesized, enriched, or purified from natural or recombinantly produced sources by methods well known in the art. For example, peptides can be synthesized using standard Fmoc chemistry and purified using high performance liquid chromatography (HPLC). Tables 1, 2, and 3 include non-limiting exemplary representations of self-assembling peptides. Table 1 indicates the sequences of exemplary peptides, while Tables 2 and 3 show chemical structures. Specifically, Table 2 relates to the respective chemical structures corresponding to Table 1 (SEQ ID NO:1-8 and Serial No.#1-9). Table 3 relates to the backbone chemical structures of the respective sequences of Table 1. The sequence listing file in ASCII text format is identified as: 18 21_Seq_Listing.txt, created on October 8, 2020, size: 2KB, which is incorporated herein by reference in its entirety. Tables 1, 2, and 3 are representative and not exclusive. Other self-assembling peptides different from those listed in Tables 1-3 can also be generated, for example, by replacing single or multiple amino acids, by including or excluding repeating amino acids, or by incorporating one or more amino acids such that non-covalent bonds can be increased or decreased, and thus modifying the macroscopic structure that self-assembles within the skin. All such modifications and substitutions or combinations are within the scope of this disclosure. To form 3D macromolecular structures in vivo within the skin, in certain compositions, the self-assembling peptides are structurally compatible. For example, side chains (amino acid R groups) of self-assembling peptides that are uncharged (neutral) at physiological pH can be provided, such as glycine or valine. Such self-assembling peptides can have a neutral charge, be neutral, or can contain amino acids that are uncharged at physiological pH. If charged or neutral amino acids in the self-assembling peptide are replaced with similar charges, there is no known significant effect on the self-assembly process. For example, neutral charged valine at position 1 can be replaced with isoleucine. However, if neutral charged residues are replaced with negatively charged residues (such as aspartates and glutamates), the self-assembling peptide may be affected. Other amino acids that form hydrogen bonds (such as asparagine and glutamine) can be incorporated into the self-assembling peptide, instead of or in addition to charged residues. By changing alanine residues in the self-assembling peptide to more hydrophobic residues (such as leucine, isoleucine), the resulting self-assembling peptide has a greater tendency to self-assemble and forms a self-assembling peptide matrix with enhanced strength. Some self-assembling peptides with amino acid compositions and lengths similar to those of the self-assembling peptides described herein also form other structures. Therefore, in addition to structural compatibility, other factors can also determine the formation of the macroscopic matrix, such as self-assembling peptide length, the degree of intermolecular interaction, and the ability to form staggered arrays, etc. The peptide can self-assemble in an unmodified state, where the N-terminus of the peptide exists as the amine (-NH 2 ) of the terminal residue, and the C-terminus of the peptide exists as the carboxylic acid (-COOH) of the opposite terminal residue. However, when one or both termini are modified, the peptide may self-assemble. The charge of the N-terminus, C-terminus, or both can also be modified. In Table 1, R 1 is represented as the N-terminus, and R 2 is represented as the C-terminus. There are traditionally considered N-terminal modifications (R 1) modifications, while others are typically C-terminal modifications (R 2 ), and in some cases, the modification can occur at either terminus (R 1 = R 2 ). Typical N-terminal modifications (R 1 ) include but are not limited to 5-carboxyfluorescein (5-FAM), 5-carboxyfluorescein aminocaproic acid (5-FAM-Ahx), aminobenzoic acid (ABz), acetyl, acryloyl, benzoyl, biotin, biotin aminocaproic acid (biotin-Ahx), tert-butoxycarbonyl (BOC), bromoacetyl (Br-Ac-), bovine serum albumin (BSA; N-terminal NH 2 ), carboxybenzyl (CBZ), 5-(dimethylamino)naphthalene-1-sulfonyl (dansyl), 5-(dimethylamino)naphthalene-1-sulfonyl aminocaproic acid (dansyl-Ahx), capric acid, diethylenetriaminepentaacetic acid (DTPA), fatty acid, fluorescein isothiocyanate (FITC), fluorescein isothiocyanate aminocaproic acid (FITC-Ahx), fluorenylmethoxycarbonyl (Fmoc), formylation, hexanoic acid, hydrazinonicotinic acid (HYNIC), keyhole limpet hemocyanin (KLH; N-terminal NH 2 ), lauric acid, lipoic acid, maleimide, 7-methoxycoumarin-4-acetic acid (MCA), myristoyl, octanoic acid, palmitoyl, polyethylene glycol (PEG), stearic acid, and succinylation. Traditionally, C-terminal (R 2)Modified including but not limited to 7-amino-4-(trifluoromethyl)-2-benzopyranone (AFC), 7-amino-4-methylcoumarinyl (AMC), amidation, bovine serum albumin (BSA; C-terminal -COOH), benzyl (Bzl), cysteamide, ester (OEt), ester (OMe), ester (OtBu), ester (OTBzI), keyhole limpet hemocyanin (KLH; C-terminal -COOH), multiple antigen peptides (MAPs asymmetric 2-branched, MAPS asymmetric 4-branched, MAPS asymmetric 8-branched), methyl (Me), N-ethylamide (NHEt), N-isopentylamide (NHisopen), N-methyl (NHMe), N-hydroxysuccinimide ester (OSU), ovalbumin (OVA; C-terminal -COOH), p-nitroaniline (pNA), and tert-butyl (tBu). Additionally, the peptide may include at least one terminal amino acid that has been modified by a non-amino acid organic functional group. Exemplary non-amino acid organic functional groups include but are not limited to alkyl, acyl, carbohydrate, polyether, phosphate ester, and fatty acid. In other compositions where the non-amino acid functional group is a phosphate ester, the phosphate ester is optionally farnesyl pyrophosphate, geranyl pyrophosphate, or 3-isopentenyl pyrophosphate. For example, R 1 can be a group or radical such as acyl (R 1 CO-, where R 1 is an organic group such as acetyl (CH 3 CO-)) can be present at the N-terminus of the self-assembling peptide to neutralize a possible additional "extra" positive charge, such as a charge not generated by the side chain of the N-terminal amino acid. Similarly, a group such as an amide (CO-NH 2 ) in the form of an amine (NH 2 ) can be used to neutralize a possible additional "extra" negative charge present at the C-terminus, such as a charge not generated by the side chain of the C-terminal amino acid. Neutralization of the charge at the terminus can promote the formation of a matrix through self-assembly. The N-terminus may include an aliphatic group, including a palmitoyl chain of a fatty acid having C 1-100 , preferably C 10-20 , and more preferably C 1-16 . The N-terminus may include a palmitoyl chain (i.e., C 16)). The derivatives of the peptides described herein are considered to be included in this disclosure. The derivatives further include, but are not limited to, acyl derivatives, which have one or more straight-chain or branched-chain, long or short, saturated or unsaturated, substituted or unsubstituted by hydroxyl, amino, aminoacyl, sulfate or sulfide groups, having 1-30 carbon atoms. N-acyl derivatives include those acyl groups that can be derived from: acetic acid, capric acid, lauric acid, myristic acid, caprylic acid, palmitic acid, stearic acid, behenic acid, linoleic acid, linolenic acid, lipoic acid, oleic acid, isostearic acid, elaidic acid, 2-ethylhexanoic acid, coconut fatty acids, tallow fatty acids, hardened tallow fatty acids, palm kernel oil fatty acids, lanolin fatty acids, etc. Preferred examples of acyl groups include acetyl, palmitoyl, elaidoyl, myristyl, biotinyl and octanoyl. These can be substituted or unsubstituted. Preferred embodiments include N-palmitoyl, as shown in SEQ.ID.NO.:3, SEQ.ID.NO.:8 (a variant of SEQ.ID.NO.:1, which has a palmitoyl (pal group) (also shown in Table 2)) and as shown in SEQ.ID.NO.#3 of the peptide having the sequence GH and its derivatives. The number of amino acids in the self-assembling peptide can vary. The self-assembling peptide can contain from about 1 amino acid to about 200 amino acids, from about 1 to about 36 amino acids, or from about 1 to about 16 amino acids or between 1 and about 6 amino acids, including all ranges and subranges therein. In addition, the amino acids can be analogs, D-forms or amino acids modified or derived by adding chemical groups, the chemical groups including but not limited to acyl, alkyl, phosphate, farnesyl, geranylgeranyl, palmitoyl or fatty acids, etc. In addition, the amino acids of the self-assembling peptide can be naturally occurring amino acids or non-naturally occurring amino acids. All 20 naturally occurring amino acids can be used in this disclosure according to the present invention. In order to enhance bioavailability, the properties of those peptides to cross the epithelial barrier can be improved by increasing their lipophilicity or lipophilic characteristics, the increase being achieved by acylation of the N-terminal NH 2 group of the peptide or by esterification of the carboxyl group with an alcohol, the alcohol being straight-chain or branched-chain, saturated or unsaturated, hydroxylated or unhydroxylated, or both. In some embodiments, the N-acyl groups used to modify the peptide backbone include but are not limited to lauroyl (C 12 ), myristoyl (C 14 ), palmitoyl (C 16 ), stearoyl (C 18 ), oleoyl (C 18:1 ), arachidoyl (C 20) or linoleyl (C 18:2)。 Biotin groups (biotin or derivatives) are also expected. The N-terminal group can be H or palmitoyl. By incorporating protease or peptidase cleavage sites into the precursor that subsequently forms a given structure and by varying the number or type of amino acids, the ease or efficiency of penetration can also be regulated. Proteases or peptidases that are naturally present in the body can be introduced. Any combination of the modifications described herein is within the scope of the present invention. For example, self-assembling peptides that include protease cleavage sites and cysteamine residues and / or crosslinking agents, kits and devices containing them, and methods of using them are contemplated and are considered to be within the scope of this disclosure. Exemplary one or more peptide sequences Classes of self-assembling peptides each having characteristics that define the primary sequence of a molecule are included in this disclosure and are described hereinafter. Peptides of these classes include, but are not limited to, dipeptides, surfactant-like peptides, peptide amphiphiles with alkyl groups, bolaamphiphilic peptides, ion-complementary self-assembling peptides, and cyclic peptides, and the properties that distinguish each class of self-assembling peptides are described herein. 1. Dipeptides: Dipeptides are self-assembling peptides. They contain two amino acids, which can be modified or unmodified. Dipeptides typically include aromatic residues, such as phenylalanine, where π-π interactions and hydrophobic effects strongly influence self-assembly. 2. Surfactant-like peptides and peptide amphiphiles: Surfactant-like peptides contain amino acids with charged polar amino acids as the head and a repeating sequence of hydrophobic amino acids as the hydrophobic tail. SEQ.ID.NO.:7 is an example of a surfactant-like peptide. The polar head contains a lysine residue, while the hydrophobic tail contains six consecutive repeating alanine residues. On the other hand, peptide amphiphiles with alkyl groups include two main characteristics. First, an alkyl tail attached to the N-terminal or C-terminal and a hydrophilic portion of the amino acids. Second, the sequence can include glycine residues to impart flexibility. The alkyl drives hydrophobic interactions, while the polar charged groups preferably interact with the aqueous environment, similar to protein folding. Non-limiting examples of peptide amphiphiles are No. #3 (in Table 1) and SEQ.ID.NO.:3. For example, No. #3 (also shown in Table 2) is Pal-GH, where the polar head contains glycine and histidine residues. Histidine is positively charged, while the hydrophobic tail contains a palmitoyl chain conjugated to a glycine residue. In SEQ.ID.NO.:3, which is Pal-KTTKS, the polar head contains several residues, namely KTTKS. Serine and threonine residues are neutral residues, while lysine is the positively charged head, and the hydrophobic tail contains a palmitoyl chain. 3. Bolaamphiphilic peptides: Bolaamphiphilic peptides contain two hydrophilic heads connected by a hydrophobic residue region. Asymmetric bolaamphiphiles include different hydrophilic heads at either end of the hydrophobic region. 4. Ion-complementary self-assembling peptides: Ion-complementary self-assembling peptides are recognized by hydrophobic tails to participate in hydrophobic effects. The hydrophilic tail contains charged amino acids to form ionic bonds, and the pattern of ionic charges is classified into four subtypes.Subtypes of ionic charges are represented as: type I is “+-+-+-”, type II is “++--++--”, type III is “+++---+++”, and type IV is “+++----”. Non-limiting examples include SEQ.ID.NO.:4, RADA-16, SEQ.ID.NO.:5, IEIK-13, SEQ.ID.NO.:6, and KLD-12, all of which are examples of type I ion-complementary self-assembling peptides. 5. Cyclic peptides: Cyclic peptides can have an even number of D and L amino acids that stack via hydrogen bonds, or they can be more amphiphilic and aggregate via the hydrophobic effect. Each non-limiting example herein describes the self-assembling properties of self-assembling peptides. The peptides described herein are non-limiting and can have self-assembling properties even if they do not fall within one or more of the peptide categories described herein. Such examples include SEQ.ID.NO.:1 and its variants and derivatives, SEQ.ID.NO.:2, and SEQ.ID.NO.:8; however, SEQ.ID.NO.:1-2 are known to self-assemble due to their elastin-like peptide (ELP) sequences. Other exemplary peptides include peptides derived from collagen, variants and derivatives of elastin, collagen, or self-assembling peptides; peptides obtained from natural protein systems (such as fibronectin), etc. The applicant demonstrates that the self-assembly of such peptides can be controlled or modified, i.e., preventing assembly in the formulation while enabling self-assembly through a selected trigger within the skin layer. It is noteworthy that the present disclosure also includes peptide sequences that generally do not fall within the self-assembly principle or peptide categories but have properties that assist self-assembly and are capable of self-assembling in vivo (i.e., SEQ.ID.NO.8). The applicant demonstrates the prevention of peptide assembly in the formulation while regulating and achieving self-assembly through in vivo triggers within the skin layer, without methods and compositions of cell or tissue biogenesis. In addition, self-assembling materials can include, but are not limited to, peptides, proteins, peptoids, lipids, polysaccharides, polynucleotides, aptamers, ligand / receptor pairs, and combinations of any of these. In addition, the selection of oligomers of peptides includes structures defined by specific substitutions or sequences that drive the specificity of the network, such properties as trigger assembly, delivery and targeting tissues by local application, the speed, size, or shape of the network, interaction with skin functional pathways, etc. B. Regardless of the exact form and overall composition of the self-assembled structure in the formulation (e.g., not limited to whether in combination with another reagent, within a device, or packaged in a kit, or in combination with another composition or form, etc.), the compositions described herein include self-assembling peptides. In particular, the compositions include peptides that are capable of self-assembling upon triggering, and more particularly, the compositions include peptides SEQ.ID.NO.: 1-8 and serial numbers #1-9, either alone or as a mixture. The composition or mixture can include the same peptide sequence of different lengths or a mixture thereof or different peptides. For example, the self-assembled structures disclosed herein can be formed from individual peptides or a heterogeneous mixture of peptides (i.e., a mixture containing more than one type of peptide conforming to a given chemical formula or conforming to two or more chemical formulas). The object of the present application is to substantially prevent self-assembly in the composition before topical application or in vitro when the peptides are present in the formulation. One or more peptides or a mixture thereof will self-assemble in vivo (i.e., the peptides in the mixture are complementary to each other and structurally compatible) within the skin (i.e., within the epidermal or dermal layer of the skin) upon application of the triggered composition, the triggering being provided by a triggered treatment or condition. According to the present disclosure, before the peptides are applied or treated, the effects of pH, temperature, hydrophobicity, hydrophilicity, or ionic strength of specific peptides in the composition must be strictly managed to achieve a sol-gel transition. In certain formulations, sugars (e.g., not limited to sucrose, fructose, etc.) can also affect the sol-gel transition parameters of the self-assembling material. When achieving the sol-gel transition parameters, self-assembly in the composition is substantially prevented before treatment while maintaining the critical gel concentration in the composition. For example, the formulation can be free of ions, such as monovalent or divalent ions, or include very small amounts of ions, monovalent or divalent ions in the range of about 5 M to 0.001 M, including about 2, 0.1, 0.01, 0.001 M, such that self-assembly of the peptides on the external skin is substantially prevented. In the composition, the ions can be salts of monovalent or divalent cations, the cations including but not limited to Na + 、K + 、Zn 2+ 、Ca 2+ 、Mg 2+ 、Mn 2+ 、Fe 2+ 、Cu 2+etc. In the composition, the pH is between about 3 - 9, preferably between about 3 - 7. In some compositions, the amount of the peptide is in the range of about 0.001% - 30% of the total weight of the composition, preferably about 0.1% - 10% (w / w) of the total weight of the composition, and the temperature is in the range of about 19°C to 42°C. C. Compositions containing self - assembling molecules form macromolecular structures within the skin layer. As described above, self - assembly of the peptide is substantially prevented on the external skin or in the formulation. However, after delivery of the peptide, self - assembly occurs within the skin layer. For example, Pal - VGVAPG self - assembles into elongated fibers within the skin layer under appropriate triggers in the skin layer (such as pH trigger at 7, temperature trigger at 37°C, and concentration trigger of ≥0.01% w / w). On the other hand, although Pal - KTTKS can self - assemble in vitro (substantially preventing such assembly), it is triggered by a pH of 5 within the skin layer at a concentration as low as 0.5% w / w and a temperature of 37°C. However, increasing the temperature in a gradient from about 10°C to 20°C from the composition to the skin layer and from the skin surface to the skin layer facilitates the kinetics of self - assembly within the skin layer, thus providing a gradient for triggering to occur within this temperature range. This results in an observable effect on the overall mechanical properties of the skin. Self - assembly can be initiated or enhanced by triggers at any subsequent time after topical application. Triggers can include ionic solutes or diluents of the peptide composition or gradient conditions within the skin or changes in pH value, temperature, etc. Alternatively, adding salts (such as ZnCl with a concentration between about 0.1 mM - 5 M) 2) will induce assembly within a short period of time (e.g., within a few minutes). Lower concentrations of salts can also induce assembly at a slower rate. In some compositions, self-assembly begins when the composition is exposed within the skin layer, and self-assembly can be promoted by topically applying another composition to the area where the composition has already been deposited. Based on the research to date, self-assembly also occurs rapidly upon contact with internal body tissues. For example, when a formulation containing elastin-like peptides is topically administered to the skin, co-assembly of the elastin-like peptides onto pre-existing fibers occurs. The subjects described herein are humans. The time required for effective assembly can be 60 seconds or less after contact with the internal tissues of the subject and the gradient conditions within the skin layer. The conditions or parameter values of such triggers or conditions within the skin that achieve such assembly can vary, e.g., conditions found within the skin layer or in the body (e.g., within 50, 40, 30, 20, or 10 seconds or less). In some cases, when the concentration of the self-assembling agent in the composition is low or when the movement of body substances is significant, self-assembly may take longer to achieve the desired effect, e.g., up to 1 minute, 5 minutes, 10 minutes, 30 minutes, 1 hour, 2 hours, or 3 hours or longer. For example, when a composition containing self-assembling peptides is applied to the skin and subsequently delivered to the layers within the skin, it can assemble and form a physically functional macrostructure within as little as 10 seconds after application or as long as 120 minutes after application. The individual components or ingredients in the composition that form new patterns or self-assembled structures may require additional components or biomolecules available within the skin. Non-limiting examples are elastin molecules present in the skin layer, which assist in further assembly within the skin. This disclosure identifies and defines the in vivo assembly of such molecules as co-assembly, and the initial structure is referred to as a "seed structure". For example, after delivery of the peptide within the skin, it can recognize another molecule or structure within the skin, such as but not limited to elastin, collagen, fibronectin, hyaluronic acid, lipid bilayer, etc., and can co-assemble with such molecules, resulting in aggregation and spontaneous assembly, thereby leading to an overall physical structure and the resulting cosmetic effect or benefit. In some cases, such assembly does not require a selected trigger, and the existing seed structure itself serves to promote assembly within the skin layer. In specific cases, oligomers of a single class of peptides or oligomers of a single type of peptide can self-assemble onto the seed structure. In other cases, oligomers of two or more different classes or types of peptides can assemble with each other and aggregate onto the seed structure within the skin layer or in the tissue. In still other cases, oligomers of multiple classes of peptides or multiple types of oligomers can co-aggregate with the seed structure within the skin layer or with the tissue. Seed structures or molecules include but are not limited to elastin, collagen, and other extracellular molecules (ECM), etc. In other specific cases, oligomers of a single class of peptides or oligomers of a single type of peptide or oligomers of multiple classes of peptides can self-assemble with another oligomer within the skin layer.Such oligomers may not assemble or aggregate spontaneously with or by themselves, except when they encounter other suitable oligomers and start co-aggregating, and aggregate with one or more such oligomers within the skin layer or in the presence of certain in vivo conditions. In addition, such oligomers can be designed to assemble only in the presence of another suitable oligomer. Thus, self-assembly occurs when materials (such as molecules, polymers, colloids, microscopic or macroscopic particles) delivered within the skin in a specific formulation organize into ordered and functional structures or patterns due to specific local interactions of the components themselves with or without any other driving force. The materials assemble only when triggered within the skin layer (i.e., within the stratum corneum, epidermis, or dermis). Compositions can be administered such that materials including peptides are maintained in a formulation that substantially prevents assembly. However, after delivery of the materials, self-assembly or phase transition is triggered by components found within the subject's body (such as ions, seed structures, or biomolecules present in the skin layer), by physiological pH, temperature, etc., or upon triggering of the trigger.. D. Triggered self-assembly systems can employ specific triggers to initiate network formation. As used herein, the term "trigger" refers to conditions that promote or inhibit the self-assembly formation of specific polymers. In the present disclosure, various triggers can be utilized, including, for example: i. Utilizing "seed structures" in the skin to promote self-assembly. Such seed structures act as triggers and can include, for example but not limited to, elastin fibers, collagen, fibronectin, hyaluronic acid, or other existing molecules within the skin layer. ii. Physical triggers in the composition, such as but not limited to temperature, shear, salinity, concentration, pH, enzyme amount, light, or ion concentration, redox potential, hydrophobic / hydrophilic balance, temperature, light, enzyme concentration, and other parameters that affect network formation. iii. Changes in the values of the above physical triggers between non-physiological and physiological values, including but not limited to changes in the values of temperature, shear, salinity, concentration, pH, ion concentration, redox potential, hydrophobic / hydrophilic balance, light, enzyme concentration, and other parameters that affect network formation. Such changes are due to differences in the respective parameter values in the composition and in the body. iv. Gradient conditions present in the skin layer, including skin gradients of pH, salinity, ionic strength, enzyme concentration, etc. v. Conditions present in the composition, such as, for example, the pH, temperature, salinity, and concentration of peptides in the composition. vi. Any combination of the above triggers. In the methods and compositions, the trigger temperature of the composition is in the range of about 19°C to about 42°C. The pH trigger of the composition is in the range of pH 3 - 9. The ionic strength of the composition that can trigger self-assembly is from about 0.0001 M to about 5 M. The peptide concentration trigger in the composition is in the range of about 0.001% to about 30%. The change in temperature value between the composition and the skin layer can be in the range of about 1°C to about 30°C. The concentration change in the skin after application is in the range of about 0.001% to about 30% (w / w). The pH value change between the pH of the composition and the pH of the skin layer is in the range of about 0.0001 to about 5 pH units. The change in ionic strength value is in the range of about 0.001 M to about 5 M. Self-assembly can be initiated by an ionic strength gradient within the skin. For example, monovalent cations (such as Li + , Na + , K + and Cs +)The concentration of such ions required to induce or enhance self-assembly is typically in the range of about 1 mM to about 5 M. Lower concentrations promote assembly, albeit at a reduced rate, where higher concentrations can enhance self-assembly. The pH within the skin triggers in the range of about 4 - 9. The temperature trigger within the skin is about 35°C to about 42°C. The peptide concentration trigger within the skin layer is about 0.001% to about 30% (w / w). The ionic strength trigger within the skin layer is about 0 M to about 5 M. Similarly, the pH gradient available in various skin layers is a pH of 3 - 7, while the temperature gradient is about 19°C to about 42°C. All ranges and sub-ranges are included herein. Self-assembly can be triggered by the salt concentration of the composition such that when there is a salt concentration gradient, the peptide begins to assemble within the skin layer. In some other cases, when there is a change in the salinity value between the composition and the skin layer, the peptide begins to aggregate and assemble within the skin. Self-assembly can also be triggered by a combination of the various triggers described in i - v above. SEQ.ID.NO.:1 and its variants and derivatives self-assemble upon triggering, for example, including but not limited to gradients of pH, temperature, concentration, and ionic strength. The change in the pH value for self-assembly can be between about 1 and about 5. The change in the temperature value for self-assembly includes about 1°C to about 30°C, including 1°C, 2°C, 3°C, 4°C, 5°C, 8°C, 10°C, and 20°C. All ranges and sub-ranges are considered within the scope of this disclosure. Concentrations include all ranges and sub-ranges. The temperature change is the difference between the ambient temperature in the formulation (i.e., about 19°C to about 25°C) before application of the cosmetic composition and the temperature within the skin layer or body temperature of about 35°C to about 42°C. For example, SEQ.ID.NO.:1 and its variants with palmitoyl, when topically administered in the formulation and delivered within the skin layer, assemble into elongated fibers of elastin when appropriately triggered under the right conditions. Such in-skin assembly provides physical or mechanical changes to the skin and also provides structural changes to the skin. The changes can be spontaneous and can be apparent after topical administration of the formulation. In-vivo changes can occur within at least about 30 seconds to at least about 120 minutes after administration of the formulation. The physical or mechanical changes can last about 15 minutes to about 12 hours, or in some cases, one or two days. Physical and mechanical changes that occur during molecular self-assembly or co-assembly include but are not limited to lifting of the skin, enhanced presence of elastin, plumpness of the skin such that the effects can be observed. These effects may be caused by the hydrophobic tendency and hydrogen bonding between molecules within the skin, such that under specific conditions, it is favorable for self-assembly. Specifically, in the presence of appropriate triggering (such as changes in the salinity, concentration, pH, and temperature values within the skin layer compared to the composition), palmitoyl hexapeptide forms small fibers that produce observable effects on the skin. Under appropriate conditions, when topically administered and delivered within the skin, in the presence of triggering, the peptide co-assembles onto the endogenous elastin present in the skin memory.In the case of palmitoyl hexapeptide, gradients including but not limited to temperature, pH, and salt concentration are triggered. For example, a change in the self-assembly temperature value from about 1 °C to about 30 °C alters the self-assembly of the peptide within the skin. In some other cases, a pH range change of about 0.001 - 5 pH units can be utilized, and an ionic strength gradient of about 0 - about 5 M ZnCl₂ can be utilized. 2 When topically administered in a suitable formulation, SEQ.ID.NO.:2 presents an overall mechanical effect on the skin, and when delivered within the skin, the peptide self-assembles within the skin. Due to the geometry of SEQ.ID.NO.:3 and the head-to-tail ratio of the peptide, it is very likely that the curvature is not conducive to the formation of long fibers. Therefore, adding fatty acids can potentially trigger an increase in fiber length by inserting itself into the fiber structure and altering its geometry to form longer fibers. Then, such co-mixed fibers reach a critical length after the entanglement points and then have a positive impact on the viscoelastic properties. E. Selection of Self-Assembling Oligomers To confer effective skin care benefits, it is important to select self-assembling polymers suitable for delivery. Polymers capable of self-assembling can be selected based on a variety of factors. Such self-assembling polymers can include but are not limited to the peptides described herein. Other polymers include but are not limited to proteins, peptoids, lipids, polysaccharides, polynucleotides, aptamers, ligand / receptor pairs, and combinations thereof. Criteria for selecting oligomers can include selecting structures defined or modified by specific substitutions or sequences that drive the specific properties of the network, such as triggering assembly, delivery, and targeting tissues, speed, size or shape of the network, interaction with skin functional pathways, etc. Preferred oligomers can be optimized considering computer-aided modeling and design and testing on skin models. Cosmetic Compositions The present disclosure provides cosmetic compositions comprising self-assembling materials, including peptides. The self-assembling materials and cosmetic compositions comprising such materials are topically administered onto human skin and thereby delivered within the skin layers, forming macroscopic structures within the skin and providing physical and visible cosmetic benefits on the skin. The compositions improve the mechanical and physical properties of the skin without biogenesis of cells or tissues. The compositions can be administered in a suitable amount, weight, or concentration effective to provide cosmetic benefits. The compositions can be formulated in various forms and amounts to facilitate administration and achieve the desired effects. Various product forms and formulation types are contemplated in the present invention, including gels, films, powders, sprays, thin films, liquids, creams, foams, emulsions, masks, aqueous washes, aqueous creams. These forms are also relevant to cosmetic and dermatological applications such as masks, patches, applicators. Formulation parameters for achieving macroscopic structure assembly formation within the skin include pH, salt, and peptide concentration, among others. After administration to the skin, self-assembly of the oligopeptides or its lack may occur due to changes or gradients in pH, temperature, peptide concentration, or salt concentration triggered by the administered formulation. More specifically, within the epidermal layer of the skin, the pH (a value of about 5.5) can alter the formulation pH, allowing oligopeptide self-assembly. Other triggering mechanisms can include changes or gradients in pH, salt concentration, and oligopeptide concentration or by evaporation of the vehicle. The self-assembling peptides can be delivered together with hydrophobic materials (e.g., cosmetically acceptable oils, oil-in-water or emulsions). The self-assembling peptides can be mixed with hydrophobic agents such as oils or lipids or can be present in the form of emulsions or oil-in-water. According to the present invention, the formulation and packaging must be designed to substantially prevent premature self-assembly from occurring in the composition and prior to administration or handling. In addition, the formulation must assist in driving specific triggers, including: triggers provided by a personal care procedure / program, including a. changes in shear, evaporation, temperature, dilution or concentration, mixing of multiple phases, and / or mixing of multiple complementary oligomers during use; and b. changes in physical parameters (either within the formulation / packaging itself or driven by differences between the skin and the formulation), such as pH, ionic strength, hydrophobic / hydrophilic balance, temperature, and other parameters affecting network formation. In addition, the formulation must be designed to deliver or facilitate penetration of the self-assembling oligomers into the correct layers within the skin or scalp or onto the skin or scalp. The CTFA Cosmetic Ingredient Handbook, 10th Edition (published by the Cosmetic, Toiletry, and Fragrance Association, Inc., Washington, D.C.) (2004) (hereinafter referred to as "CTFA") describes various non-limiting materials that can be added to the compositions herein.Examples of these ingredient categories include, but are not limited to: abrasives, absorbents, aesthetic components such as fragrances, pigments, coloring agents / colorants, essential oils, skin sensates, astringents such as cosmetic and pharmaceutical astringents (e.g., clove oil, menthol, camphor, eucalyptus oil, eugenol, menthyl lactate, witch hazel distillate), anti-acne agents, anti-caking agents, anti-foaming agents, anti-microbial agents (e.g., iodopropyl butylcarbamate), antibacterial agents, anti-fungal agents, antioxidants, binders, biological additives, buffers, fillers, chelating agents, chemical additives, colorants, cosmetic biocides, denaturants, topical analgesics, film-forming agents or materials, such as polymers for assisting the film-forming properties and directness of the composition (e.g., copolymer of eicosenylene and vinylpyrrolidone), opacifiers, pH regulators, plant derivatives, plant extracts, plant tissue extracts, plant seed extracts, vegetable oils, preservatives, propellants, reducing agents, sebum control agents, and polyvalent chelating agents. The concentration of the self-assembling peptide can vary from about 0.001% w / v (0.001 mg / mL) to about 99.99% w / v (999.9 mg / mL), including the end values. For example, the concentration in the formulation can be between about 0.001% (0.1 mg / mL) - 30% (3000 mg / mL), including the end values (e.g., about 0.01% - 5%; 0.5% - 5%; 1.0%; 1.5%; 2.0%; 2.5%; 3.0%; 4.0%; 10%; 20% or higher). In some embodiments, the concentration can also be less than 0.001%. The concentration of the self-assembling material (such as a peptide) can vary in any given formulation and can be between about 0.001 wt% - 30 wt% of the total weight of the composition, including the end values, preferably between 0.001 wt% - 30 wt%. The concentration of the self-assembling material (e.g., in liquid, serum, cream, gel formulations) can be about 0.001 - 30.0% (0.1 - 300 mg / mL) (e.g., 0.01 - 10% of the total weight of the composition; 1.0 - 20.0%; 2.0 - 30.0% or 0.5 - 30.0%, including all ranges and sub-ranges). The concentration of the self-assembling material can be higher in the stock solution and solid (e.g., powder) formulations. The solid formulation can have a self-assembling material concentration close to 100 wt% (e.g., the concentration of the self-assembling material can be 95, 96, 97, 98, 99 wt% or more of the composition weight (e.g., 99.99 wt%)). Whether in liquid or solid form, the material (such as a peptide) can be brought to the desired concentration by adding an acceptable diluent (e.g., water), filler, or oil. The formulation can include an acceptable carrier or other reagents. For example, in a composition comprising at least one of SEQ.ID.NO.: 1 - 8 of Serial Nos. #1 - 9, the amount of the self-assembling peptide can be an amount within the range of about 0.001% to about 30% (w / w) of the total weight of the composition.In certain compositions, the amount of the self-assembling peptide is from about 0.001% to about 15% (w / w) of the total weight of the composition. In certain compositions, the amount of the self-assembling peptide is from about 0.5% to about 20% (w / w) of the total weight of the composition. In certain compositions, the amount of the self-assembling peptide is from about 0.5% to about 10% (w / w) of the total weight of the composition. All ranges and sub-ranges are considered to be included herein. The compositions disclosed herein may further comprise biomolecules, including but not limited to proteins, peptides, or bioorganic molecules other than peptides. The biomolecules may be mixed with the self-assembling materials disclosed herein. Such biomolecules may be provided as separate solutions and may be administered before or after the topical administration of the composition. The composition may also comprise additional unmodified peptides that are structurally complementary and compatible and allow for an increase in the cosmetic benefits on the skin. Such additional peptides in the composition and the peptides disclosed herein are present in a ratio of about 1:1, 1:10, 1:100, 10:1, 5:1, 9:1, or 99:1 or sub-ranges therein. The composition is substantially free of gelling agents. This enables self-assembly to occur in vivo to form macroscopic structures (i.e., within the skin layer upon contact with tissue). Other optional components that may be incorporated into the compositions described herein include but are not limited to one or more cosmetic skin care agents. A cosmetic skin care agent is any substance, material, or compound intended to be applied to the skin for improving an undesirable skin condition (or its symptoms). Some undesirable skin conditions include externally visible and tactilely perceptible manifestations due to skin aging and any other macroscopic or microscopic effects. Such signs may be induced or caused by intrinsic or extrinsic factors, e.g., chronological aging and / or environmental damage. These signs may be caused by processes including but not limited to the development of texture discontinuities such as wrinkles (including fine surface wrinkles and coarse deep wrinkles), folds, skin lines, cracks, lumps, large pores (e.g., associated with accessory structures such as sweat gland ducts, sebaceous glands, or hair follicles), scaly, flaky, and / or other forms of skin non-uniformity or roughness, loss of skin elasticity (loss and / or inactivation of functional cutaneous elastin), sagging (including edema in the eye area and lower cheeks), loss of skin firmness, loss of skin tightness, loss of skin recoil due to deformation, discoloration (including under-eye circles), spots, sallowness, hyperpigmented skin areas such as age spots and freckles, keratosis, abnormal differentiation, hyperkeratinization, elastotic degeneration, collagenolysis, and other histological changes in the stratum corneum, dermis, epidermis, cutaneous vascular system (e.g., telangiectasia or spider veins), and underlying tissues (especially those close to the skin).The processing solutions / procedures required to form self-assembled networks must provide control over several possible parameters, including the proximity of interacting oligomers, the concentration of oligomers, the shear forces in use, the layering of interacting phases, the enhanced penetration of oligomers, targeting the network to specific locations on or in the skin, and triggering through changes in physical parameters. The composition can contain a dermatologically, cosmetically acceptable carrier or excipient. Thus, the carrier can act as a diluent, dispersant, solvent, etc. for peptides and other materials, compounds, and / or agents. Exemplary acceptable excipients include any and all solvents, dispersion media, diluents, or other liquid vehicles, dispersion or suspension aids, surfactants, isotonic agents, thickening or emulsifying agents, preservatives, solid binders, lubricants suitable for topical administration and dosage. Except to the extent that any conventional carrier medium is incompatible with the substances or their derivatives, e.g., by producing any undesired biological effects or interacting in a detrimental manner with any one or more other components of the composition, its use is contemplated within the scope of the present invention. The carrier can contain one or more acceptable solid, semi-solid, or liquid fillers, diluents, solvents, bulking agents, etc. The carrier can be solid, semi-solid, or liquid. The carrier itself can be inert, or it can have its own dermatological or cosmeceutical benefits. The concentration of the carrier can vary depending on the selected carrier and the desired concentrations of the essential and optional components. In the composition, the carrier is present at a level of about 50% to about 99.99% (e.g., about 60% to about 99.9%, or about 70% to about 98%, or about 80% to about 95%) by weight of the composition. Acceptable carriers can be provided in a variety of forms. Non-limiting examples include but are not limited to simple solutions (water-based or oil-based), emulsions, and solid or semi-solid forms (gels, sticks). For example, emulsion carriers can include but are not limited to water-in-oil, oil-in-water, silicone-in-water, water-in-oil-in-water, and silicone-in-water-in-oil emulsions. As understood by those skilled in the art, a given component will be predominantly distributed into the aqueous or oily phase, depending on the water solubility / dispersibility of the component in the composition. In some embodiments, the personal care compositions described herein are formulated as water-in-oil emulsions. Suitable carriers also include oils. The composition can contain about 1% to about 95% by weight of one or more oils. The composition can contain about 0.1%, 0.5%, 1%, 2%, 5%, 10%, 15%, 20%, 25%, 30%, 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, or 90% to about 90%, 85%, 80%, 75%, 70%, 65%, 60%, 55%, 50%, 45%, 40%, 35%, 30%, 25%, 20%, 15%, 10%, 5%, or 3% of one or more oils. Oils can be used to dissolve, disperse, or carry materials that are not suitable for water or water-soluble solvents. Suitable oils include silicones, hydrocarbons, esters, amides, ethers, and mixtures thereof.The oil can be a fluid at room temperature. The oil can be volatile or non-volatile. "Non-volatile" refers to a material that exhibits a vapor pressure of no more than about 0.2 mm Hg at 25°C under one atmosphere and / or a material that has a boiling point of at least about 300°C under one atmosphere. "Volatile" refers to a material that exhibits a vapor pressure of at least about 0.2 mm Hg at 20°C. When a heavy, greasy film is not desired, a volatile oil can be used to provide a lighter feel. When the skin care composition is in the form of an emulsion, the oil is the carrier that is typically associated with the oil phase. The composition can include an emulsifier. An emulsifier is particularly suitable when the composition is in the form of an emulsion or if immiscible materials are incorporated. The skin care composition can include from about 0.05%, 0.1%, 0.2%, 0.3%, 0.5% or 1% to about 20%, 10%, 5%, 3%, 2% or 1% of an emulsifier. The emulsifier can be nonionic, anionic or cationic. The compositions described herein can be in the form of a pourable liquid (under ambient conditions). Thus, the composition can include an aqueous carrier, which is typically present at a level of from about 20% to about 95% (or from about 60% to about 85%) based on the weight of the composition. The aqueous carrier can include water, or a miscible mixture of water and an organic solvent, but preferably includes water with a minimal or no significant concentration of an organic solvent, unless otherwise incorporated incidentally as a minor component of other necessary or optional components into the composition. The compositions of the present invention further include a carrier, which is present at a level of from about 20% to about 99.99%, from about 30% to about 90%, from about 40% to about 80% of the weight of the composition. The carrier can be in various forms. Non-limiting examples include simple solutions (e.g., aqueous, organic solvent or oil-based), emulsions, suspensions and solid forms (e.g., gels, sticks, flowable solids or amorphous materials). In certain embodiments, the dermatologically acceptable carrier is in the form of an emulsion or a suspension. Emulsions or suspensions can generally be classified as having a continuous aqueous phase (e.g., water-in-oil and water-in-oil-in-water) or a continuous oil phase (e.g., oil-in-water and oil-in-water-in-oil). The oil phase of the present invention can include silicone oils, non-silicone oils such as hydrocarbon oils, esters, ethers, etc. and mixtures thereof. The emulsion can further include an emulsifier. The composition can include any suitable percentage of an emulsifier to adequately emulsify the carrier. Suitable weight ranges include from about 0.1% to about 10% or from about 0.2% to about 5% of an emulsifier based on the weight of the composition. The emulsifier can be nonionic, anionic or cationic. Suitable emulsifiers are disclosed, for example, in U.S. Patent No. 3,755,560, U.S. Patent No. 4,421,769 and McCutcheon's Detergents and Emulsifiers, North American Edition, pages 317 - 324 (1986). Suitable emulsions can have a wide range of viscosities, depending on the desired product form. The carrier can further include thickeners known in the art to provide a composition with suitable viscosity and rheological characteristics.The compositions of the present invention may further comprise at least one film-forming polymer. The film-forming polymer may be selected from cellulose polymers such as nitrocellulose, cellulose acetate, cellulose acetate / butyrate, cellulose acetate / proprionate, and ethyl cellulose; polyurethanes; acrylic polymers; vinyl polymers; polyvinyl butyral; alkyd resins; resins obtained from aldehyde condensation products such as aryl sulfonamide-formaldehyde resins such as toluene sulfonamide-formaldehyde resins, and aryl sulfonamide-epoxy resins. Other non-limiting examples of suitable film-forming polymers include nitrocellulose from Hercules; toluene sulfonamide-formaldehyde resin "Ketjentflex MS80" from Akzo; "Santolite MHP", "Santolite MS 80", and "Resimpol 80" from Pan Americana; alkyd resin "Beckosol ODE 230-70-E" from Dainippon; acrylic resin "Acryloid B66" from Rohm & Haas; and polyurethane resin "Trixene PR 4127" from Baxenden. The film-forming polymer may generally be present in the composition in an amount of from about 1% to about 50%, preferably from about 2% to about 40%, and most preferably from about 2% to about 35%. Transdermal Delivery Vehicles For self-assembly beneath the skin surface, the self-assembly materials of the present disclosure can optionally be delivered via a transdermal delivery vehicle. The transdermal delivery vehicle can include physical or chemical mechanisms designed to deliver materials beneath the skin surface. Such physical mechanisms can include, for example, known penetration-enhancing cosmetic compositions or ingredients, subcutaneous injection needles, micromanipulation needles, transdermal patches, electrospun nanofibers, etc. Other delivery systems can include, for example, the use of chemical enhancers, non-cavitating ultrasound, iontophoresis, and other energy devices. The compositions of the present disclosure can further include at least one film-forming polymer. The film-forming polymer can be selected from cellulose polymers such as nitrocellulose, cellulose acetate, cellulose acetate / butyrate, cellulose acetate / propionate, and ethyl cellulose; polyurethanes; acrylic polymers; vinyl polymers; polyvinyl butyral; alkyd resins; resins obtained from aldehyde condensation products such as arylsulfonamide-formaldehyde resins such as toluenesulfonamide-formaldehyde resins, and arylsulfonamide-epoxy resins. Other non-limiting examples of suitable film-forming polymers include nitrocellulose obtained from Hercules; toluenesulfonamide-formaldehyde resin "Ketjentflex MS80" obtained from Akzo; "Santolite MHP", "Santolite MS 80", and "Resimpol 80" obtained from Pan Americana; alkyd resin "Beckosol ODE 230-70-E" obtained from Dainippon; acrylic resin "Acryloid B66" obtained from Rohm & Haas; and polyurethane resin "Trixene PR 4127" obtained from Baxenden. The film-forming polymer can generally be present in the composition in an amount of about 1% to about 50%, preferably about 2% to about 40%, and most preferably about 2% to about 35%. Adhesives The compositions of the present invention can include from about 0.1% to about 10%, preferably from about 0.1% to about 2% of an adhesive. The type and amount of the adhesive are selected to provide, for example, more flexible and longer-lasting benefits to the composition, and / or better compatibility with other skin care or cosmetic formulations. Examples of suitable adhesives include polyurethanes, including Polyderm PE-PA available from Alzo International Inc.; copolymerized amidoester compounds, including Polyderm PPG-17 available from Alzo International Inc.; and acrylic latex dispersions. Skin Active Agents The compositions of the present invention can include skin active agents that provide specific skin care benefit characteristics when using a skin care product. Herein, skin care benefits can include benefits related to the appearance or beauty of the skin. Skin care active agents can provide acute (immediate and short-term) benefits or chronic (long-term and more persistent) benefits. Skin active agents that can be used herein include skin brighteners, anti-acne agents, emollients, non-steroidal anti-inflammatory agents, local anesthetics, artificial tanning agents, anti-microbial and anti-fungal active agents, skin soothers, sunscreens, skin barrier repair agents, anti-wrinkle agents, anti-skin atrophy active agents, lipids, sebum inhibitors, skin sensates, protease inhibitors, anti-itch agents, hair growth inhibitors, desquamase enhancers, anti-glycation agents, and mixtures thereof. When including a skin active agent, the composition of the present invention contains from about 0.001% to about 20%, preferably from about 0.1% to about 10% of at least one skin active agent. The type and amount of the skin active agent are selected such that the inclusion of the specific agent does not affect the stability of the composition. For example, a hydrophilic agent can be incorporated in an amount soluble in the aqueous phase, and a lipophilic agent can be incorporated in an amount soluble in the oil phase. Other skin active agents intended to exhibit the benefit of relaxing the expression lines for the present invention include, but are not limited to, Lavandox, available from Barnet Products Corporation; Thallasine 2, available from BiotechMarine; Argireline NP, available from Lipotec; Gatuline In-Tense and Gatuline Expression, available from Gattefosse; Myoxinol LS 9736, obtained from BASF Chemical Company, Syn-ake, available from DSM Nutritional Products, Inc.; and Instensyl®, available from Silab, Inc.; Sesaflash™, available from Seppic Inc. Skin brighteners that can be used herein refer to active ingredients that improve hyperpigmentation compared to pretreatment. Skin brighteners useful herein include ascorbic acid compounds, vitamin B3 compounds, azelaic acid, butylated hydroxyanisole, gallic acid and its derivatives, glycyrrhizic acid, hydroquinone, kojic acid, arbutin, mulberry extract, and mixtures thereof. It is believed that the use of combinations of skin brighteners is advantageous because they can provide skin brightening benefits through different mechanisms. Ascorbic acid compounds that can be used herein include L-ascorbic acid itself, ascorbates, and derivatives thereof. Ascorbates that can be used herein include sodium salts, potassium salts, lithium salts, calcium salts, magnesium salts, barium salts, ammonium salts, and protamine salts. Ascorbic acid derivatives that can be used herein include, for example, esters of ascorbic acid and ester salts of ascorbic acid.Particularly preferred ascorbic acid compounds include 2-O-D-glucopyranosyl-L-ascorbic acid, which is an ester of ascorbic acid and glucose and is commonly referred to as L-ascorbic acid 2-glucoside or ascorbyl glucoside, and its metal salts, and L-ascorbic acid phosphate salts such as sodium ascorbate phosphate, potassium ascorbate phosphate, magnesium ascorbate phosphate, and calcium ascorbate phosphate. Commercially available ascorbic acid compounds include magnesium ascorbate phosphate available from Showa Denko, 2-O-D-glucopyranosyl-L-ascorbic acid available from Hayashibara, and sodium ascorbate phosphate under the trade name STAY C available from Roche. Vitamin B3 compounds that can be used herein include, for example, those having the following formula: wherein R is -CONH 2 (such as nicotinamide) or -CH 2OH (such as nicotinol); its derivatives; and their salts. Exemplary derivatives of the aforementioned vitamin B3 compounds include nicotinic acid esters, including non-vasodilating esters of nicotinic acid, nicotinyl amino acids, nicotinol esters of carboxylic acids, nicotinic acid N-oxides, and nicotinamide N-oxides. Preferred vitamin B3 compounds are nicotinamide and tocopheryl nicotinate, and more preferably nicotinamide. In a preferred embodiment, the vitamin B3 compound contains a limited amount of the salt form, and more preferably is substantially free of the salt of the vitamin B3 compound. The preferred vitamin B3 compound contains less than about 50% of such salts, and more preferably is substantially free of the salt form. Commercially available vitamin B3 compounds highly useful herein include nicotinamide USP available from Reilly. Other hydrophobic skin brighteners that can be used herein include ascorbic acid derivatives, such as tetrahexyldecyl ascorbate (e.g., VC-IP, available from Nikko Chemical), ascorbyl palmitate (e.g., available from Roche Vitamins), ascorbyl dipalmitate (e.g., NIKKOL CP, available from Nikko Chemical); undecylenoyl phenylalanine (e.g., SEPIWHITE MSH, available from Seppic); octadecenedioic acid (e.g., ARLATONE DIOIC DCA, available from Uniquema); evening primrose seed extract, apple (pyrus malus) fruit extract, water, Myritol 318, butylene glycol, tocopherol, tetrahexyldecyl ascorbate, parabens, carbopol 980, and DNA / SMARTVECTOR UV, available from COLETICA; magnesium ascorbyl phosphate in hyaluronic acid filled spheres, available from COLETICA, and mixtures thereof.Other skin actives useful herein include those selected from N-acetyl-D-glucosamine, panthenol (e.g., DL-panthenol, available from Alps Pharmaceutical Inc.), tocopheryl nicotinate, benzoyl peroxide, 3-hydroxybenzoic acid, flavonoids (e.g., flavanones, chalcones), farnesol, phytantriol, glycolic acid, lactic acid, 4-hydroxybenzoic acid, acetylsalicylic acid, 2-hydroxybutyric acid, 2-hydroxypentanoic acid, 2-hydroxyhexanoic acid, cis-retinoic acid, trans-retinoic acid, retinol, retinyl esters (e.g., retinyl propionate), phytic acid, N-acetyl-L-cysteine, lipoic acid, tocopherol and its esters (e.g., tocopheryl acetate: DL-α-tocopheryl acetate, available from Eisai), azelaic acid, arachidonic acid, tetracycline, ibuprofen, naproxen, ketoprofen, hydrocortisone, acetaminophen, resorcinol, phenoxyethanol, phenoxypropanol, phenoxyisopropanol, 2,4,4'-trichloro-2'-hydroxydiphenylether, 3,4,4'-trichlorocarbanilide, octopirox, lidocaine hydrochloride, clotrimazole, miconazole, ketoconazole, neomycin sulfate, theophylline, and mixtures thereof. In a preferred example, the level of the skin active is from about 0.001% to about 20%, more preferably from about 0.1% to about 10%. Thickeners Thickeners are useful for the present invention. Thickeners can be used to solidify the solid oil-in-water form compositions of the present invention. When a thickener is used, the thickener is maintained at about 15% or less of the composition. Thickeners that can be used herein are selected from fatty compounds, gelling agents, inorganic thickeners, and mixtures thereof. The amount and type of thickener are selected according to the desired viscosity and properties of the product. These properties can include synergistic effects between the thickener and the film-forming component, thereby enhancing product / film adhesion, shrinkage, or flexibility while reducing whiteness. Thickeners that can be used in the present invention include, but are not limited to, crosslinked polyacrylates such as Carbopol™ (Goodrich); polyacrylate copolymers such as Sepimax Zen (Seppic, Inc.); modified acrylate copolymers such as Sepiplus S (Seppic, Inc.) polymer carboxylates, including modified and unmodified starches, polysaccharide gums such as xanthan gum (e.g., Keltrol CGT and Keltrol T630 from CP Kelco, Xanthan Gum from Jungbunzlauer), dehydrogenated xanthan gum (e.g., Amaze XT, from AkzoNobel), galactomannan (Solagum Tara, from Seppic), and cellulose derivatives (e.g., Natrosol 250). Gums can also include, but are not limited to, crosslinked xanthan gum, hydroxypropyl xanthan gum, undecylenoyl xanthan gum, deacetylated xanthan gum, guar gum, cellulose gum, carrageenan, hydroxypropyl methyl cellulose, and sodium carboxymethyl chitosan. Polymers that can be used herein include swellable, lightly to moderately crosslinked polyvinylpyrrolidone (PVP) such as ACP-1120 (International Specialty Products), acrylate copolymers / crosslinked polymers / blends such as acrylate / steareth-20 itaconate copolymer (Structure 2001, from AkzoNobel), acrylate / C10-30 alkyl acrylate copolymer (Amaze XT, from AkzoNobel), acrylic acid / VP crosslinked polymer (Ultrathix P100, from International Specialty Products). Fatty compounds that can be used herein include stearic acid, palmitic acid, stearyl alcohol, cetyl alcohol, behenyl alcohol, stearic acid, palmitic acid, polyethylene glycol ethers of stearyl alcohol or cetyl alcohol having an average of about 1 to about 5 ethylene oxide units, and mixtures thereof. Preferred fatty compounds are selected from stearyl alcohol, cetyl alcohol, behenyl alcohol, polyethylene glycol ether of stearyl alcohol having an average of about 2 ethylene oxide units (steareth-2), polyethylene glycol ether of cetyl alcohol having an average of about 2 ethylene oxide units, and mixtures thereof.Gelling agents that can be used as thickeners in the present invention include esters and amides of fatty acid gelling agents, hydroxy acids, hydroxy fatty acids, other amide gelling agents, and crystalline gelling agents. N-acyl amino acid amides that can be used herein are prepared from glutamic acid, lysine, glutamine, aspartic acid, and mixtures thereof. Other Optional Components The compositions herein can further contain additional components, such as those conventionally used in topical products, for example, those for providing aesthetic or functional benefits to the composition or the skin, such as sensory benefits related to appearance, odor, or feel, therapeutic benefits, or prophylactic benefits (it should be understood that the above-mentioned desired materials can themselves provide such benefits), optically active and color enhancing materials or ingredients, concealers, blurring agents, dyes, pearls, pigments, etc. These components can include, but are not limited to, materials intended to smooth, tighten, or lift sagging or wrinkled skin, including: Quicklift, available from BASF Chemical Company; Syntran PC5100, available from Interpolymer Corporation; Glycolift, available from Solabia USA Inc.; Alguard, available from Frutarom; Easyliance, obtained from Soliance; and Phytodermina Lifting code 9002, available from Istituto Ricerche Applicate. The CTFA Cosmetic Ingredient Handbook, 2nd Edition (1992) describes a wide variety of non-limiting cosmetic and pharmaceutical ingredients commonly used in the industry, which are applicable to the topical compositions of the present invention. Depending on the relative solubility of the components of the composition, such other materials can be dissolved or dispersed in the composition. Methods for various treatments, applications, conditioning or improvements can utilize the above-described compositions. Administration of the compositions of the present invention can occur on any skin surface of the body. Skin surfaces of greatest concern tend to be those that are not normally covered by clothing, such as facial skin surfaces, hand and arm skin surfaces, foot and leg skin surfaces, and neck and chest skin surfaces (e.g., décolletage). Specifically, administration can be on the facial skin surface, including the forehead, perioral, chin, periorbital, nasal and / or cheek skin surfaces. Improve the mechanical and physical properties of the skin without biogenesis using the compositions disclosed herein. This improvement in skin mechanical properties provides the visible cosmetic benefits and effects disclosed herein through the regimens and treatment methods provided herein. There are many regimens for administering the compositions to the skin. During the treatment period, the composition can be administered at least once a day, twice a day or on a more frequent daily basis. When administered twice a day, the first administration and the second administration are separated by at least 1 to about 12 hours. Typically, the composition can be administered in the morning and / or evening. The cosmetic composition can be administered as part of a treatment regimen that includes other products or formulations. Before or after administering the composition, a second administration of a different composition or different conditions (such as temperature), a penetration enhancer by means or component can be administered. Preferably, such an administration can be incorporated as a second, third, fourth or further treatment step. Such an administration can condition the skin prior to the treatment administration of the cosmetic composition. For example, the second or other administration step can change the pH, temperature, salinity of the skin or other conditions that prepare and induce self-assembly within the skin after or before the treatment. Any number of products or treatment steps can be included as part of the regimen in any necessary order. Examples of using a second composition or a different composition include changing the pH, ionic strength, temperature, adding or removing chemical or biochemical triggers, etc. prior to the treatment. Through the use of a regimen or several administrations of self-assembling materials, the treatment can allow the material to accumulate in the tissue to achieve a critical concentration and allow it to see its nearest neighbors, thereby generating 2D and / or 3D macromolecular structures and components. Such repeated use of the treatment methods and compositions described herein will provide accumulation of self-assembling materials and structures within the skin layers, thereby providing enhanced cosmetic benefits over time. The step of applying the composition to the skin can be carried out by topical application to the area containing the wrinkles. With respect to the administration of the composition, the terms "topical", "topically" or "topically" refer to delivering the composition to the destination area (e.g., the skin area containing the wrinkles) while minimizing delivery to skin surfaces or subcutaneous layers that do not require treatment. The composition can be applied and gently massaged into the skin. It is recognized that topical application allows a reasonable amount of the composition to be applied to the area adjacent to the wrinkles to be treated (i.e., it is not possible for the composition to be applied or retained within the boundaries of the wrinkles without some spreading). The form of the composition or dermatologically acceptable carrier should be selected to facilitate topical application.While certain embodiments of the present invention contemplate local application of the composition to the wrinkled area, it should be understood that the compositions of the present invention can be applied more generally or broadly to one or more facial skin surfaces to reduce the appearance of wrinkles within those facial skin areas. Similarly, the composition can be applied as a continuous film or in a pattern. Stripes, pattern dots, or random application of the composition may be desirable. Applicators as described below can be useful in illustrating patterned deposition. According to a particular method, the composition can be applied to a skin area in need of a desired lifting effect. For example, the composition can be applied to the hairline, temples, jawline, and other surrounding facial areas to apply a lifting effect to other facial areas. This method utilizes the lifting effect around the face to reduce, for example, wrinkles in the eye area, laugh lines around the mouth, under-eye wrinkles, and smooth the wrinkles around the cheek area. According to this method, the composition can be applied around the face without directly applying the composition to the target wrinkles. In another aspect, the present disclosure provides a method of improving mammalian skin, the method comprising administering an effective amount of the composition. In some embodiments, improving mammalian skin includes treating a mammalian keratinous tissue condition. Such treatment of a keratinous tissue condition can include topical application, including improving the cosmetic appearance of mammalian keratinous tissue. In some embodiments, the method includes, but is not limited to, preventing, delaying, and / or treating uneven skin color; reducing the pore size in mammalian skin; regulating the oily / glossy appearance of mammalian skin; thickening the keratinous tissue (i.e., constructing the epidermis and / or dermis and / or subcutaneous layer of the skin and, where applicable, the stratum corneum of the nail and hair shaft); preventing, delaying, and / or treating uneven skin color by acting as a brightening agent or a pigmentation reducing cosmetic; preventing, delaying, and / or treating mammalian skin atrophy; softening and / or smoothing mammalian lips, hair, and nails; preventing, delaying, and / or treating mammalian skin itching; preventing, delaying, and / or treating the appearance of dark circles and / or puffy eyes; preventing, delaying, and / or treating mammalian skin sallowness; preventing, delaying, and / or treating mammalian skin sagging (i.e., glycation); preventing and / or delaying mammalian skin tanning; exfoliating, peeling, and / or increasing the metabolic turnover of mammalian skin; preventing, delaying, and / or treating hyperpigmentation, such as post-inflammatory hyperpigmentation; preventing, delaying, and / or treating the appearance of spider veins and / or erythema on mammalian skin; preventing, delaying, and / or treating fine lines and wrinkles in mammalian skin; preventing, delaying, and / or treating skin dryness (i.e., roughness, flaking, peeling); and preventing, delaying, and / or treating the appearance of cellulite in mammalian skin. In some embodiments, the composition is used to treat signs of aging. For example, in some embodiments, the composition is used to regulate signs of aging. In some embodiments, the composition is used to reduce or decrease signs of aging. In some embodiments, the composition is used to prevent signs of aging in keratinous tissue (e.g., skin, hair, or nails).Improving the condition of the keratinized tissue can involve topically applying a safe and effective amount of the disclosed compositions to the keratinized tissue. Non-limiting examples of skin care compositions include, but are not limited to, sunscreens and skin care bars, mousses, bath and shower gels, lip balms, skin conditioners, cold creams, moisturizers, soaps, body scrubs, body washes, facial washes, body sprays, peelants, astringents, scruffing washes, shaving and depilatory agents, pre-shave and post-shave products, deodorants and antiperspirants, cleansers, skin gels and rinses, skin brightening and self-tanning compositions. Non-limiting examples of hair care compositions include, but are not limited to, shampoos, conditioners, treatments, styling agents, hair sprays, permanent waving agents, tonics, cream rinses, hair dyes, hair colorings, hair bleaches, hair glosses, hair serums, anti-curling agents, volumizers, split end repair agents, anti-dandruff preparations, and mascaras. Non-limiting examples of other cosmetic compositions include, but are not limited to, cosmetics, including lipsticks, rouges, foundations, blushes, eyeliners, lip liners, lip glosses, facial or body powders, nail polishes, eye shadows, etc. Additionally, the compositions can be topically applied by using patches or other delivery devices. Delivery devices can include, but are not limited to, those that can be heated or cooled, and those that utilize iontophoresis or ultrasound. In some embodiments, for example, the compositions described herein are in the form of skin washes, clear washes, milky washes, creams, gels, foams, ointments, pastes, lotions, sprays, conditioners, tonics, cosmetics, lip balms, foundations, nail polishes, aftershaves, etc., which are intended to remain on the skin or other keratinized tissue for some aesthetic, prophylactic, therapeutic, or other benefit (i.e., "leave-on" compositions or skin care compositions). After applying the composition to the keratinized tissue (e.g., skin), it is preferably retained for at least about 2 minutes, 5 minutes, 15 minutes, more preferably at least about 30 minutes, even more preferably at least about 1 hour, and even more preferably for at least several hours, such as up to about 12 hours. Any part of the external portion of the face, hair, and / or nails can be treated (e.g., the face, lips, under-eye area, eyelids, scalp, neck, torso, arms, hands, legs, feet, fingernails, toenails, head hair, eyelashes, eyebrows, etc.). Application of the compositions of the present invention can be carried out using the palm and / or fingers or devices or tools (e.g., cotton balls, swabs, pads, application pens, spray applicators, etc.). Another way to ensure continuous exposure of the keratinized tissue to at least a minimum level of the composition is by applying the compound using, for example, a patch applied to the face. Such methods are particularly useful for problem skin areas that require more in-depth treatment (e.g., the crow's feet area of the face, frown lines, under-eye area, upper lip, etc.). The patch can be closed, semi-closed, or non-closed, and can be adhesive or non-adhesive. The composition can be contained within the patch or applied to the skin prior to applying the patch.In some embodiments, the patch is formed by the self-assembled peptide structure itself without the need for an additional non-peptide substrate. The patch can also include additional active agents, such as chemical initiators for exothermic reactions. The patch can also contain an electrical energy source (such as a battery) to, for example, increase the delivery of the composition and the active agent (such as iontophoresis). The patch is preferably left on the keratinized tissue for at least about 5 minutes, or at least about 15 minutes, or at least about 30 minutes, or at least about 1 hour time period, or as a form of night treatment at night. Applicator In some embodiments, the composition can be delivered by a variety of applicators suitable for topical and general administration. By way of example, suitable applicators can be droppers and bottles that contain the composition. A pen-shaped stick with a housing that can contain the composition can also be used. The stick can include a handle, a shaft, and an applicator head. The applicator head can include fibers, foam, cotton, a roller ball, or any other suitable material that can releasably contain the composition. Exemplary applicators include devices, penetration enhancers, micromanipulation needles, etc. A simple cotton swab can topically apply the composition to the wrinkled area. Other suitable applicators include the SH-0127 pen-type applicator, which can be obtained from Shya Hsin Plastic Works, Inc. in Taiwan; and the Xpress Tip or liquid-filled swab, which can be obtained from SwabPlus, Inc. in China. The applicator can be configured to easily apply the composition to a wrinkled area having an approximate diameter between about 2 mm and about 20 mm and allow the dose of the composition to be between about 0.01 and about 2 mg / cm 2 or between about 0.1 and about 1 mg / cm 2 between. The thickness of the applied film can be measured or calculated based on the application area and the application dose given directly above. In another embodiment, the applicator can be in the form of a pre-treated strip. The strip can be treated or impregnated with the composition herein and then applied to the skin by any suitable strip dispensing mechanism. In a particularly preferred embodiment, the strip can contain a dissolvable material, such as a water-soluble polyvinyl alcohol (PVA) film. Such a material allows the user to apply the pre-treated strip without removing the strip backing during application because the backing will eventually dissolve, leaving only the composition at the treatment site. In a preferred embodiment, the applicator can facilitate the transdermal delivery of the composition herein. Thus, the applicator can take the form of a transdermal patch, a micromanipulation needle applicator, etc. KitAs described above and in general herein, the present invention also provides a kit comprising the self-assembling peptide or a composition thereof of the present invention. The kit is typically provided in a suitable container (e.g., foil, plastic, or cardboard packaging). The kit of the present invention may include one or more excipients, additives, etc., as described herein. The kit of the present invention may include means for proper administration, including an applicator. The kit of the present invention may include instructions for proper administration and / or a formulation for proper administration. For example, in certain embodiments, the present invention provides a beauty kit comprising: (a) the self-assembling peptide of the present invention, its beauty composition; (b) instructions for inducing the self-assembly of the peptide into a macroscopic structure within the skin; and (c) instructions for topically introducing the self-assembling peptide into a subject, including in a liquid in which the peptide can be dissolved, its ions or salts for inducing or triggering the self-assembly of the peptide, and one or more optional compositions, triggering or treatment regimens, as needed. Although some of the methods described herein contemplate the administration of the compositions of the present invention using an applicator, it should be understood that an applicator is not required and the compositions of the present invention can also be administered directly by using a finger or in other conventional ways. The dimensions and values disclosed herein should not be construed as being strictly limited to the exact numerical values recited. Instead, unless otherwise stated, each such dimension is intended to represent the recited value and a functionally equivalent range around that value.Experimental and ExamplesThe following representative examples are intended to assist in illustrating the present invention and are not intended nor should they be construed as limiting the scope of the present invention. In fact, various modifications of the present invention and many other embodiments thereof will become apparent to those skilled in the art from the entire contents of this document, including the following examples and the scientific and patent literature cited herein. The following examples contain important additional information, illustrations, and guidance, which can be adapted for the practice of the present invention in its various embodiments and their equivalents. Testing Method Examples 2 : Characterization of the self-assembling compositionThe solution-gel (sol-gel) transition of each peptide was studied in the research, and the results are shown in Table 4 below. In some cases, when the sol-gel transition was affected by adding salts, the higher the ionic strength, the lower the peptide concentration required to form a gel, and the formulation parameters were maintained in the composition such that the peptide did not form a gel. In the composition, by adding any monovalent and / or divalent cations or temperature to pH 3-9, an ionic strength of about 0 M - about 5 M salt concentration (e.g., ZnCl 2The influence of, for example, NaCl, etc. plays a key role in preventing self-assembly in the formulation. In the composition, the pH can be in the range of about 3 - 9. In some compositions, the amount of the peptide can be in the range of about 0.001 wt% to 30 wt%, and the temperature of the composition can be in the range of about 19°C to 42°C. Example 3 : The generation of temperature-dependent self-assembled elastic fibers from peptides in ex vivo dermal tissue involves a condensation self-assembly process, which causes the accumulation of hydrophobic tropoelastin molecules prior to cross-linking at lysine to produce mature elastic fibers. Elastin-like peptides (ELPs) undergo a temperature-driven conformational change upon heating, known as inverse temperature transition (ITT). The inventors of this application showed that the peptides self-assembled into cell-free ex vivo dermal tissue under different temperature conditions, indicating that self-assembly occurred on the existing elastic fibers present in the skin layer and was enhanced with increasing temperature. To demonstrate the temperature-driven self-assembly of ELP on existing elastic fibers, abdominal skin samples were obtained and stabilized overnight in DMEM containing 10% fetal bovine serum (FBS) and 3% penicillin / streptomycin / amphotericin B. Biopsies (12 mm) were isolated and immersed in de-epithelialization buffer (0.605% Trizma, 4% NaCl, and 0.202% EDTA in PBS) at 37 °C overnight to remove the epidermis, and then immersed in four changes of decellularization buffer (1% Triton X-100 and 0.25% tributyl phosphate in PBS) at 37 °C for 48 h. After decellularization, the skin (hereinafter referred to as dermis) was washed three times in PBS buffer (1X) for 2 h each time. The decellularized dermis was immersed in PBS, 100 μg / mL Pal-VGVAPG, or Ace-IGVAPG for five days, with the solution changed daily. The three ex vivo dermis used for each treatment were incubated at 4 °C, 37 °C, or 42 °C. The decellularized dermis was fixed in 10% formalin overnight, embedded in paraffin, and sectioned at 8 μm. H & E and Elastin van Gieson staining were performed to confirm decellularization and visualize elastic fibers, respectively. Using NIH ImageJ software, elastic fiber density quantification was performed by thresholding the elastic fibers, and the measurements were recorded. H & E staining confirmed successful decellularization of the tissue (data not shown). The absence of cell nuclei demonstrated that the dermis could not resynthesize elastic proteins. Figure 1A indicates a representative image of decellularized dermis stained with Elastin van Gieson, which was incubated with Pal-VGVAPG and Ace-IGVAPG at different temperatures while the concentration was kept constant (100 μg / mL). Elastic fibers were stained black on a 50 μm scale bar. As shown in Figure 1A, Elastin van Gieson staining showed temperature-driven co-assembly of ELP with existing elastic fibers compared to dermis immersed in PBS. The results showed a moderate increase was observed when the dermis was incubated at 4 °C, while higher temperatures of 37 °C and 42 °C showed more significant elastic protein staining. Dermis immersed in Pal-VGVAPG showed an increase in signal with increasing temperature, while the Ace-IGVAPG peptide showed the highest increase at 37 °C.Dermis immersed in PBS showed similar baseline intensity, independent of temperature, as shown in Figure 1A. Figure 1B shows the quantification of elastic fiber density (arbitrary units) in the decellularized dermis, where the mean was considered significant when compared to PBS at the same temperature. p ≤ 0.05, **p ≤ 0.01, and when compared within the same treatment at different temperatures, + p≤0.05. Statistical significance of differences between means was performed using two-way ANOVA, followed by Tukey's multiple comparison test. Error bars represent the standard error of the mean (SEM). All analyses were performed using Prism 8 software (GraphPad, San Diego, CA, USA). The results showed that, consistent with qualitative histological observations, analysis of elastic fiber density by Elastin van Gieson staining confirmed that when the dermis was treated with Pal-VGVAPG, the integrated density increased significantly at 37 °C and 42 °C, while treatment with Ace-IGVAPG showed a significant increase in integrated density at 42 °C compared to PBS-treated samples at the same temperature. In addition, a significant difference was observed between 42 °C and 4 °C in the dermis treated with Pal-VGVAPG. The results in Figures 1A and 1B indicate that ELP co-assembles with existing elastic fibers and that this assembly is positively regulated with increasing temperature. These results also suggest that the increase in elastic protein staining in the decellularized dermis is due to self-assembly, and that temperature acts as a catalyst or trigger for assembly within the skin layer. Example 4 : The self-assembly of concentration-driven biomolecules within the skin depends on the critical self-assembly concentration, where the self-assembling biomolecules remain monomers below the critical concentration and assemble above a specific concentration threshold. Using the in vitro critical concentration, we showed that increasing the concentration of ELP increased the elastic fiber density, indicating enhanced non-covalent interactions of ELP with pre-existing elastic fibers. To demonstrate concentration-driven self-assembly, as described in Example 3, abdominal skin explants were obtained and stabilized overnight, and biopsies were performed. Biopsies (12 mm) were topically treated with various concentrations of Ace-IGVAPG or Pal-VGVAPG (12.5, 25, 50 μg / mL) while maintained in DMEM containing 10% FBS and 1% penicillin / streptomycin / amphotericin B. The skin was fixed with formalin, embedded in paraffin, sectioned at 8 μm, and stained for elastin with Elastin van Gieson. Figure 2 shows representative images of ex vivo skin topically treated with various concentrations of ELP, Pal-VGVAPG, and Ace-IGVAPG. Elastin van Gieson staining shows enhanced elastin (dark black fibers) with increasing concentration at a scale of 20 μm. The results in Figure 2 indicate that histological evaluation of skin treated with ELP shows a direct correlation between the elastin fiber staining intensity and the concentrations of Pal-VGVAPG and Ace-IGVAPG, where the elastin intensity increases at 12.5 μg / mL, 25 μg / mL, and 50 μg / mL of the peptide amphiphile Pal-VGVAPG, respectively. Similarly, the results show that the elastin intensity increases at 25 μg / mL and 50 μg / mL of Ace-IGVAPG, respectively. Example 5 : within intact ex vivo skin pH Both exogenous and endogenous factors control self-assembly, two of which are pH and salinity. The skin has a pH gradient, where the skin surface is approximately between pH 4.2 - 5.6, significantly increasing to pH 6.8 at the interface of the stratum corneum and granular layer, and the pH continues to increase to 7.4 in the dermis. The skin also varies in salt content, with an interstitial NaCl level of approximately 0.9%, while the NaCl level in sweat secretions on the skin surface is approximately 0.2%. However, the surface salt content depends on climate adaptation. To illustrate the visualization of the effects of pH and salinity on peptide self-assembly in tissues, peptides were labeled with propargylglycine using F-moc chemistry. As described in Example 4, biopsies (12 mm) of abdominal skin explants were isolated, maintained, and topically treated with propargylglycine-labeled peptides (8 μL) twice a day for 5 days. Propargylglycine-labeled peptides included A6K, IEIK-13, KLD-12, RADA-16, IGVPAG, and VGVPAG. To determine how pH and salinity affect peptide assembly in the skin, propargylglycine-labeled peptides were prepared at various pHs from pH 3 - 9 or at salinities or in the presence of salt contents ranging from 0.1 - 3.0%. The skin was fixed, cryoprotected, cryosectioned (8 μm), and stored at -20 °C until copper(I)-catalyzed alkyne-azide cycloaddition (CuAAC) or click chemistry was performed to detect peptide assembly. Representative results are shown herein. Click chemistry was performed by incubating tissue sections with a working solution of Alexa Fluor-594 azide (12.5 μM), sodium ascorbate (2.5 mM), copper(II) sulfate pentahydrate (75 μM), and tris(3-hydroxypropyltriazolylmethyl)amine (THPTA, 150 μM) for 1 hour. The sections were washed, mounted with Fluoromount-G plus DAPI, and imaged using a Zeiss Axio Observer Z1 fluorescence automated microscope. Click chemistry is a technique using two bioorthogonal functional groups (alkyne and azide) that form a triazole in the presence of copper(I). The effect of the alkyne on the end of the peptide on various aspects of the molecule can be neglected, which will affect the penetration of the peptide in the tissue (i.e., molecular weight, log P, isoelectric points, and self-assembly), allowing the peptide to penetrate based on its inherent properties. Once the alkyne-peptide is delivered to the tissue, the sample is fixed and "stained" with an azide-fluorophore. The tissue is incubated with the azide-fluorophore, copper(II) sulfate pentahydrate (catalyst), THPTA (ligand), and sodium ascorbate (reductant), and the system forms an active copper(I) complex that is capable of forming a triazole between the alkyne of the peptide and the azide of the fluorophore. Because CuAAC is a rapid, chemoselective, bioorthogonal reaction, only the alkyne-labeled peptide is reactive, leaving the tissue unaffected and intact. This click histology protocol allows for the selective detection of peptides of interest by fluorescence microscopy in the presence of endogenous peptides and / or proteins. Micrographs of skin topically treated with the propargylglycine forms of KLD-12, Pal-VGVAPG, and Ace-IGVAPG at a constant concentration (0.6 mg / mL) at pH 4 - 9. Bright field (left panel) and Alexa Fluor 594 click-labeled peptides (right panel) are shown in Figure 3 at a scale of 20 μm. Figure 3 shows the results of click histology, which reveals that at all pH levels, the peptides insert and assemble within the stratum corneum. However, at specific pH levels, peptide self-assembly is also observed in the lower layers of the skin, as seen for KLD-12 at pH 6 in Figure 3, Pal-VGVAPG at pH 6 and 8 in Figure 5, and Ace-IGVAPG at pH 5 and 7 (data not shown). Figure 4 shows micrographs of ex vivo skin topically treated with the propargylglycine forms of KLD-12, Pal-VGVAPG, and Ace-IGVAPG (0.6 mg / mL) at different ionic strengths by varying the salt content (0.1%, 0.5%, 1%, 2%, 3% NaCl). Bright field (left panel) and Alexa Fluor 594 click-labeled peptides (right panel) are shown at a scale of 20 μm. The results in Figure 4 show that when evaluating the effect of salinity on peptide assembly in the skin, the peptides assemble within the stratum corneum at different NaCl concentrations. At specific salt concentrations, peptide assembly is seen in the underlying skin layers, as visible for KLD-12 at 0.1%, 1%, and 2% NaCl levels in Figure 4 and Pal-VGVAPG at 0.1% and 2% NaCl levels in Figure 5. Representative results of Pal-VGVAPG regarding the combination of pH and salinity related to dermal staining are shown in Figure 5. As described above, the click histology results reveal that at specific pH and salinity levels, peptide self-assembly is also observed in the lower layer (i.e., the dermal layer) of the skin. Example 6 : in ex vivo skin ELP Self-assembly related increase in skin elasticity To demonstrate the cosmetic benefits of increased skin elasticity through peptide self-assembly and co-assembly, ex vivo skin biopsies (12 mm) were topically treated with Ace-IGVAPG. After 24 hours, a TA.XT Plus texture analyzer was used to indent the ex vivo skin, using a 7 mm cylindrical probe, a strain of 40%, and a withdrawal rate of 0.1 mm / s. The TA.XT Plus software generated a curve representing the force (g) applied to the probe by the biopsy over time (seconds), and the percentage of recovery was calculated using the area under the curve of the indentation duration and the probe withdrawal time. The percentage of recovery is the area under the curve (A 2 ) during the withdrawal phase and the area under the curve (A 1) ratio, as shown in exemplary Figure 6A. Figure 6B shows the results of the cosmetic benefit of enhanced skin elasticity. The pure elastic material has a 100% recovery percentage. Since the skin is viscoelastic, its recovery will never be equal to that of the pure elastic material. For example, the recovery percentage of ex vivo skin is 25%-35%. As an example, Figure 6A shows an exemplary curve generated by the index connection software associated with the texture analyzer and the recovery percentage equation shown below the curve. Figure 6B shows the recovery percentage of an ex vivo skin biopsy after topical treatment with Ace-IGVAPG (25 mg / mL) for 24 hours. Error bars represent SEM (standard error of the mean), by two-tailed t-test, where **p ≤ 0.01. All analyses were performed using Prism 8 software (GraphPad, San Diego, CA, USA). The results showed that the skin treated with 25 μg / mL of Ace-IGVAPG had a significantly higher recovery percentage (p = 0.0056) when compared to the untreated control, indicating an increase in the elasticity of the ex vivo skin biopsy. Thus, the results in Figure 6B show that after 24 hours of topical treatment, topical treatment with Ace-IGVAPG (25 μg / mL) provides approximately 25% higher recovery than the untreated sample. In the case of reciting a numerical range, it should be understood that each intermediate integer value and each fraction between the upper and lower limits recited in the range of the recitation are also specifically disclosed, as well as each sub-range between such values. The upper and lower limits of any range can be independently included in or excluded from the range, and each range that does not include any limit value or both limit values is also included in the present invention. When the values discussed have inherent limits, such as when a component can be present at a concentration of 0.001-30%, or when the pH of an aqueous solution can be in the range of 3-9, those inherent limits are specifically disclosed. When a value is explicitly recited, it should be understood that values of approximately the same quantity or amount as the recited value are also within the scope of the present invention, as well as the ranges based thereon. In the case of disclosing a combination, each sub-combination of the elements of the combination is also specifically disclosed and within the scope of the present invention. Conversely, in the case of disclosing different elements or groups of elements, their combinations are also disclosed. In the case where any element of the present invention is disclosed as having multiple alternatives, examples of the present invention are also hereby disclosed in which each alternative is excluded individually or in any combination with other alternatives; more than one element of the present invention can have such exclusions, and all combinations of elements having such exclusions are hereby disclosed. Unless explicitly excluded or otherwise limited, each document cited herein (including any cross-reference or related patent or application) is incorporated herein by reference in its entirety. The citation of any document is not an admission that it is prior art to any invention disclosed or claimed herein, or that it alone or in any combination with any other reference, or references, teaches, suggests, or discloses any such invention.In addition, when any meaning or definition of a term in the present invention conflicts with any meaning or definition of the same term in a document incorporated by reference, the meaning or definition of the term specified in the present invention shall prevail. Although specific embodiments of the present invention have been illustrated and described, it will be apparent to those skilled in the art that many other changes and modifications can be made without departing from the spirit and scope of the present invention. Accordingly, the appended claims are intended to cover all such changes and modifications within the scope of the present invention. [Figure 1] shows the results of elastin fiber measurements obtained from histological images and corresponding analyses. Figure 1A shows elastin van Gieson staining, showing the co-assembly of temperature-driven elastin-like peptides (ELPs) with existing elastin fibers compared to the dermis. Figure 1B shows the quantification of elastin fiber density in acellular dermis. [Figure 2] shows representative images of ex vivo skin topically treated with various concentrations of ELP, Pal-VGVAPG, and Ace-IGVAPG. [Figure 3] shows the results of click histology. [Figure 4] shows the salinity effect of peptide self-assembly. [Figure 5] shows representative results for the combination of pH and salinity for Pal-VGVAPG. [Figure 6] demonstrates the cosmetic benefit of increased skin elasticity in ex vivo skin through self-assembly and co-assembly of peptides.

Claims

1. A cosmetic composition comprising at least one self-assembling material for use in the manufacture of an agent for reconstructing the skin without cellular biogenesis by influencing structural changes within the skin, wherein the structural changes are sufficiently large to be visible at a magnification of 10x or greater; wherein the self-assembling material is a peptide having a Pal-KTTKS chemical structure; wherein the self-assembling material, upon triggering, forms a large, ordered, well-defined 3D functional macromolecular structure within the skin, wherein the large, ordered, well-defined 3D functional macromolecular structure is sufficiently large to be visible at a magnification of 10x or greater; wherein the triggering includes a pH of 5, a temperature of 37°C, and a concentration of ≥ 0.5% w / w; and wherein upon triggering, the agent self-assembles into elastin fibers within the skin.

2. The use as claimed in claim 1, further comprising enabling the self-assembly of the at least one self-assembly material within the skin while substantially preventing the self-assembly of the at least one self-assembly material present in the cosmetic composition prior to its application.

3. The use as claimed in claim 2, wherein the use provides at least one cosmetic skin care treatment.

4. As claimed in claim 1, wherein the agent achieves self-assembly after topical application.

5. As claimed in claim 4, wherein the agent achieves self-assembly within 6 hours after topical application.

6. As claimed in claim 4, wherein the agent achieves self-assembly within 4 hours after topical application.

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