Hybrid polymer comprising a polysaccharide polymer and peptide chains

Abstract

The present invention relates to a hybrid polymer comprising a polysaccharide polymer and certain peptide chains, to blends, hydrogels and formulations comprising the hybrid polymer, and to the use of the hybrid polymer as a rheology modifying agent.

Description

[0001]HYBRID POLYMER COMPRISING A POLYSACCHARIDE POLYMER AND PEPTIDE CHAINS The present invention relates to a hybrid polymer comprising a polysaccharide polymer and certain peptide chains, to blends, hydrogels and formulations comprising the hybrid polymer, and to the use of the hybrid polymer as a rheology modifying agent.Cleansing and caring for skin and hair is very important for general hygiene, e.g. forremoval of unwanted materials such as sebum, oils, dirt, makeup, or formoisturization, coloring or protection. Many cosmetic products require a certainminimum viscosity in order to achieve ease of application to the substrate and / or retention on the substrate to be treated. Many cosmetic products comprise viscosity-increasing or rheology modifying agents. These are often referred to as thickeningagents, thickeners or gelling agents. Thickening agents used in cosmetics orpersonal care products include polyethylene glycol, polyacrylic acid, vegetable gums,polycarboxylates (Carbopols), homopolymers and copolymers based on 2-acrylamido-2-methyl-1-propanesulfonic acid (AMPS).Many ingredients used in cosmetics are traditionally derived from crude oil.Environmental and economic factors restrict the use of products derived from thislimited resource. There is a desire to identify more sustainable and biodegradable, yet gentle and effective materials. Indeed, consumers are interested in naturalproducts including products with a high percentage of natural ingredients and / oringredients that are derived from renewable materials. Consumers perceive productsderived from natural materials to be gentler and more environmentally friendly.Ingredients derived from renewable materials have various other benefits such asincreased biodegradability and more sustainable availability. Compounds derivedfrom plant-based resources are particularly useful because the source compound cansimply be regrown. WO2018 / 108663, WO2018 / 108664, WO2018 / 108665, and WO2018 / 108667 disclose water-soluble and / or water-swellable hybrid polymers comprising a polysaccharide polymer and a synthetic polymer.There is an ongoing need for polymeric rheology modifiers that can provide theexcellent performance of modern polymers with the increased biodegradability and the more sustainable availability of natural-based polymers. It has now been found that hybrid polymers comprising a polysaccharide polymer and certain peptide chains are useful as rheology modifying agents. The present invention relates to a hybrid polymer comprising(a) a polysaccharide polymer; and(b) peptide chains comprising an amino acid sequence of general formula (I):X1–A4–A5–A6–X2(I) wherein X1represents –H, A3–, A2–A3– or A1–A2–A3–; X2represents –H, –A7, –A7–A8, –A7–A8–A9, –A7–A8–A9–A10, or –A7–A8–A9–A10–A11; A1and A4represent independently of each other a small neutral amino acid or a neutral hydrophilic amino acid; A2and A5represent independently of each other a neutral amino acid, an aromatic amino acid or an amino acid amide; A3 represents a basic amino acid, a large neutral amino acid, or an amino acidamide; A6 represents an amino acid selected from S, T, C, N, Q, Y, A, G and V;A7and A8represent independently of each other a neutral amino acid; A9 represents a basic amino acid, or an amino acid amide;A10 represents a basic amino acid, or an aromatic amino acid; andA11represents a neutral amino acid, a hydrophilic amino acid, or an amino acid amide. The hybrid polymers of the invention show excellent performance as rheologymodifying agents. They form hydrogels having the desired properties.Advantageously, the hybrid polymers of the invention have a high renewable carboncontent and are biodegradable, i.e., they are sustainable.The hybrid polymer of the invention comprises (a) a polysaccharide polymer and (b)peptide chains as defined herein. Preferably, the combined amount of (a) thepolysaccharide polymer and (b) the peptide chains in the hybrid polymer is at least 50 wt-%, more preferably at least 60 wt-%, more preferably at least 70 wt-%, morepreferably at least 75 wt-%, more preferably at least 80 wt-%, more preferably atleast 85 wt-%, even more preferably at least 90 wt-%, even more preferably at least95 wt-%, even more preferably at least 97 wt-%, even more preferably at least 98 wt-%, particularly preferably at least 99 wt-%, based on the total weight of the hybridpolymer. The hybrid polymer of the invention comprises (a) a polysaccharide polymer. Preferably, the polysaccharide polymer is water-soluble and / or water-swellable. In at least one embodiment, the polysaccharide polymer absorbs water and / or forms a gel or gum when immersed in water. In at least one embodiment, the polysaccharide polymer is a natural gum. Natural gums are useful because they are generallysoluble in water due to the presence of an excessive number of OH groups whichform hydrogen bonds with water molecules. In at least one embodiment, the polysaccharide polymer is a natural gum derived from a plant.In preferred embodiments, the polysaccharide polymer is selected from dextran,dextrin, hyaluronic acid, chitosan, xanthan gum, fenugreek gum, tara gum, locustbean gum, carrageenan, guar gum, alginate, agar, agarose, starch, amylose,amylopectin, tragacanth gum, tamarind kernel gum, arabica gum, cherry gum, karayagum, okra gum, cassia gum, chicle gum, konjac gum, ghatti gum, pectin, sclerotiumgum, gellan gum, paramylon, paramylum, curdlan, cellulose, diutan gum, inulin,derivatives thereof and mixtures thereof. In more preferred embodiments, the polysaccharide polymer is selected from dextran, dextrin, hyaluronic acid, xanthan gum, tara gum, locust bean gum, carrageenan, guar gum, alginate, starch, amylose, amylopectin, tamarind kernel gum, arabica gum, karaya gum, konjac gum, pectin, sclerotium gum, gellan gum,diutan gum, inulin, derivatives thereof and mixtures thereof. In more preferredembodiments, the polysaccharide polymer is selected from dextran, dextrin, xanthan gum, tara gum, locust bean gum, carrageenan, guar gum, alginate, starch, amylose,amylopectin, tamarind kernel gum, arabica gum, karaya gum, konjac gum, pectin,sclerotium gum, gellan gum, diutan gum, inulin, derivatives thereof and mixturesthereof. In even more preferred embodiments, the polysaccharide polymer is selected from dextran, dextrin, hyaluronic acid, xanthan gum, tara gum, locust bean gum, carrageenan, guar gum, alginate, starch, amylose, amylopectin, konjac gum, pectin,inulin, derivatives thereof and mixtures thereof. In even more preferred embodiments,the polysaccharide polymer is selected from dextran, dextrin, xanthan gum, tara gum,locust bean gum, carrageenan, guar gum, starch, amylose, amylopectin, konjac gum,inulin, derivatives thereof and mixtures thereof.In particularly preferred embodiments, the polysaccharide polymer is dextran orhyaluronic acid. In particularly preferred embodiments, the polysaccharide polymer isdextran. In particularly preferred embodiments, the polysaccharide polymer ishyaluronic acid.Derivatives of the above polysaccharide polymers may also be used. “Derivative”means that the polysaccharide polymer was subjected to one or more suitablephysical, chemical or enzymatic processes to be converted into a derivative of thepolysaccharide polymer. Examples of such processes include:- acidic treatment of polysaccharide polymer by the reaction with acids (e.g.hydrochloric acid, phosphoric acid, or sulfuric acid)- alkaline treatment of polysaccharide polymer by the reaction with bases (e.g.sodium hydroxide or potassium hydroxide)- bleached polysaccharide polymer by the reaction with peracetic acid, hydrogenperoxide, sodium hypochlorite, sulfur dioxide, sulfites, potassium permanganate or ammonium persulfate- enzymatic modification of the polysaccharide polymer by treatment with enzymes- oxidized polysaccharide polymer by oxidation (e.g. with sodium hypochlorite)- acetylated polysaccharide polymer by esterification with e.g. anhydrides- hydroxypropyl polysaccharide polymer by reaction with propylene oxide- hydroxyethyl polysaccharide polymer by reaction with ethylene oxide- carboxymethylation of the polysaccharide polymer- glycol polysaccharide polymerPreferred derivatives of the polysaccharide polymers are selected from carboxymethyl polysaccharides, hydroxyethyl polysaccharides, carboxymethyl hydroxyethyl polysaccharides, carboxypropyl polysaccharides, glycol polysaccharides, and mixtures thereof. Examples of preferred derivatives of the polysaccharide polymers are carboxymethyl cellulose, hydroxyethyl cellulose, carboxymethyl hydroxyethyl cellulose,carboxypropyl cellulose, carboxymethyl chitosan, glycol chitosan, or mixtures thereof.The polysaccharide polymers may, for example, be used in the form of its salts.Hyaluronic acid may, for example, be used in the form of its salts. Hyaluronic acidmay, for example, be used in the form of its sodium salt.In preferred embodiments, the polysaccharide polymer has a weight averagemolecular weight of from 3000 to 12000000 g / mol, preferably from 10000 to 5000000 g / mol, more preferably from 30000 to 2000000 g / mol, even more preferably from 50000 to 1000000 g / mol, particularly preferably from 100000 to 500000 g / mol. In preferred embodiments, the polysaccharide polymer has a weight average molecular weight of from 3000 to 1000000 g / mol, preferably from 10000 to 500000 g / mol, more preferably from 20000 to 300000 g / mol, even more preferably from 30000 to 200000 g / mol, particularly preferably from 40000 to 150000 g / mol. In a preferred embodiment, the polysaccharide polymer has a weight averagemolecular weight of from 15000 to 75000 g / mol, preferably from 20000 to 70000g / mol, more preferably from 20000 to 60000 g / mol, more preferably from 30000 to60000 g / mol, even more preferably from 30000 to 50000 g / mol, even more preferablyfrom 35000 to 45000 g / mol, for example 40000 g / mol. In a preferred embodiment, thepolysaccharide polymer has a weight average molecular weight of from 40000 to 60000 g / mol, preferably from 45000 to 55000 g / mol, for example 50000 g / mol. In a preferred embodiment, the polysaccharide polymer has a weight average molecular weight of from 100000 to 200000 g / mol, preferably from 120000 to 180000 g / mol, more preferably from 130000 to 170000 g / mol, even more preferably from 140000 to 160000 g / mol, for example 150000 g / mol.In a preferred embodiment, the polysaccharide polymer has a weight averagemolecular weight of at least 180000 g / mol, preferably at least 200000 g / mol. As used herein, the molecular weight, including the weight average molecular weight,of the polysaccharide polymer is determined using gel permeation chromatography(GPC). GPC experiments are performed using a PSS SECcurity2instrument consisting of a pump, autosampler and column oven. A column SUPREMA LIN XL of300 x 8 mm and 10 µm average particle size is used at a flow rate of 1.0 mL / min anda column temperature of 25°C. As eluent 0.1M NaNO3 is used. The hybrid polymer of the invention comprises (b) peptide chains comprising an amino acid sequence of general formula (I): X1–A4–A5–A6–X2(I) wherein X1represents –H, A3–, A2–A3– or A1–A2–A3–; X2represents –H, –A7, –A7–A8, –A7–A8–A9, –A7–A8–A9–A10, or –A7–A8–A9–A10–A11; A1and A4represent independently of each other a small neutral amino acid or a neutral hydrophilic amino acid; A2and A5represent independently of each other a neutral amino acid, an aromatic amino acid or an amino acid amide;A3 represents a basic amino acid, a large neutral amino acid, or an amino acidamide;A6 represents an amino acid selected from S, T, C, N, Q, Y, A, G and V;A7and A8represent independently of each other a neutral amino acid;A9 represents a basic amino acid, or an amino acid amide;A10 represents a basic amino acid, or an aromatic amino acid; andA11represents a neutral amino acid, a hydrophilic amino acid, or an amino acid amide.Preferably, A6 represents an amino acid selected from S, T, C, N and Y.Particularly preferably, A6 represents an amino acid selected from S and T.In a preferred embodiment, A1, A2, A3, A4, A5, A6, A7, A8, A9, A10, and A11in the general formula (I) have the following meanings: A1represents an amino acid selected from G and A; A2represents an amino acid selected from Y, F, and W; A3represents an amino acid selected from R, K, and L; A4represents an amino acid selected from G and A; A5represents an amino acid selected from I, Y, Q, N, L, and F; A6represents an amino acid selected from S and T; A7represents an amino acid selected from L, I, and V; A8represents an amino acid selected from A, G, and V; A9represents an amino acid selected from K, N, and Q;A10 represents an amino acid selected from W and F; andA11represents an amino acid selected from M, M-NH2, L, I, V, A, and G. In a more preferred embodiment, A1, A2, A3, A4, A5, A6, A7, A8, A9, A10, and A11in the general formula (I) have the following meanings: A1represents an amino acid selected from G and A; A2represents an amino acid selected from Y and F; A3represents an amino acid selected from R, K, and L; A4represents an amino acid selected from G and A; A5represents an amino acid selected from I and Y; A6represents an amino acid selected from S and T; A7represents an amino acid selected from L and I; A8represents an amino acid selected from A and G; A9represents an amino acid selected from K and N;A10 represents an amino acid selected from W and F; andA11represents an amino acid selected from M, M-NH2, L, I, and V. In an even more preferred embodiment, A1, A2, A3, A4, A5, A6, A7, A8, A9, A10, and A11in the general formula (I) have the following meanings: A1represents G; A2represents an amino acid selected from Y and F; A3represents an amino acid selected from R, K and L; A4represents G; A5represents an amino acid selected from I and Y; A6represents an amino acid selected from S and T; A7represents L; A8represents A; A9represents an amino acid selected from K and N;A10 represents W; andA11represents an amino acid selected from M, M-NH2, and V.In a preferred embodiment, X1 and X2 in the general formula (I) have the followingmeanings: X1represents A2–A3– or A1–A2–A3–; and X2represents –A7–A8–A9, –A7–A8–A9–A10, or –A7–A8–A9–A10–A11.In a preferred embodiment, the peptide chains (b) comprise (or consist of) an aminoacid sequence selected from GYLGIS (SEQ ID NO: 2), GISLAN (SEQ ID NO: 3), YRGISLANWM (SEQ ID NO: 4), YRGISLANW (SEQ ID NO: 5), GFRGISLANWM (SEQ ID NO: 6), GYKGISLANWM (SEQ ID NO: 7), GYRGISLANWM (SEQ ID NO: 8), GYRGYSLANWM (SEQ ID NO: 9), GYRGITLANWM (SEQ ID NO: 10), GYRGISLAKWM (SEQ ID NO: 11) GYRGISLANWV (SEQ ID NO: 12), GYLGISLANW (SEQ ID NO: 13), and GYRGISLANWM-NH2 (SEQ ID NO: 14). In a preferred embodiment, the peptide chains (b) comprise (or consist of) an amino acid sequence selected from GYL-GIS (SEQ ID NO: 2), GIS-LAN (SEQ ID NO: 3), YR-GIS-LANWM (SEQ ID NO: 4), YR-GIS-LANW (SEQ ID NO: 5),GFR-GIS-LANWM (SEQ ID NO: 6),GYK-GIS-LANWM (SEQ ID NO: 7), GYR-GIS-LANWM (SEQ ID NO: 8), GYR-GYS-LANWM (SEQ ID NO: 9), GYR-GIT-LANWM (SEQ ID NO: 10), GYR-GIS-LAKWM (SEQ ID NO: 11) GYR-GIS-LANWV (SEQ ID NO: 12), GYL-GIS-LANW (SEQ ID NO: 13), and GYR-GIS-LANWM-NH2(SEQ ID NO: 14). In a more preferred embodiment, the peptide chains (b) comprise (or consist of) an amino acid sequence selected from GYLGIS (SEQ ID NO: 2), GISLAN (SEQ ID NO:3), and GYRGISLANWM (SEQ ID NO: 8).In a particularly preferred embodiment, the peptide chains (b) comprise (or consist of)the amino acid sequence GYRGISLANWM (SEQ ID NO: 8).In a preferred embodiment, the peptide chains (b) comprise (or consist of) an amino acid sequence selected from CGYLGIS (SEQ ID NO: 15), CGISLAN (SEQ ID NO: 16), CYRGISLANWM (SEQ ID NO: 17), CYRGISLANW (SEQ ID NO: 18),CGFRGISLANWM (SEQ ID NO: 19), CGYKGISLANWM (SEQ ID NO: 20),CGYRGISLANWM (SEQ ID NO: 21), CGYRGYSLANWM (SEQ ID NO: 22), CGYRGITLANWM (SEQ ID NO: 23), CGYRGISLAKWM (SEQ ID NO: 24) CGYRGISLANWV (SEQ ID NO: 25), CGYLGISLANW (SEQ ID NO: 26), and CGYRGISLANWM-NH2(SEQ ID NO: 27). In a preferred embodiment, the peptide chains (b) comprise (or consist of) an amino acid sequence selected from CGYL-GIS (SEQ ID NO: 15), CGIS-LAN (SEQ ID NO: 16), CYR-GIS-LANWM (SEQ ID NO: 17), CYR-GIS-LANW (SEQ ID NO: 18),CGFR-GIS-LANWM (SEQ ID NO: 19),CGYK-GIS-LANWM (SEQ ID NO: 20), CGYR-GIS-LANWM (SEQ ID NO: 21), CGYR-GYS-LANWM (SEQ ID NO: 22), CGYR-GIT-LANWM (SEQ ID NO: 23), CGYR-GIS-LAKWM (SEQ ID NO: 24) CGYR-GIS-LANWV (SEQ ID NO: 25), CGYL-GIS-LANW (SEQ ID NO: 26), and CGYR-GIS-LANWM-NH2 (SEQ ID NO: 27). In a more preferred embodiment, the peptide chains (b) comprise (or consist of) anamino acid sequence selected from CGYLGIS (SEQ ID NO: 15), CGISLAN (SEQ IDNO: 16), and CGYRGISLANWM (SEQ ID NO: 21).In a particularly preferred embodiment, the peptide chains (b) comprise (or consist of) the amino acid sequence CGYRGISLANWM (SEQ ID NO: 21). In a preferred embodiment, the peptide chains (b) comprise (or consist of) an amino acid sequence selected from GYLGIS (SEQ ID NO: 2), GISLAN (SEQ ID NO: 3), GYRGISLANWM (SEQ ID NO: 8), CGYLGIS (SEQ ID NO: 15), CGISLAN (SEQ ID NO: 16), and CGYRGISLANWM (SEQ ID NO: 21). In a particularly preferred embodiment, the peptide chains (b) comprise (or consist of) an amino acid sequence selected from GYRGISLANWM (SEQ ID NO: 8) and CGYRGISLANWM (SEQ ID NO: 21).Throughout this specification, amino acid residues will be denoted by the three-letterabbreviation or single-letter code as follows: Amino Acid Three-letter abbreviation One-letter SymbolAlanine Ala AArginine Arg RAsparagine Asn NAspartic Acid Asp DCysteine Cys CGlutamine Gln QGlutamic Acid Glu EGlycine Gly GHistidine His HIsoleucine Ile ILeucine Leu LLysine Lys KMethionine Met MPhenylalanine Phe FProline Pro PSerine Ser SThreonine Thr TTryptophan Trp WTyrosine Tyr YValine Val VThe term “neutral amino acid”, as used herein, refers to any proteinogenic and non-proteinogenic amino acid having an aliphatic or cyclic side chain or no side chain,including but not limited to glycine (Gly, G), alanine (Ala, A), proline (Pro, P), leucine(Leu, L), valine (Val, V), isoleucine (Ile, I), and methionine (Met, M).The term “small neutral amino acid”, as used herein, refers to any proteinogenic andnon-proteinogenic neutral amino acid having a volume of less then 120 ų (van derWaals volume ų; 1 Å = 100 pm = 0.1 nm = 10⁻¹⁰ m), including but not limited toglycine (Gly, G), alanine (Ala, A), and proline (Pro, P).The term “large neutral amino acid”, as used herein, refers to any proteinogenic andnon-proteinogenic neutral amino acid having a volume of more then 120 ų (van derWaals volume ų; 1 Å = 100 pm = 0.1 nm = 10⁻¹⁰ m), including but not limited toleucine (Leu, L), valine (Val, V), isoleucine (Ile, I), and methionine (Met, M).The term “neutral hydrophilic amino acid”, as used herein, refers to any proteinogenicand non-proteinogenic hydrophilic amino acid having a protic functional group in theside chain, but lacking an acidic or basic group in the side chain, including but notlimited to serine (Ser, S), threonine (Thr, T), and cysteine (Cys, C).The term “aromatic amino acid”, as used herein, refers to any proteinogenic and non-proteinogenic amino acid having an aromatic group in the side chain, including butnot limited to phenylalanine (Phe, F), tryptophane (Trp, W), and tyrosine (Tyr, Y).The term “amino acid amide”, as used herein, refers to any proteinogenic and non-proteinogenic hydrophilic amino acid having an amide functional group in the sidechain, including but not limited to asparagine (Asn, N) and glutamine (Gln, Q).The term “acidic amino acid”, as used herein, refers to any proteinogenic and non-proteinogenic amino acid having an acidic (carboxy) group in the side chain,including but not limited to aspartic acid (Asp, D) and glutamic acid (Glu, E).The term “basic amino acid”, as used herein, refers to any proteinogenic and non-proteinogenic amino acid having a basic (amino) group in the side chain, includingbut not limited to lysine (Lys, K), arginine (Arg, R), and histidine (His, H).The amino acids in the peptide chains may have any stereochemical orientation. Forexample, each amino acid may independently from each other be an L-amino acid or a D-amino acid. In one embodiment, all amino acids in the peptide chains are L-amino acids. In one embodiment, all amino acids in the peptide chains are D-aminoacids.The amino acids in the peptide chains may optionally be in its salt form. A personskilled in the art knows that this may depend, for example, on the environment of the peptide chains. For example, an acidic environment may lead to protonation of basicfunctional groups of the side chains of the amino acids. For example, a basicenvironment may lead to deprotonation of acidic functional groups of the side chainsof the amino acids. In preferred embodiments, the peptide chains form aggregates with each other.In preferred embodiments, the peptide chains are self-assembling. Without wishing tobe bound by theory: The peptide chains may form noncovalent bonds with each other. The peptide chains may form a supramolecular assembly. This may lead to noncovalent or supramolecular crosslinking, which may lead to gelation. In one embodiment, the peptide chains may form nanofibers or nanofibrillar structures. In one embodiment, the peptide chains may form beta sheets. In preferred embodiments, at least 50%, preferably at least 60%, more preferably at least 70%, even more preferably at least 80%, even more preferably at least 90%,even more preferably at least 95%, even more preferably at least 98%, particularlypreferably at least 99%, of the amino acids in the peptide chains are proteinogenicamino acids. In preferred embodiments, all amino acids in the peptide chains areproteinogenic amino acids. Preferably, the proteinogenic amino acids are selectedfrom leucine, isoleucine, phenylalanine, valine, tyrosine, tryptophan, lysine, aspartic acid, glutamic acid, arginine, histidine, methionine, serine, threonine, glycine, alanine,proline, cysteine, asparagine, glutamine, selenocysteine, and pyrrolysine. Morepreferably, the proteinogenic amino acids are selected from leucine, isoleucine, phenylalanine, valine, tyrosine, tryptophan, lysine, aspartic acid, glutamic acid, arginine, histidine, methionine, serine, threonine, glycine, alanine, proline, cysteine, asparagine, and glutamine.The peptide chains may optionally contain further amino acids. In embodiments, atmost 50%, preferably at most 40%, more preferably at most 30%, even morepreferably at most 20%, even more preferably at most 10%, even more preferably atmost 5%, even more preferably at most 2%, particularly preferably at most 1%, of theamino acids in the peptide chains are such further amino acids. In embodiments, thepeptide chains do not contain any such further amino acids. Preferably, such furtheramino acids are amino acids other than proteinogenic amino acids. Preferably, suchfurther amino acids are selected from fluorine-containing amino acids, hydroxy group-containing amino acids other than proteinogenic amino acids, boronic acid-containingamino acids, anthracenyl-containing amino acids, amino acids having C2-C10 alkylgroups other than proteinogenic amino acids, amino acids having C2-C10 alkenylgroups, and amino acids having C2-C10 alkynyl groups. Preferably, such furtheramino acids are selected from azidohomoalanine, acridinylalanine, phenylselenocysteine, sulfoserine, p-iodophenylalanine, bipyridylalanine, dansylalanine, o-nitrobenzyl cysteine, 7-nitroindolinyl-amino acids, propargylglycine, azidonorleucine, 5-bromotryptophan, L-4’-deoxy-4’-iodophenylalanine, tetrazine alanine, dipyridyl tetrazine serine, hydroxyproline, beta-alanine, citrulline, ornithine,norleucine, 3-nitrotyrosine, nitroarginine, pyroglutamic acid, and methionine sulfoxide.Preferably, such further amino acids are selected from azidohomoalanine,acridinylalanine, phenylselenocysteine, sulfoserine, p-iodophenylalanine, bipyridylalanine, dansylalanine, o-nitrobenzyl cysteine, 7-nitroindolinyl-amino acids, propargylglycine, azidonorleucine, 5-bromotryptophan, L-4’-deoxy-4’- iodophenylalanine, tetrazine alanine, dipyridyl tetrazine serine, hydroxyproline, beta- alanine, citrulline, ornithine, norleucine, 3-nitrotyrosine, nitroarginine, and pyroglutamic acid. Preferably, the peptide chains (b) have at least 4 amino acids, more preferably at least 6 amino acids, even more preferably at least 8 amino acids, even morepreferably at least 10 amino acids, even more preferably at least 11 amino acids,particularly preferably at least 12 amino acids.Preferably, the peptide chains (b) have at most 200 amino acids, more preferably atmost 100 amino acids, even more preferably at most 50 amino acids, even morepreferably at most 30 amino acids, even more preferably at most 25 amino acids,particularly preferably at most 20 amino acids.Also preferably, the peptide chains (b) have at most 30 amino acids, more preferably at most 25 amino acids, even more preferably at most 20 amino acids, even morepreferably at most 15 amino acids, even more preferably at most 12 amino acids,particularly preferably at most 11 amino acids.In preferred embodiments, the peptide chains (b) have from 4 to 200 amino acids,more preferably from 6 to 100 amino acids, even more preferably from 8 to 50 aminoacids, even more preferably from 10 to 30 amino acids, even more preferably from 11to 25 amino acids, particularly preferably from 12 to 20 amino acids.In preferred embodiments, the peptide chains (b) have from 4 to 30 amino acids, more preferably from 6 to 25 amino acids, even more preferably from 8 to 20 amino acids, even more preferably from 10 to 15 amino acids, even more preferably from 11 to 12 amino acids.In more preferred embodiments, the peptide chains (b) have from 4 to 15 aminoacids, more preferably from 5 to 13 amino acids, even more preferably from 6 to 12amino acids.In particularly preferred embodiments, the peptide chains (b) have from 8 to 15 aminoacids, more preferably from 10 to 13 amino acids, even more preferably from 11 to 12 amino acids. In particularly preferred embodiments, the peptide chains (b) have from 4 to 10 amino acids, more preferably from 5 to 8 amino acids, even more preferably from 6 to 7 amino acids.In embodiments, the peptide chains (b) have from 3 to 5000, preferably from 3 to4000, more preferably from 4 to 3000, more preferably from 5 to 2000, morepreferably from 5 to 1000, even more preferably from 6 to 500, even more preferablyfrom 6 to 100, particularly preferably from 7 to 50 amino acids.In embodiments, the peptide chains (b) have from 3 to 100, preferably from 3 to 50,more preferably from 4 to 30, even more preferably from 5 to 20, particularlypreferably from 6 to 15 amino acids.In embodiments, the peptide chains (b) have from 100 to 5000, preferably from 200to 4000, more preferably from 300 to 3000, even more preferably from 400 to 2000,particularly preferably from 500 to 1000 amino acids.Preferably, the peptide chains (b) have a weight average molecular weight of from 150 to 3000 g / mol, more preferably from 300 to 2500 g / mol, even more preferablyfrom 400 to 2000 g / mol, particularly preferably from 500 to 1500 g / mol.Preferably, the peptide chains (b) have a weight average molecular weight of from 600 to 3000 g / mol, more preferably from 800 to 2500 g / mol, even more preferably from 1000 to 2000 g / mol, particularly preferably from 1200 to 1500 g / mol. Preferably, the peptide chains (b) have a weight average molecular weight of from 150 to 1000 g / mol, more preferably from 300 to 900 g / mol, even more preferably from 400 to 800 g / mol, particularly preferably from 500 to 750 g / mol. Preferably, the peptide chains (b) have a molecular weight of from 150 to 3000 g / mol, more preferably from 300 to 2500 g / mol, even more preferably from 400 to 2000g / mol, particularly preferably from 500 to 1500 g / mol.Preferably, the peptide chains (b) have a molecular weight of from 600 to 3000 g / mol, more preferably from 800 to 2500 g / mol, even more preferably from 1000 to 2000 g / mol, particularly preferably from 1200 to 1500 g / mol. Preferably, the peptide chains (b) have a molecular weight of from 150 to 1000 g / mol, more preferably from 300 to 900 g / mol, even more preferably from 400 to 800 g / mol, particularly preferably from 500 to 750 g / mol.In preferred embodiments, the peptide chains (b) have a weight average molecularweight of from 150 to 600000 g / mol, preferably from 200 to 400000 g / mol, more preferably from 300 to 300000 g / mol, more preferably from 400 to 200000 g / mol, more preferably from 500 to 100000 g / mol, even more preferably from 600 to 50000g / mol, even more preferably from 700 to 10000 g / mol, particularly preferably from750 to 5000 g / mol, for example from 800 to 1500 g / mol. In preferred embodiments, the peptide chains (b) have a weight average molecular weight of from 150 to 10000 g / mol, preferably from 300 to 5000 g / mol, more preferably from 500 to 4000 g / mol, even more preferably from 600 to 3000 g / mol, particularly preferably from 700 to 2000 g / mol, for example from 800 to 1500 g / mol. In preferred embodiments, the peptide chains (b) have a weight average molecular weight of from 10000 to 600000 g / mol, preferably from 20000 to 400000 g / mol, more preferably from 30000 to 300000 g / mol, even more preferably from 40000 to 200000 g / mol, particularly preferably from 50000 to 100000 g / mol. In preferred embodiments, the peptide chains (b) have a molecular weight of from 150 to 600000 g / mol, preferably from 200 to 400000 g / mol, more preferably from 300 to 300000 g / mol, more preferably from 400 to 200000 g / mol, more preferably from 500 to 100000 g / mol, even more preferably from 600 to 50000 g / mol, even more preferably from 700 to 10000 g / mol, particularly preferably from 750 to 5000 g / mol, for example from 800 to 1500 g / mol. In preferred embodiments, the peptide chains (b) have a molecular weight of from 150 to 10000 g / mol, preferably from 300 to 5000 g / mol, more preferably from 500 to 4000 g / mol, even more preferably from 600 to 3000 g / mol, particularly preferably from 700 to 2000 g / mol, for example from 800 to 1500 g / mol. In preferred embodiments, the peptide chains (b) have a molecular weight of from 10000 to 600000 g / mol, preferably from 20000 to 400000 g / mol, more preferably from 30000 to 300000 g / mol, even more preferably from 40000 to 200000 g / mol, particularly preferably from 50000 to 100000 g / mol. The peptide used in the present invention preferably is a tripeptide, oligopeptide, polypeptide or protein. A person skilled in the art knows what peptides and proteins are. The peptide may also be a hydrolyzed protein. A person skilled in the art knows what a hydrolyzed protein, also referred to as protein hydrolysate, is. A hydrolyzed protein may be obtained by hydrolysis of a protein into peptides and amino acids. Such hydrolysis may be a chemical hydrolysis or an enzymatic hydrolysis. Enzymatic hydrolysis is preferred because it allows for a controlled hydrolysis by targeting specific peptide bonds.The peptides used in the present invention may be commercially available, or theymay be described in the literature, or they may be produced biotechnologically, orthey may be prepared according to methods known in the art. For example, thepeptides used in the present invention may be prepared by solid phase peptidesynthesis or by solution phase peptide synthesis. In general, peptides are preparedfrom the corresponding amino acids using known techniques (e.g. carboxylic acid activation, coupling reagents) and protecting group strategies. In one preferred embodiment, the peptide chains are of synthetic origin. In one preferred embodiment, the peptide chains are of natural origin. The peptide chains may, for example, be of plant origin, animal origin or human origin, or they may, for example, be viral peptides, proteins or fragments thereof or bacterial peptides, proteins or fragments thereof. In one preferred embodiment, the peptide chains are of plant origin.A person skilled in the art knows how to couple peptides to polysaccharides. Inpreferred embodiments, the peptide chains (b) are linked to the polysaccharidepolymer (a) through a linker. Any linker can be used.In a preferred embodiment, the linker results from the incorporation of a compound having at least two electrophilic functional groups. Preferably, the compound having at least two electrophilic functional groups has from 1 to 20 carbon atoms and from 0 to 10 heteroatoms, more preferably from 2 to 12carbon atoms and from 1 to 7 heteroatoms, even more preferably from 3 to 9 carbonatoms and from 2 to 5 heteroatoms, particularly preferably from 4 to 7 carbon atoms and from 3 to 4 heteroatoms. Preferably, the at least two electrophilic functional groups are selected from epoxy groups, C=C double bonds, carbonyl groups, C=C double bonds substituted with at least one carbonyl group, and mixtures thereof. Preferably, the compound having at least two electrophilic functional groups isselected from glycidyl methacrylate, maleimide, and mixtures thereof. Particularlypreferably, the compound having at least two electrophilic functional groups is glycidyl methacrylate. In one embodiment, the linker does not result from the incorporation of glycidyl methacrylate. In preferred embodiments, the linker contains a methacrylate moiety, acrylate moiety,maleimide moiety, norbornene moiety, N-hydroxysuccinimide moiety, hydrazonemoiety, carbonate moiety, disulfide moiety, disulfide carbamate moiety,dibenzocyclooctyne moiety or dibenzocyclooctyne-amine moiety.In more preferred embodiments, the linker contains a methacrylate moiety, acrylatemoiety, maleimide moiety, norbornene moiety, N-hydroxysuccinimide moiety, ordibenzocyclooctyne moiety.In preferred embodiments, the linker is a methacrylate, acrylate, maleimide,norbornene, N-hydroxysuccinimide, hydrazone, carbonate, disulfide, disulfidecarbamate, dibenzocyclooctyne or dibenzocyclooctyne-amine.In more preferred embodiments, the linker is a methacrylate, acrylate, maleimide,norbornene, N-hydroxysuccinimide, or dibenzocyclooctyne.In one embodiment, the peptide chains (b) are linked to the polysaccharide polymer(a) through synthetic chemical groups that form chemical bonds with primary amines. Examples of such groups are isothiocyanates, isocyanates, acyl azides, N-hydroxysuccinimide esters, sulfo-N-hydroxysuccinimide esters, disuccinimidylsuberate, bis(sulfosuccinimidyl)suberate, sulfonyl chlorides, aldehydes, glyoxals, epoxides, oxiranes, carbonates, aryl halides, imidoesters, carbodiimides, anhydrides, or fluorophenyl esters.In one embodiment, the peptide chains (b) are linked to the polysaccharide polymer(a) through a coupling reagent or a catalyst. The coupling reagent can be used with or without additives. Any coupling reagent, additive, or catalyst can be used. In oneembodiment, the additive is N-Hydroxybenzotriazole or a derivative thereof, forexample, ethyl 2-cyano-2-(hydroximino)acetate. In one embodiment, the additive is 4-(N,N-dimethylamino)pyridine.In one embodiment, the peptide chains (b) are linked to the polysaccharide polymer(a) using a group of organic compounds with the general formula RN=C=NR, whereR can be any organic group. In one embodiment, the peptide chains (b) are linked tothe polysaccharide polymer (a) via carbodiimide-mediated amide bond formation.Examples of carbodiimides are diisopropylcarbodiimide or N-(3-dimethylaminopropyl)-N’-ethylcarbodiimide · HCl. In one embodiment, the hybrid polymer of the invention comprises (a) a polysaccharide polymer and (b) peptide chains as defined herein and (c) optionally a linker. Preferably, the combined amount of (a) the polysaccharide polymer and (b)the peptide chains and (c) optionally the linker in the hybrid polymer is at least 50 wt-%, more preferably at least 60 wt-%, more preferably at least 70 wt-%, more preferably at least 75 wt-%, more preferably at least 80 wt-%, more preferably at least 85 wt-%, even more preferably at least 90 wt-%, even more preferably at least 95 wt-%, even more preferably at least 97 wt-%, even more preferably at least 98 wt- %, particularly preferably at least 99 wt-%, based on the total weight of the hybrid polymer. In one embodiment, the hybrid polymer of the invention comprises (a) a polysaccharide polymer and (b) peptide chains as defined herein and (c) a linker. Preferably, the combined amount of (a) the polysaccharide polymer and (b) thepeptide chains and (c) the linker in the hybrid polymer is at least 50 wt-%, morepreferably at least 60 wt-%, more preferably at least 70 wt-%, more preferably at least 75 wt-%, more preferably at least 80 wt-%, more preferably at least 85 wt-%, even more preferably at least 90 wt-%, even more preferably at least 95 wt-%, even more preferably at least 97 wt-%, even more preferably at least 98 wt-%, particularly preferably at least 99 wt-%, based on the total weight of the hybrid polymer.In preferred embodiments, from 1 to 100%, preferably from 3 to 50%, morepreferably from 5 to 40%, even more preferably from 8 to 30%, particularly preferablyfrom 10 to 25%, of the monosaccharide units of the polysaccharide polymer (a) aremodified with the peptide chains (b), optionally through a linker. In preferredembodiments, from 0.5 to 30%, preferably from 1 to 25%, more preferably from 2 to20%, even more preferably from 4 to 15%, particularly preferably from 5 to 10%, ofthe monosaccharide units of the polysaccharide polymer (a) are modified with the peptide chains (b), optionally through a linker. Modification of the monosaccharideunits / the polysaccharide polymer typically occurs via modifiable groups of themonosaccharide units / the polysaccharide polymer. Preferably, a modifiable group is a hydroxy group. A modifiable group may, for example, also be an amino group. In the case of dextran, the monosaccharide unit is a glucose unit, and the modifiablegroup is a hydroxy group. Preferably, a modifiable group is a carboxy group.In preferred embodiments, the peptide chains (b) are linked to the polysaccharidepolymer (a), optionally through a linker, via the N-terminal amino acid or the C-terminal amino acid of the peptide chains (b). In preferred embodiments, the peptidechains (b) are linked to the polysaccharide polymer (a), optionally through a linker,via the N-terminal amino acid of the peptide chains (b). In preferred embodiments,the peptide chains (b) are linked to the polysaccharide polymer (a), optionally througha linker, via the C-terminal amino acid of the peptide chains (b).Any amino acid can be used as the N-terminal amino acid or the C-terminal amino acid of the peptide chains. In one embodiment, the N-terminal amino acid or the C- terminal amino acid of the peptide chains is cysteine. In one embodiment, the N- terminal amino acid of the peptide chains is cysteine. In one embodiment, the C- terminal amino acid of the peptide chains is cysteine. In one embodiment, the C-terminal amino acid of the peptide chains is selected from leucine, isoleucine, phenylalanine, valine, tyrosine, tryptophan, glycine, alanine,proline, methionine, serine, and asparagine. In one embodiment, the C-terminalamino acid of the peptide chains is selected from leucine, isoleucine, phenylalanine,valine, tyrosine, tryptophan, glycine, alanine, proline, and methionine. In one embodiment, the C-terminal amino acid of the peptide chains is selected frommethionine, serine, and asparagine. In one embodiment, the C-terminal amino acid ofthe peptide chains is selected from serine and asparagine. In one embodiment, theC-terminal amino acid of the peptide chains is methionine.The N-terminal amino acid of the peptide chains may optionally be capped, forexample, it may optionally be acetylated. The N-terminal amino acid of the peptidechains may optionally be protected with a protecting group, for example afluorenylmethoxycarbonyl (Fmoc) group. The N-terminal amino acid of the peptidechains may optionally be capped, for example, with a C3-C6 alkyl group. The C-terminal amino acid of the peptide chains may optionally be capped, for example, itmay optionally be amidated. The present invention also relates to a blend comprising(a) from 1 to 99 wt-%, preferably from 20 to 80 wt-%, more preferably from 30 to 70wt-%, even more preferably from 40 to 65 wt-%, particularly preferably from 50to 60 wt-%, of a hybrid polymer of the present invention, based on the totalweight of the blend; and(b) from 1 to 99 wt-%, preferably from 20 to 80 wt-%, more preferably from 30 to 70wt-%, even more preferably from 35 to 60 wt-%, particularly preferably from 40to 50 wt-%, of one or more polysaccharide polymers and / or one or morepeptides, based on the total weight of the blend. Preferred hybrid polymers are described further above. In a preferred embodiment, the blend of the invention comprises(a) from 1 to 99 wt-%, preferably from 20 to 80 wt-%, more preferably from 30 to 70wt-%, even more preferably from 40 to 65 wt-%, particularly preferably from 50to 60 wt-%, of a hybrid polymer of the present invention, based on the totalweight of the blend; and(b) from 1 to 99 wt-%, preferably from 20 to 80 wt-%, more preferably from 30 to 70wt-%, even more preferably from 35 to 60 wt-%, particularly preferably from 40to 50 wt-%, of one or more polysaccharide polymers, based on the total weightof the blend.Preferred polysaccharide polymers are described further above.Preferably, the polysaccharide polymer is selected from dextran, dextrin, hyaluronic acid, chitosan, xanthan gum, fenugreek gum, tara gum, locust bean gum, carrageenan, guar gum, alginate, agar, agarose, starch, amylose, amylopectin, tragacanth gum, tamarind kernel gum, arabica gum, cherry gum, karaya gum, okra gum, cassia gum, chicle gum, konjac gum, ghatti gum, pectin, sclerotium gum, gellangum, paramylon, paramylum, curdlan, cellulose, diutan gum, inulin, derivativesthereof and mixtures thereof.More preferably, the polysaccharide polymer is selected from dextran, dextrin, hyaluronic acid, xanthan gum, tara gum, locust bean gum, carrageenan, guar gum, alginate, starch, amylose, amylopectin, tamarind kernel gum, arabica gum, karaya gum, konjac gum, pectin, sclerotium gum, gellan gum, diutan gum, inulin, derivativesthereof and mixtures thereof. More preferably, the polysaccharide polymer is selectedfrom dextran, dextrin, xanthan gum, tara gum, locust bean gum, carrageenan, guar gum, alginate, starch, amylose, amylopectin, tamarind kernel gum, arabica gum, karaya gum, konjac gum, pectin, sclerotium gum, gellan gum, diutan gum, inulin,derivatives thereof and mixtures thereof.Even more preferably, the polysaccharide polymer is selected from dextran, dextrin, hyaluronic acid, xanthan gum, tara gum, locust bean gum, carrageenan, guar gum, starch, amylose, amylopectin, konjac gum, inulin, derivatives thereof and mixturesthereof. Even more preferably, the polysaccharide polymer is selected from dextran,dextrin, xanthan gum, tara gum, locust bean gum, carrageenan, guar gum, starch, amylose, amylopectin, konjac gum, inulin, derivatives thereof and mixtures thereof. Particularly preferably, the polysaccharide polymer is xanthan gum. In a preferred embodiment, the blend of the invention comprises(a) from 1 to 99 wt-%, preferably from 20 to 80 wt-%, more preferably from 30 to 70wt-%, even more preferably from 40 to 65 wt-%, particularly preferably from 50to 60 wt-%, of a hybrid polymer of the present invention, based on the totalweight of the blend; and(b) from 1 to 99 wt-%, preferably from 20 to 80 wt-%, more preferably from 30 to 70wt-%, even more preferably from 35 to 60 wt-%, particularly preferably from 40to 50 wt-%, of one or more peptides, based on the total weight of the blend.Preferred peptides are described further above.The present invention also relates to the use of a hybrid polymer of the presentinvention or a blend of the present invention as a rheology modifying agent. In apreferred embodiment, the rheology modifying agent is a thickening agent. Preferably, the hybrid polymer of the present invention or the blend of the presentinvention is used as a rheology modifying agent in a cosmetic formulation. In apreferred embodiment, the cosmetic formulation is a skin care formulation or a haircare formulation. More preferably, the hybrid polymer of the present invention or theblend of the present invention is used as a rheology modifying agent in a skin care formulation or a hair care formulation. Particularly preferably, the hybrid polymer of the present invention or the blend of the present invention is used as a rheologymodifying agent in a skin care formulation. Also particularly preferably, the hybridpolymer of the present invention or the blend of the present invention is used as a rheology modifying agent in a hair care formulation. Preferably, the hybrid polymer of the present invention or the blend of the present invention is used as a thickening agent in a cosmetic formulation. In a preferred embodiment, the cosmetic formulation is a skin care formulation or a hair careformulation. More preferably, the hybrid polymer of the present invention or the blendof the present invention is used as a thickening agent in a skin care formulation or a hair care formulation. Particularly preferably, the hybrid polymer of the present invention or the blend of the present invention is used as a thickening agent in a skin care formulation. Also particularly preferably, the hybrid polymer of the present invention or the blend of the present invention is used as a thickening agent in a hair care formulation. The present invention also relates to a hydrogel comprising a hybrid polymer of thepresent invention or a blend of the present invention, water, optionally a pH adjustingagent, and optionally an ionic strength adjusting agent. In one embodiment, the hydrogel comprises a hybrid polymer of the present invention or a blend of the present invention, water, and a pH adjusting agent or an ionic strength adjusting agent. In one embodiment, the hydrogel comprises a hybrid polymer of the present inventionor a blend of the present invention, water, and a pH adjusting agent.In one embodiment, the hydrogel comprises a hybrid polymer of the present invention or a blend of the present invention, water, and an ionic strength adjusting agent. In one embodiment, the hydrogel comprises a hybrid polymer of the present invention or a blend of the present invention, water, a pH adjusting agent, and an ionic strength adjusting agent. Preferred hybrid polymers are described further above.In preferred embodiments, the hydrogel comprises from 0.1 to 10 wt-%, preferablyfrom 0.2 to 5 wt-%, more preferably from 0.3 to 3 wt-%, even more preferably from0.4 to 2 wt-%, particularly preferably from 0.5 to 1 wt-%, of the hybrid polymer or theblend, based on the total weight of the hydrogel.Preferably, the hydrogel comprises a pH adjusting agent. The pH adjusting agentmay, for example, be an acid, a base, a buffer, or combinations thereof. Examples ofpreferred acids are hydrochloric acid, acetic acid, trifluoroacetic acid, citric acid,formic acid, vitamin C, or combinations thereof. Examples of preferred bases aresodium hydroxide, potassium hydroxide, sodium carbonate, potassium carbonate,sodium bicarbonate (sodium hydrogencarbonate), potassium bicarbonate (potassiumhydrogencarbonate), or combinations thereof. Examples of preferred buffers arephosphate buffer, citrate buffer, acetate buffer, or combinations thereof. A particularly preferred pH adjusting agent is a buffer. A particularly preferred bufferis a phosphate buffer. A particularly preferred pH adjusting agent is a phosphatebuffer. Optionally, the hydrogel comprises an ionic strength adjusting agent. The ionic strength adjusting agent may, for example, be a salt. Examples of preferred salts aresodium chloride, potassium chloride, or combinations thereof. A particularly preferredionic strength adjusting agent is sodium chloride.Preferably, the hydrogel has a pH of from 3 to 9, more preferably from 4 to 8.5, evenmore preferably from 5 to 8, particularly preferably from 5.5 to 7.5.In preferred embodiments, the hydrogel further comprises an active ingredient. Preferably, the active ingredient is selected from vitamins, moisturizing agents, anti-aging agents, anti-wrinkle agents, anti-inflammatory agents, amino acids, peptides,and mixtures thereof. More preferably, the active ingredient is selected from vitamins,moisturizing agents, anti-aging agents, anti-wrinkle agents, anti-inflammatory agents, and mixtures thereof.The present invention also relates to a formulation comprising(a) from 0.1 to 10 wt-%, preferably from 0.2 to 5 wt-%, more preferably from 0.3 to3 wt-%, even more preferably from 0.4 to 2 wt-%, particularly preferably from0.5 to 1 wt-%, of a hybrid polymer of the present invention or a blend of thepresent invention, based on the total weight of the formulation; and(b) from 90 to 99.9 wt-%, preferably from 95 to 99.8 wt-%, more preferably from 97to 99.7 wt-%, even more preferably from 98 to 99.6 wt-%, particularly preferablyfrom 99 to 99.5 wt-%, of one or more further components, based on the totalweight of the formulation.In a preferred embodiment, the formulation is a cosmetic formulation, preferably askin care formulation or a hair care formulation. In one preferred embodiment, theformulation is a skin care formulation. In another preferred embodiment, theformulation is a hair care formulation.In preferred embodiments, the formulation is selected from the group consisting of shampoo, body wash, facial cleanser, face mask, bubble bath, intimate wash, bath oil, cleansing milk, micellar water, make-up remover, cleansing wipes, hair mask, perfume, liquid soap, shaving soap, shaving foam, cleansing foam, day cream, anti- aging cream, body milk, body lotion, body mousse, face serum, eye cream, sunscreen lotion, sun cream, face cream, after-shave lotion, pre-shaving cream, depilatory cream, skin-whitening gel, self-tanning cream, anti-acne gel, mascara, foundation, primer, concealer, blush, bronzer, blemish balm (bb) cream, eyeliner, night cream, eye brow gel, highlighter, lip stain, hand sanitizer, hair oil, nail varnish remover, skin conditioner, hair conditioner, hair styling gel, hair styling cream, anti- frizz serum, scalp treatment, hair colorant, split end fluid, deodorant, antiperspirant, baby cream, insect repellent, hand cream, sunscreen gel, foot cream, exfoliator, body scrub, cellulite treatment, bar soap, cuticle cream, lip balm, hair treatment, eye shadow, bath additive, body mist, eau de toilette, mouthwash, toothpaste, lubricating gel, moisturizer, serum, toner, aqua sorbet, cream gel, styling mousse, dry shampoo, lip stick, lip gloss, body oil, shower milk, illuminator, lip crayon, hair spray, combing cream, and sunblock. In more preferred embodiments, the formulation is selected from the group consisting of body wash, facial cleanser, face mask, bubble bath, intimate wash, bath oil, cleansing milk, micellar water, make-up remover, cleansing wipes, perfume, liquid soap, shaving soap, shaving foam, cleansing foam, day cream, anti-aging cream, body milk, body lotion, body mousse, face serum, eye cream, sunscreen lotion, sun cream, face cream, after-shave lotion, pre-shaving cream, depilatory cream, skin- whitening gel, self-tanning cream, anti-acne gel, mascara, foundation, primer, concealer, blush, bronzer, blemish balm (bb) cream, eyeliner, night cream, eye brow gel, highlighter, lip stain, hand sanitizer, nail varnish remover, skin conditioner, scalp treatment, deodorant, antiperspirant, baby cream, insect repellent, hand cream, sunscreen gel, foot cream, exfoliator, body scrub, cellulite treatment, bar soap, cuticle cream, lip balm, eye shadow, bath additive, body mist, eau de toilette, mouthwash, toothpaste, lubricating gel, moisturizer, serum, toner, aqua sorbet, cream gel, lip stick, lip gloss, body oil, shower milk, illuminator, lip crayon, and sunblock. In even more preferred embodiments, the formulation is selected from the group consisting of body wash, facial cleanser, face mask, intimate wash, cleansing milk, micellar water, make-up remover, cleansing wipes, liquid soap, shaving soap, shaving foam, cleansing foam, day cream, anti-aging cream, body milk, body lotion, body mousse, face serum, eye cream, sunscreen lotion, sun cream, face cream, after-shave lotion, pre-shaving cream, depilatory cream, skin-whitening gel, self- tanning cream, mascara, foundation, primer, concealer, blush, bronzer, blemish balm (bb) cream, night cream, highlighter, lip stain, hand sanitizer, nail varnish remover, skin conditioner, deodorant, antiperspirant, baby cream, insect repellent, hand cream, sunscreen gel, foot cream, exfoliator, body scrub, cellulite treatment, cuticle cream, lip balm, lubricating gel, moisturizer, toner, cream gel, lip stick, lip gloss, body oil, shower milk, illuminator, lip crayon, and sunblock.The following examples are intended to illustrate the subject-matter of the presentinvention without restricting it thereto. ExamplesP1 (CGYRGISLANWM, SEQ ID NO: 21), P2 (CGYRGITLANWM, SEQ ID NO: 23),P3 (CGYLGIS, SEQ ID NO: 15) and P4 (CGISLAN, SEQ ID NO: 16) refer to peptidesand were synthesized according to methods known in the art. All used amino acidsare L-amino acids.If not stated otherwise, RT refers to room temperature (20 – 25°C).1 Synthesis1.1 Dextran-methacrylate (1a, 1b,1c, 2) and Tara gum-methacrylate: Glycidylmethacrylate (GMA, 3) functionalization of dextran (4, 5) and Tara gum.In a typical reaction, dextran (15 g, molecular weight (MW) 40,000 g / mol, 4), providedin a flask in nitrogen atmosphere, was dissolved by addition of dry dimethyl sulfoxide(DMSO, 90 mL) and stirred (approx.30min) until dissolution was complete. The mixturewas heated to 40°C under stirring in an oil bath to help with dissolution. 4-(Dimethylamino)pyridin (DMAP, 2.25g, 0.2eq, 6) was dissolved in dry DMSO (24mL)separately. Subsequently, GMA (4.65 mL, 0.4 eq, 3) was added to the DMAP (6)solution and the mixture was added to the dextran solution. The reaction was stirred20 h at 40°C. All steps were performed under nitrogen atmosphere. The reaction waspurified by dialysis (molecular weight cut-off (MWCO) 3.5 kDa) in deionized water for5 days including water exchange every 2-3 h on day one and twice a day the remainingtime. After lyophilization for 4 days, the product (1a) was obtained as white solid. Thequantification of GMA functionalization was conducted via 1H NMR (DMSO-d6). Thereaction resulted in the modification of ~21% glucose units in dextran with methacrylatefunctional groups. The described method was applied to dextran of various molecularweights, e.g., MW 40 kg / mol (4) and 150 kg / mol (5), resulting in their methacrylatedspecies, i.e., 1a, 1b, or 2, respectively. Variations of different molecular weights ofdextran and different degrees of methacrylation were achieved by varying the educts as summarized in Error! Reference source not found..Table 1: Overview of dextran GMA-functionalization syntheses.1a, 1b: Dextran-GMAfrom Dextran 40 kg / mol.2: Dextran-GMA from Dextran 150 kg / mol. GMA (3): glycidylmethacrylate. DMAP (6): 4-(Dimethylamino)pyridin. Dextran-Dextran DMSO GMADMAP Reaction Functionali- GMA (3) (6) zation rateam(g) V (mL) V (mL) m (g) Time (h) GMAb (%)1a 4 15 114 4.65 2.25 20 211b 4 1 10 0.31 0.15 20 132 5 1 10 0.31 0.15 20 19aanalyzed via 1H NMRb % of glucose repeating units modified with GMAAlternatively, dextran (100 mg, molecular weight (MW) 40,000 g / mol, 4), was dissolvedin 0.7 mL DMSO in nitrogen atmosphere and heated to 40 °C. After 1 h, 0.045g DMAP(6) was dissolved separately in 0.48 mL DMSO and 0.093 mL GMA (3) were added,the mixture was added to the dextran solution. The reactions was kept stirring for 24 hat 40 °C. The reaction was purified by dialysis (molecular weight cut-off (MWCO) 3.5kDa) in deionized water for 5 days including water exchange every 2-3 h on day oneand twice a day the remaining time. After lyophilization for 3 days, the product (1c) wasobtained as white solid. The quantification of GMA functionalization was conducted via1H NMR (DMSO-d6). The reaction resulted in the modification of ~60% glucose unitsin dextran with methacrylate functional groups. Tara gum: In a typical reaction, a polysaccharide (15 g), provided in a flask in nitrogen atmosphere, was dissolved by addition of dry dimethyl sulfoxide (DMSO, 90 mL) and stirred (approx. 30min). The mixture was heated to 40°C under stirring. 4- (Dimethylamino)pyridin (DMAP, 2.25 g) was dissolved in dry DMSO (24 mL) separately. Subsequently, GMA (4.7 or 2.3 mL, as indicated in Table A) was added tothe DMAP solution and the mixture was added to the polysaccharide solution. Thereaction was stirred 20 h at 40°C. All steps were performed under nitrogenatmosphere. The reaction was purified by dialysis (molecular weight cut-off (MWCO)3.5 kDa) in deionized water for 5 days including water exchange every 2-3 h on dayone and twice a day the remaining time. The dissolved product was lyophilized. The product was obtained as white solid. Table A: Synthesized GMA-functionalized polysaccharides (Tara Gum) GMA-functionalized Polysaccharide GMA, polysaccharide V (mL) Tara Gum-GMA 1 Tara Gum 4.7Tara Gum-GMA 2 Tara Gum 2.3 1.2 Peptide-dextran Hybrids, peptide-hyaluronic acid hybrids, and peptide-Tara gum hybridsGeneral synthesis description, exemplary for hybrid H1 on the basis of peptide P1(CGYRGISLANWM, C: Cysteine, G: Glycine, Y: Tyrosine, R: Arginine, I: Isoleucine, S: Serine, K: Lysine, A: Alanine, N: Asparagine, W: Tryptophane, M: Methionine): The GMA-functionalized dextran (1, 40kDa, 10 mg) was dissolved in 0.1% trifluoracetic acid (7, TFA) in water (MilliQ, 0.2mL) (A). Separately, tris-(2-carboxyethyl)-phosphin(8, TCEP, 2.4 mg) was dissolved in 0.1% TFA / H2O (0.7 mL) and added to the peptide(P1, 4.42 mg), the mixture (B) was incubated in a shaker for 30 min at roomtemperature. Solution B was then added to solution A and stirred overnight (18h) at 66°C in nitrogen atmosphere (shaker 1000rpm). The reaction was purified by ultrafiltration in 0.1% TFA / H2O using Vivaspin tubes (5x, MWCO 5kDa, PES) at 4000 rpm, 25°C. After lyophilization for 3 days, the hybrid (H1) was obtained as white powder.General synthesis description, exemplary for hybrids H2-H4 on the basis of peptidesP2, P3, and P4 (P2: CGYRGITLANWM; P3: CGYLGIS; P4: CGISLAN, C: Cysteine,G: Glycine, Y: Tyrosine, R: Arginine, I: Isoleucine, S: Serine, A: Alanine, N:Asparagine, W: Tryptophane, M: Methionine T: Threonine), respectivley: The GMA-functionalized backbone (dextran-methacrylate, 1c, 40kDa, 10 mg) was dissolved in0.1% trifluoracetic acid (7, TFA) in water (MilliQ, 0.2mL) (A). Separately, tris-(2- carboxyethyl)-phosphin (8, TCEP, 2.4 mg) was dissolved in 0.1% TFA / H2O (0.7 mL)and added to the respective peptide (P2, 4.24 mg; or P3, 2.18 mg; or P4, 2.07 mg),the mixture (B) was incubated in a shaker for 30 min at room temperature. Solution B was then added to solution A and stirred overnight (18h) at 66°C in nitrogen atmosphere (shaker 1000rpm). The reaction was purified by ultrafiltration in 0.1% TFA / H2O using Vivaspin tubes (5x, MWCO 5kDa, PES) at 4000 rpm, 25°C. In certain cases, to remove excessive TFA ions, the reaction was purified by ultrafiltration in 0.1% TFA / H2O and subsequently in MilliQ water (last two cycles) using Vivaspintubes (7x , MWCO 5kDa, PES) at 4000 rpm, 25°C. After lyophilization for 3 days, thehybrid (H2 from P2, H3 from P3, or H4 from P4) was obtained as white powder.General synthesis description, exemplary for hybrids H5-H7 on the basis of peptidesP2, P3, and P4 (P2: CGYRGITLANWM; P3: CGYLGIS; P4: CGISLAN, C: Cysteine,G: Glycine, Y: Tyrosine, R: Arginine, I: Isoleucine, S: Serine, K: Lysine, A: Alanine, N:Asparagine, W: Tryptophane, M: Methionine T: Threonine), respectivley: The GMA-functionalized backbone (hyaluronic acid-methacrylate, average degree of substitution 35%, average Mw 55000, purchased from Sigma Aldrich, 10 mg) was dissolved in 0.1% trifluoracetic acid (7, TFA) in water (MilliQ, 0.2mL) (A). Separately, tris-(2-carboxyethyl)-phosphin (8, TCEP, 2.4 mg) was dissolved in 0.1% TFA / H2O(0.7 mL) and added to the respective peptide (P2, 4.24 mg; or P3, 2.18 mg; or P4,2.07 mg), the mixture (B) was incubated in a shaker for 30 min at room temperature.Solution B was then added to solution A and stirred overnight (18h) at 66°C in nitrogen atmosphere (shaker 1000rpm). The reaction was purified by ultrafiltration in 0.1% TFA / H2O and MilliQ water (last two cycles) using Vivaspin tubes (7x, MWCO5kDa, PES) at 4000 rpm, 25°C. After lyophilization for 3 days, the hybrid (H5 fromP2, H6 from P3, or H7 from P4) was obtained as white powder.General synthesis description, exemplary for hybrid H8 on the basis of peptides P1,(CGYRGISLANWM, C: Cysteine, G: Glycine, Y: Tyrosine, R: Arginine, I: Isoleucine, S: Serine, A: Alanine, N: Asparagine, W: Tryptophane, M: Methionine): The GMA- functionalized dextran (1c, 40kDa, 5 mg) was dissolved in 0.1% trifluoracetic acid (7, TFA) in water (MilliQ, 0.2mL) (A). Separately, the respective peptide (P1, 2.21 mg) was dissolved in 0.1% TFA / H2O (0.7 mL) and added to solution A and stirred overnight (18h) at 66°C in nitrogen atmosphere (shaker 1000rpm). The reaction was purified by ultrafiltration in 0.1% TFA / H2O and MilliQ watrer (last two cycles) using Vivaspin tubes (7x, MWCO 5kDa, PES) at 4000 rpm, 25°C. After lyophilization for 3 days, the hybrid (H8) was obtained as white powder.General synthesis description, exemplary for hybrid H9 on the basis of peptides P1,(CGYRGISLANWM, C: Cysteine, G: Glycine, Y: Tyrosine, R: Arginine, I: Isoleucine, S: Serine, A: Alanine, N: Asparagine, W: Tryptophane, M: Methionine): The GMA- functionalized backbone (hyaluronic acid-methacrylate, average degree of substitution 35%, average Mw 55000, purchased from Sigma Aldrich, 5 mg) was dissolved in 0.1% trifluoracetic acid (7, TFA) in water (MilliQ, 0.2mL) (A). Separately, the respective peptide (P1, 2.21 mg) was dissolved in 0.1% TFA / H2O (0.7 mL) and added to solution A and stirred overnight (18h) at 66°C in nitrogen atmosphere (shaker 1000rpm). The reaction was purified by ultrafiltration in 0.1% TFA / H2O and MilliQ water (last two cycles) using Vivaspin tubes (7x, MWCO 5kDa, PES) at 4000 rpm, 25°C. After lyophilization for 3 days, the hybrid (H9) was obtained as white powder.General synthesis description, exemplary for hybrids H10 on the basis of peptidesP1, (CGYRGISLANWM, C: Cysteine, G: Glycine, Y: Tyrosine, R: Arginine, I: Isoleucine, S: Serine, A: Alanine, N: Asparagine, W: Tryptophane, M: Methionine): The GMA-functionalized backbone (Tara Gum-methacrylate, Tara Gum-GMA 2, 4.8 mg) was dissolved in 0.1% trifluoracetic acid (7, TFA) in water (MilliQ, 0.2mL) (A). Separately, the respective peptide (P1, 2.12 mg) was dissolved in 0.1% TFA / H2O (0.7 mL) and added to solution A and stirred overnight (18h) at 66°C in nitrogen atmosphere (shaker 1000rpm). The reaction was purified by ultrafiltration in 0.1% TFA / H2O and MilliQ water (last two cycles) using Vivaspin tubes (7x, MWCO 5kDa, PES) at 4000 rpm, 25°C. After lyophilization for 3 days, the hybrid (H10) was obtained as white powder.General synthesis description, exemplary for hybrids H11 on the basis of peptidesP2, (CGYRGITLANWM, C: Cysteine, G: Glycine, Y: Tyrosine, R: Arginine, I: Isoleucine, T: Threonine, A: Alanine, N: Asparagine, W: Tryptophane, M: Methionine): The GMA-functionalized backbone (hyaluronic acid-methacrlyate, average degree of substitution 35%, average Mw 55000, purchased from Sigma Aldrich, 5 mg) was dissolved in 0.1% trifluoracetic acid (7, TFA) in water (MilliQ, 0.2mL) (A). Separately, the respective peptide (P2, 2.21 mg) was dissolved in 0.1% TFA / H2O (0.7 mL) and added to solution A and stirred overnight (18h) at 66°C innitrogen atmosphere (shaker 1000rpm). The reaction was purified by ultrafiltration in0.1% TFA / H2O and MilliQ watrer (last two cycles) using Vivaspin tubes (7x, MWCO 5kDa, PES) at 4000 rpm, 25°C. After lyophilization for 3 days, the hybrid (H11) was obtained as white powder. 1.3 Hydrogel preparationa) Peptide-dextran hybrids, Peptide-hyaluronic acid hybrids, and peptide-Taragum hybridsi) Direct addition of buffer to hybrid (solid):The hydrogel was prepared by direct addition of the respective amount of buffer to thehybrid powder. For example, to obtain a 1wt% hydrogel, 30 µL of 100mM phosphatebuffer pH 7.4 (in the following referred to as pH 7) were added to 0.3 mg hybrid. Toobtain a 4wt% hydrogel, 30 µL of 100mM phosphate buffer pH 7.4 or pH 8 (in thefollowing referred to as pH 7) were added to 1.2 mg hybrid to yield a pH 7 hydrogel.Alternatively, the hybrid was dissolved in 15µL DPBS and 15µL 100mM PB pH 8 wereadded to adjust the pH to 7. To obtain a 1wt% hydrogel, 30 µL of 100mM acetate bufferpH 4.75 (in the following referred to as pH 5) were added to 0.3 mg hybrid. Gelation occurred upon gentle mixing.2 Methods / Characterizations2.1 NMR1H NMR was conducted to quantify functionalization rates of polysaccharides with GMA. DMSO-d6 was used for analysis. Spectra were recorded on Bruker 300 MHz or 400 MHz NMR spectrometers. 2.2 Rheology Rheological characterization of hydrogels and formulations was conducted using a DHR3 rheometer (TA Instruments) equipped with a temperature controller. Experiments were performed using a) 8 mm parallel-plate geometry with solvent reservoir to prevent hydrogel drying with hydrogels of 30 μL volume resulting in a gap size of ~ 0.50 mm, or b) 20 mm cone-plate geometry (2.007°) with solvent reservoir to prevent hydrogel drying. Characterization of the mechanical properties was performedat 20 °C or 25 °C. Several different measurement setups were performed: (i) Time sweep: The linear viscoelastic region was found to include the range of0.05 – 1% strain and 1 – 1.6 Hz frequency. Therefore, oscillatory time-sweepmeasurements were performed at a fixed strain and fixed frequency within this range at different temperatures and time intervals. (ii) Thixotropy measurement: Consecutive combined measurements of anoscillatory strain sweep (0.01 – 1000%) at 25°C with a fixed frequency of 1 Hz followedby an oscillatory time sweep measurement with a fixed strain of 0.1% and frequency of 1 Hz for 1000 s at 25 °C were conducted to analyze the self-healing capacity of the hydrogels. Notably, the healing efficiency of hydrogels was quantified from the storage modulus acquired from this experiment. In this context, the initial hydrogel recovery (first acquired data point, ~ 13 s) and the mean hydrogel recovery during the following oscillatory time sweep (0.1% strain, 800s) were analyzed for each strain sweep. (iii) Flow ramp: Continuous flow rheology experiment. Flow ramp from initial stress of 0 to up to 60 Pa over 180 s at 20 °C or 25 °C. Several experiments were performed using these experimental setups:- Examination of rheology modification or gelation- Investigation of peptide graft amino acid sequence effect on gel mechanicalproperties like stiffness (G’, G’’), crossover strain, thixotropy, recovery, flow- Investigation of pH effect on gel mechanical properties like stiffness, crossoverstrain, thixotropy, recovery (pH 5 – pH 7). In order to assess the effect of pHchanges on the hydrogel mechanical properties, hydrogels were prepared at either pH 5 using 100mM acetate buffer pH 4.75 or pH 7 using, e.g., 100mM phosphatebuffer pH 7.4 as described before (1.3ai) and rheological characterization was conducted.Two key parameters are of particular significance for the comprehensiveunderstanding of the material viscoelastic properties as they provide insights into stiffness and damping characteristics: i) Storage Modulus (G’): Measure of thestored energy in a material during deformation and reflection of the material’s elasticbehavior. A higher storage modulus indicates higher stiffness and lowerdeformability of the material. ii) Loss Modulus (G”): Measure of the dissipatedenergy, e.g., as heat during deformation and reflection of the material’s viscousbehavior. A higher loss modulus indicates more damping and energy dissipation bythe material.2.3 Molecular weightThe molecular weight of the polysaccharide polymer was determined using gel permeation chromatography (GPC). GPC experiments were performed using a PSS SECcurity2instrument consisting of a pump, autosampler and column oven. A column SUPREMA LIN XL (PSS Polymer Standards Service GmbH, Mainz, Germany) of 300 x 8 mm and 10 µm average particlesize was used at a flow rate of 1.0 mL / min and a column temperature of 25°C. Aseluent 0.1M NaNO3 was used. The samples having 1 mg / ml concentration were filtered prior to measurement through0.45 µm HA filter. The injection volume was 50 μL. Detection was accomplished withan RI detector. Data acquisition and evaluation were performed using PSS WINGPC UniChrom (PSS Polymer Standards Service GmbH, Mainz, Germany). Calibration was carried out by using dextran standards (molecular weight ranging from 298000 g / mol to 180 g / mol) (PSS Polymer Standards Service GmbH, Mainz, Germany). In general, calibration is carried out by using an appropriate standard. A person skilled in the art knows how to select an appropriate standard. In the experimental section of the present patent application, reference is made to “Dextran 40 kg / mol”, “dextran (… molecular weight (MW) 40,000 g / mol, 4)”, “dextran ... MW 40 kg / mol (4)”, “Dextran 4”, or variations thereof. This dextran is commercially available, and its packaging indicates a molecular weight of 40 kg / mol (determined by intrinsic viscosity). However, when the molecular weight of this dextran is determined according to the method described herein (chapter 2.3), i.e. using gel permeation chromatography (GPC) as described herein (chapter 2.3), the following results are obtained: Mn = 15099 g / mol, Mw = 33693 g / mol. In the experimental section of the present patent application, reference is made to “Dextran 150 kg / mol”, “dextran … MW 150 kg / mol (5)”, “Dextran 5”, or variations thereof. This dextran is commercially available, and its packaging indicates a molecular weight of 150 kg / mol (determined by intrinsic viscosity). However, when the molecular weight of this dextran is determined according to the method described herein (chapter 2.3), i.e. using gel permeation chromatography (GPC) as described herein (chapter 2.3), the following results are obtained: Mn = 20312 g / mol, Mw = 156959 g / mol. A bimodal distribution of molecular weight was observed. In the experimental section of the present patent application, reference is made to“Hyaluronic acid-methacrylate 55 kg / mol”, “55 kDa hyaluronic acid backbone”,“average degree of substitution 35%, average Mw 55000, purchased from SigmaAldrich”. This Hyaluronic acid-methacrylate is commercially available, and itspackaging indicates a molecular weight of average Mw 55000 Da.4 Results4.1 NMR (GMA functionalization and peptide conjugation)Dextran was functionalized with GMA to yield a biopolymer for further peptideconjugation. Analysis via 1H NMR with DMSO-d6 as solvent was used to determine the degree of GMA-modification of the polymer. The results are summarized in Table 1 and refer to the percentage of GMA-functionalized repeat units, i.e. glucose units. Calculations are based on the integrals of vinyl-signals of the GMA (approx.5.5-6.5 ppm) that was coupled to the biopolymer in relation to the integral of the proton signals of the glucose repeat units (approx.4-5 ppm).4.2 Rheology4.2.1 Peptide-dextran hybridsA) Adjustability of G’The peptide-dextran hybrid resulted in hydrogels that featured an adjustability of G‘ via the grafted peptide, the wt% of the peptide-dextran hybrid as well as the pH used. Thiswas demonstrated with P1, P2, or P4 peptide grafts on a polysaccharide, i.e., dextranbackbone yielding the hybrids H1, H2, H4, or H8.i) 40 kg / mol dextran backboneTable 8: Adjustability of mechanical properties of hydrogels in dependency of peptide sequence, wt% of hybrid as well as used pH / buffer system. Unlike the hybrids, theplain backbone 1 was not capable of hydrogel formation or rheology modification.Using the hybrids, G’ was adjustable in a broad range. n.d. = not determined. YP = Yield point. Preparation method and rheology measurement method are indicated for each data set with corresponding reference to chapters 1.3 (hydrogel preparation) and 2.2 (rheology). M1: 1.3ai, 2.2b (20mm cone plate), 2.2i, 0.05% strain, 10 rad / s, 25°C. M2: 1.3ai, 2.2b (20mm cone plate), 2.2iii, 0-20Pa stress in 180s, 25°C. M3: 1.3ai, 2.2b (20mm cone plate), 2.2i, 0.05% strain, 10 rad / s, 20°C. M4: 1.3ai, 2.2b (20mm cone plate), 2.2iii, 0-20Pa stress in 180s, 20°C. M5: 1.3ai, 2.2a (8mm parallel plate), 2.2i -0.05% strain, 1 Hz, 25°C. M6: 1.3ai, 2.2a (8mm parallel plate), 2.2i - 0.05% strain, 10rad / s, 25°C. M7: 1.3ai, 2.2a (8mm parallel plate), 2.2i - 0.05% strain, 10 rad / s, 25°C.M9: 1.3ai, 2.2a (8mm parallel plate), 2.2i - 0.1% strain, 1Hz, 25°C. M10: 1.3ai, 2.2a(8mm parallel plate), 2.2i - 0.3% strain, 1Hz, 25°C. M11: 1.3ai, 2.2a (8mm parallelplate), 2.2i - 0.1% strain, 1Hz, 25°C. *: Hybrids were washed twice more with waterduring the last step of purification according to the synthesis protocol reported above. Compound wt% pH G’ (Pa) G’’ (Pa) YP (Pa)1 1 7 2 M1 1M1 0 M2H1 1 7 38 M3 7 M3 0.5 M4H1 4 7 823 M5 204 M5 n.d.H1 4.3 7 1574 M6 394 M6 n.d.H1 1 5 183 M7 20 M7 n.d.H2 8 7 118M9 25 M9 n.d.H2 5 7 91M9 25 M9 n.d.H4 8 7 110M9 36 M9 n.d.H8 * 1 7 250 M10 90 M10 n.d.H8 * 4 7 105 M11 41 M11 n.d.B) Self-healing behavior of 4wt% and 1wt% peptide-dextran hybrid hydrogels,demonstrated with peptide grafts on 40 kg / mol dextran backbone (H1) in pH 7 and pH 5.Table 10: Shear-thinning behavior and regeneration properties of hydrogels independency of wt% of hybrid as well as used pH / buffer system. G’i gives the G’ before liquefying strain was applied at 0.1% strain. R.a and R.b describe G’ regeneration after 13s or 1000s after the liquefying strain was removed, respectively. CS = Crossoverstrain with gel to sol transition (G’ = G’’). G’1 - G’4 give G’ after a regeneration time of1000s in cycle 1-4, respectively. n.d. = not determined. n.a. = not applicable - note thathere the crossover with gel to sol transition occurs above the tested regime, whichcovers strains up to 1000% (at approx. 100% strain, G' reached low values (~ 1Pa)that are almost equal to G''). Preparation method and rheology measurement method are indicated for each data set with corresponding reference to chapters 1.3 (hydrogel preparation) and 2.2 (rheology). M8: 1.3ai, 2.2a (8mm parallel plate), 2.2ii, oscillatorystrain sweep 0.01 - 1000% strain, 1 Hz, 25°C, oscillatory time sweep 0.1% strain, 1Hz, 25°C. Compound Initial Cycle 1 Cycle 2G’i G’’i CS R.a R.b G’1 G’’1 CS R.a R.b G’2 G’’2 (Pa) (Pa) (%) (%) (%) (Pa) (Pa) (%) (%) (%) (Pa) (Pa) H1M8 1435 388 2 32 92 1327 285 2 38 80 1060 216H1M8 820 196 2 40 95 775 159 2 46 121 937 167H1M8 176 24 n.a. 12 103 182 29 4 n.d. n.d. n.d. n.d.Cycle 3 Cycle 4 pH wt%CS R.a R.b G’3 G’’3 CS R.a R.b G’4 G’’4 (%) (%) (%) (Pa) (Pa) (%) (%) (%) (Pa) (Pa) H1M8 2 49 99 1050 201 2 35 105 1100 171 7 4.3H1M8 3 34 93 872 159 2 29 91 791 133 7 4H1M8 n.d. n.d. n.d. n.d. n.d. n.d. n.d. n.d. n.d. n.d. 5 1The hybrid hydrogels from H1 showed regenerative behavior after mechanical stressat different wt% and pH.4.2.2 Peptide-hyaluronic acid hybridsA) Adjustability of G’The peptide-hyaluronic acid hybrid resulted in hydrogels. This was demonstrated withP1 or P2 peptide grafts on a polysaccharide, i.e., hyaluronic acid backbone, yieldingH5, H9 or H11.i) 55 kDa hyaluronic acid backboneTable B: Hydrogel formation of peptide-hyaluronic acid hybrids from peptides P1 or P2.Preparation method and rheology measurement method are indicated for each data set with corresponding reference to chapters 1.3 (hydrogel preparation) and 2.2(rheology). M9:1.3ai, 2.2a (8mm parallel plate), 2.2i - 0.1% strain, 1Hz, 25°C.M10: 1.3ai, 2.2a (8mm parallel plate), 2.2i - 0.3% strain, 1Hz, 25°C. *: Hybrids werewashed twice more with water during the last step of purification according to the synthesis protocol reported above. Compound wt% pH G’ (Pa) G’’ (Pa)H5* 3.4 7 20120M9 3095M9H5* 2 7 3145M9 533M9H9* 1 7 120 M10 50 M10H11* 4 7 296 M10 31 M10Table C: Shear-thinning behavior and regeneration properties of hydrogels in dependency of wt% of hybrid as well as used pH / buffer system. G’i gives the G’ before liquefying strain was applied at 0.1% strain. R.a and R.b describe G’ regeneration after 13s or 1000s at 0.3% strain after the liquefying strain was removed, respectively. CS= Crossover strain with gel to sol transition (G’ = G’’). G’1 gives G’ after a regenerationtime of 1000s in cycle 1. Preparation method and rheology measurement method are indicated for each data set with corresponding reference to chapters 1.3 (hydrogelpreparation) and 2.2 (rheology). M10: 1.3ai, 2.2a (8mm parallel plate), 2.2i - 0.3% strain, 1Hz, 25°C. *: Hybrids were washed twice more with water during the last step of purification according to the synthesis protocol reported above. Compound wt% pH Initial Cycle 1G’i G’’i CS R.a R.b G’1 G’’1 (Pa) (Pa) (%) (%) (%) (Pa) (Pa) H9*M10 1 7 152 47 16 12 99 151 83The hybrid hydrogel from H9 showed regenerative behavior after mechanical stress.Example Compositions The following Example Compositions comprise Hybrid H, which is the hybrid polymerof the present invention, in particular hybrid polymer H1 (as defined in Example 1.2).% as used herein refers to wt.-%, based on the total weight of the composition. Example Composition 1: After Sun Cream Gel Mineral Oil 3.00 %Isopropyl Palmitate 3.00 %Cetearyl Isononanoate 3.00 %Jojoba Oil 3.00 %Walnut Oil 3.00 %Tocopheryl Acetate 1.00 %Hybrid H 1.20 %Water ad 100 %Glycerin 3.00 %Allantoin (Clariant) 0.20 %Nipaguard®POM (Clariant) 1.00 % Phenoxyethanol, Methylparaben, Piroctone Olamine Panthenol 1.00 %Collagen nativ 1 % 3.00 %Ethanol 1.50 %Example Composition 2: Sun Milk SPF 15 Ethylhexyl Stearate 7.00 %Decyl Oleate 5.00 %Plantasens®Natural Emulsifier HE 20 (Clariant) 3.00 % Cetearyl Glucoside (and) Sorbitan Olivate Dimethicone 2.00 %Octocrylene 7.00 %Butyl Methoxydibenzoylmethane 2.50 %Ethylhexyl Salicylate 4.50 %Water Ad 100 % Glycerin 3.00 % Hybrid H 1.00 %Nipaguard®POM (Clariant) 1.00 % Phenoxyethanol (and) Piroctone Olamine (and) Methylparaben Citric Acid q.s.Example Composition 3: Liquid Soap Water Ad 100 %Glycerin 3.00 % 1,2-Propanediol 2.00 %Hybrid H 3.00 % Genapol®LRO liquid (Clariant) 20.00 % Sodium Laureth Sulfate Genagen®CAB 818 (Clariant) 4.00 % Cocamidopropyl Betaine GlucoTain®Clear (Clariant) 2.00 % Capryloyl / Caproyl Methyl Glucamide NipaguardTMDMDMH (Clariant) 0.40 % DMDM Hydantoin Fragrance 0.20 %Sodium Cloride 0.50 %Citric Acid 0.10 %Example Composition 4: Effect Shower Gel Genapol®LRO liquid (Clariant) 30.00 % Sodium Laureth Sulfate Genagen®CAB 818 (Clariant) 6.00 % Cocamidopropyl Betaine Hostapon®KCG (Clariant) 5.00 % Sodium Cocoyl Glutamate Water Ad 100 %Hybrid H 1.40 %Nipaguard®DMDMH (Clariant) 0.50 % DMDM Hydantoin Cirebelle 104 Blue 1.00% Synthetic Wax Example Composition 5: Facial Cleanser Water Ad 100 %Hybrid H 1.80 %Genapol®LRO paste (Clariant) 4.50 % Sodium Laureth Sulfate Medialan®LD (Clariant) 13.50 % Sodium Lauroyl Sarcosinate Genagen®CAB 818 (Clariant) 3.00 % Cocamidopropyl Betaine Citric Acid q.s.Benzoic Acid 0.50 % Example Composition 6: Mascara Hydroxyethylcellulose 0.50 %Hybrid H 0.50 %1,2-Propyleneglycol 1.00 %Magnesium Aluminium Silicate 1.00 %Triethanolamine 99% 1.50 %Water Ad 100 %Stearic Acid 3.00 %SilCare®Silicone 41M15 (Clariant) 1.00 % Caprylyl Methicone SilCare®Silicone 31M50 (Clariant) 2.00 % Caprylyl Trimethicone Tego® Care 4504.00 % Polyglyceryl-3 Methylglucose Distearate Polybutene. 2.00 %Beeswax 2.50 %Plantasens®Olive Wax S51 (Clariant) 2.50 % Hydrogenated Olive Oil Microcrystalline Wax 3.50 %Iron Oxides 10.0 %PhenonipTMME (Clariant) 1.00 % Phenoxyethanol, Methylparaben, Ethylparaben Baycusan®C 1004 2.00 % Polyurethane-35 Example Composition 7: BB Cream SPF 15 Water Ad 100 %Glycerin 2.00 % Hybrid H 1.00 %Hostaphat®KW 340 D (Clariant) 3.00 % Triceteareth-4 Phosphate Cetearyl Alcohol 2.00 % Octocrylene 7.00 %Butyl Methoxydibenzoylmethane 2.50 %Ethylhexyl Salicylate 4.50 %Plantasens®Olive LD (Clariant) 2.00 % Hydrogenated Ethylhexyl Olivate (and) Hydrogenated Olive Oil Unsaponifiables 12-15 Alkyl Benzoate 8.00 %Plantasens®Olive Squalane (Clariant) 2.00 % Squalane Plantasens®Shea Butter (Clariant) 1.00 % Butyrospermum Parkii (Shea) Butter XIAMETER®PMX-200 Silicone Fluid 200 CS 2.00 % Dimethicone Chroma-Lite®Black 0.05 % Mica (and) Bismuth Oxychloride (and) Iron Oxides Chroma-Lite®Red 0.20 % Mica (and) Bismuth Oxychloride (and) Iron Oxides Chroma-Lite®Yellow 0.60 % Mica (and) Bismuth Oxychloride (and) Iron Oxides Titanium Dioxide 5.00 %Butylene Glycol 4.00 %Plantasens®Natural Vitamin E (Clariant) 1.00 % Tocopherol Panthenol 0.50 %Gatuline®Age Defense 2 1.00 % Aqua (and) Juglans Regia (Walnut) Seed Extract Sodium Hyaluronate 0.40 %Orgasol®4000 EXD NAT COS Caresse 1.00 % Nylon-6 / 12 Fragrance 0.20 %Nipaguard®POB (Clariant) 0.80 % Phenoxyethanol (and) Piroctone Olamine (and) Benzoic Acid Citric Acid q.s.Example Composition 8: O / W Foundation Water Ad 100 %Hybrid H 1.00 %Magnesium Aluminium Silicate 1.00 %Plantasens®Natural Emulsifier HP10 (Clariant) 4.50 % Sucrose Polystearate, Cetearyl Alcohol, Olea Europaea (Olive) Oil Unsaponifiables SilCare®Silicone 31M50 (Clariant) 2.00 % Caprylyl Trimethicone XIAMETER®PMX-200 Silicone Fluid 100 CS 2.00 % Dimethicone Caprylic / Capric Triglyceride 5.00 %Plantasens®Olive Wax S51 (Clariant) 1.50 % Hydrogenated Vegetable Oil Chroma-Lite®Black 0.10 % Mica (and) Bismuth Oxychloride (and) Iron Oxides Chroma-Lite®Red 0.40 % Mica (and) Bismuth Oxychloride (and) Iron Oxides Chroma-Lite®Yellow 1.20 % Mica (and) Bismuth Oxychloride (and) Iron Oxides Titanium Dioxide 7.00 %Dicaprylyl Carbonate 4.00 %Butylene Glycol 3.00 % Plantasens®Natural Vitamin E (Clariant) 1.00 % Tocopherol Orgasol®4000 EXD NAT COS Caresse 1.00 % Nylon-6 / 12 Fragrance 0.20 %Nipaguard®POB (Clariant) 0.80 % Phenoxyethanol (and) Piroctone Olamine (and) Benzoic Acid Citric Acid q.s. Example Composition 9: Liquid Highlighter Water Ad 100 %Bentonite 1.00 %Hybrid H 1.00 %Liquiwax™ PolyIPL2.00 % Stearyl / PPG-3 Myristyl Ether Dimer Dilinoleate Plantasens®Olive Wax S51 (Clariant) 2.00 % Hydrogenated Olive Oil Stearic Acid 1.20 %Isostearic Acid 0.90 %Water 5.00 %Sodium Hydroxide 0.12 %Orgasol®4000 EXD NAT COS Caresse 1.50 % Nylon-6 / 12 Timiron®Super Gold 2.50 % Mica, Titanium Dioxide Xirona®Indian Summer 2.50 % Silica (and) Iron Oxides Panthenol 0.50 %Cyclopentasiloxane 7.50 %PhenonipTMME (Clariant) 1.00 % Phenoxyethanol, Methylparaben, Ethylparaben Tocopheryl Acetate 1.00 %Example Composition 10: Lipstain Water Ad 100 %Glycerin 30.00 %Hybrid H 3.00 %FD&C Red No.40 0.15 % CI16035 Emulsogen®HCO 040 (Clariant) 0.50 % PEG-40 Hydrogenated Castor Oil PhenonipTMME (Clariant) 1.00 % Phenoxyethanol, Methylparaben, Ethylparaben Flavour 0.20 %Example Composition 11: Eyeliner Gel Water Ad 100 %Glycerin 1.00 %Hybrid H 2.00 %PhenonipTMME (Clariant) 1.00 % Phenoxyethanol, Methylparaben, Ethylparaben PVP 1.50 %Water 10.00 %Timiron®Super Gold 12.00 % Mica, CI77891, Titanium Dioxide Example Composition 12: After Shave Balm Hostaphat® KL 340 D (Clariant) 2.00 % Trilaureth-4 Phosphate Octopirox® (Clariant) 0.05 % Piroctone Olamine Plantasens® Abyssinian Oil (Clariant) 2.00 % Crambe Abyssinica Seed Oil Isopropyl Isostearate 3.00 %Plantasens® Inca Inchi Serum (Clariant) 1.00 % Plukenetia Volubilis Seed Oil (and) Phytosterols (and) Olea Europaea (Olive) Oil Unsaponifiables (and) Beeswax Water Ad 100 %Polyglykol 400 (Clariant) 3.00 % PEG-8 Allantoin 0.30 %Hybrid H 1.50 % Dimethicone 1.00 %Citric Acid q.s.PhenonipTMME (Clariant) 1.00 % Phenoxyethanol, Methylparaben, Ethylparaben Example Composition 13: Sprayable Body Milk Hostaphat®KL 340 D (Clariant) 1.00 % Trilaureth-4 Phosphate Mineral Oil 8.00 %Isopropyl Palmitate 3.00 %Cetearyl Alcohol 0.50 %Caprylic / Capric Triglyceride 2.00 %Glyceryl Stearate 0.50 %SilCare®Silicone 41M15 (Clariant) 1.00 % Caprylyl Methicone Hybrid H 1.00 %Water ad 100 %Glycerin 5.00 %Ethanol 5.00 %Tocopheryl Acetate 1.00 %Nipaguard®POM (Clariant) 1.00 % Phenoxyethanol, Methylparaben, Piroctone Olamine Example Composition 14: Body Lotion for Men Caprylic / Capric Triglyceride 3.50 %Plantasens®Olive LD (Clariant) 3.00 % Hydrogenated Ethylhexyl Olivate (and) Hydrogenated Olive OilUnsaponifiables Myristyl Myristate 2.50 %Cetearyl Alcohol 2.00 %Octyldodecanol 1.00 %Glyceryl Stearate Citrate 1.50 %Hybrid H 1.20 %Water ad 100 %Glycerin 5.00 %Ethanol 3.00 %Tocopheryl Acetate 1.00 %Aloe Barbadensis Leaf Juice 1.00 %Nipaguard®POM (Clariant) 1.00 % Phenoxyethanol, Methylparaben, Piroctone Olamine Fragrance 0.20 %Sodium Hydroxide q.s.Example Composition 15: Anti-Aging Cream Gel Caprylic / Capric Triglyceride 5.00 %Dicaprylyl Ether 5.00 %Cetearyl Alcohol 2.00 %Nipaguard®POB (Clariant) 0.80 % Phenoxyethanol (and) Piroctone Olamine (and) Benzoic Acid Ubiquinone 0.10 %Aristoflex®HMB (Clariant) 0.40 % Ammonium Acryoyldimethyltaurate / Beheneth-25 Methacrylate Crosspolymer Hybrid H 0.40 %Sodium Hyaluronate 0.30 %Water Ad 100 %Tocopheryl Acetate 0.30 %Fragrance 0.30 % Example Composition 16: Light Day Cream Water Ad 100 %Hybrid H 0.75 %Glycerin 3.00 % Plantasens®Natural Emulsifier HE20 (Clariant) 1.20 % Cetearyl Glucoside, Sorbitan Olivate Aristoflex®AVC (Clariant) 0.10 % Ammonium Acryloyldimethyltaurate / VP Copolymer Plantasens®Abyssinian Oil (Clariant) 3.00 % Crambe Abyssinica Seed Oil Octyldodecanol 5.00 %Isodecyl Neopentanoate 3.00 %Plantasens®Natural Vitamin E (Clariant) 0.50 % Tocopherol Nipaguard®SCP (Clariant) 1.00 % Phenoxyethanol (and) Sorbitan Caprylate Fragrance 0.30 %Citric Acid q.s. Example Composition 17: Caring Night Cream Water Ad 100 %Glycerin 2.00 % Hybrid H 1.00 %Hostaphat®KW 340 D (Clariant) 2.00 % Triceteareth-4 Phosphate Plantasens®Oat Serum (Clariant) 3.00 % Avena Sativa (Oat) Kernel Oil (and) Phytosterols (and) Olea Europaea (Olive) Oil Unsaponifiables (and) Beeswax Plantasens®Shea Butter (Clariant) 7.00 % Butyrospermum Parkii (Shea) Butter Isopropyl Palmitate 5.00 %Macadamia Integrifolia Seed Oil 4.00 %Cera Alba (Beeswax) 3.00 %Nipaguard®SCP (Clariant) 1.00 % Phenoxyethanol (and) Sorbitan Caprylate Fragrance 0.30 %Sodium Hydroxide 0.10 %Example Composition 18: Sprayable Hair Styling Gel Hybrid H 0.90 %Water Ad 100 %Genapol®LA-230 (Clariant) 4.00 % Laureth-23 Diaformer®Z-632N (Clariant) 4.50 % Acrylates / Stearyl Acrylate / Ethylamine Oxide Methacrylate Copolymer Dipropylene Glycol 1.00 %Polyglykol 400 0.50 % PEG-8 Nipaguard™ DMDMH (Clariant)0.50 % DMDM Hydantoin Panthenol 0.50 %Emulsogen®HCO 040 (Clariant) 0.50 % PEG-40 Hydrogenated Castor Oil Fragrance 0.30 %Example Composition 19: Conditioning Shampoo Water Ad 100 %Hybrid H 1.10 %Genapol®LRO liquid (Clariant) 30.00 % Sodium Laureth Sulfate Genagen®CAB 818 (Clariant) 6.00 % Cocamidopropyl BetaineXIAMETER®PMX-200 Silicone Fluid 50 CS 0.25 % Dimethicone Water 10.00 %Jaguar®C-162 0.20 % Hydroxypropyl Guar (and) Hydroxypropyl Guar Hydroxypropyltrimonium Chloride Citric Acid q.s.Water 4.00 %Sodium Benzoate 0.45 %Sodium Chloride 0.50 % Example Composition 20: Nail Varnish Remover Gel Water Ad 100 %Ethanol 27.00 %Polyglykol®400 (Clariant) 3.00 % PEG-8 Glycerin 3.00 % Aristoflex®TAC (Clariant) 0.20 % Ammonium Acryloyldimethyltaurate / Carboxyethyl Acrylate Crosspolymer Hybrid H 1.00 %Ethyl Acetate 30.00 %Example Composition 21: Whitening Gel Genapol®T 250 (Clariant) 2.00 % Ceteareth-25 Genapol®DAT 100 (Clariant) 1.10 % PEG-150 Polyglyceryl-2 Tristearate Water Ad 100 %Ascorbic Acid 2-Glucoside 3.00 %Sodium Hydroxide q.s.Hybrid H 1.50 %NipaguardTMDMDMH (Clariant) 2.00 % DMDM Hydantoin Example Composition 22: O / W Self-Tanning Cream Hostaphat®CC 100 (Clariant) 1.00 % Cetyl Phosphate Glyceryl Stearate 0.50 %Cetearyl Alcohol 0.50 %Mineral Oil 8.00 %Isopropyl Palmitate 7.00 %Tocopheryl Acetate 1.00 %SilCare®Silicone 41M15 (Clariant) 1.00 % Caprylyl Methicone Hybrid H 2.00 %Water ad 100 %Hostapon®KCG (Clariant) 0.50 % Sodium Cocoyl Glutamate Glycerin 5.00 %Fragrance 0.20 %PhenonipTMME (Clariant) 1.00 % Phenoxyethanol, Methylparaben, Ethylparaben Dihydroxyacetone 5.00 %Water 8.00 %Sodium Hydroxide q.s.Example Composition 23: Make Up Remover Water ad 100 %Glycerin 3.00 %Hybrid H 0.80 %Hostaphat®KL 340 D (Clariant) 3.00 % Trilaureth-4 Phosphate Cetearyl Alcohol 1.50 %Plantasens®Olive LD (Clariant) 2.00 % Hydrogenated Ethylhexyl Olivate (and) Hydrogenated Olive Oil Unsaponifiables Isostearyl Isostearate 4.00 %Isohexadecane 4.00 %Sodium Hydroxide q.s.Nipaguard®SCP (Clariant) 1.00 % Phenoxyethanol (and) Sorbitan Caprylate Fragrance 0.20 %Example Composition 24: Insect Repellent Lotion Diethyl Toluamide 10.00 % DEET Hostaphat®KL 340 D (Clariant) 1.00 % Trilaureth-4 Phosphate Isohexadecan 5.00 %C12-15 Alkyl Benzoate 5.00 %Cyclopentasiloxane 2.00 %Hybrid H 1.00 %Water Ad 100 % Ethanol 10.00 %Fragrance 0.30 %Nipaguard®POB (Clariant) 0.80 % Phenoxyethanol (and) Piroctone Olamine (and) Benzoic Acid Example Composition 25: Emulsifier-free Cream Gel Caprylic / Capric Triglyceride 3.00 %Glycine Soya (Soybean) Oil 1.00 %Isopropyl Palmitate 3.60 %Glycerin 1.00 %Water Ad 100 %Hybrid H 1.50 %Fragrance 0.30 %Nipaguard®POB (Clariant) 0.80 % Phenoxyethanol (and) Piroctone Olamine (and) Benzoic Acid Sodium hydroxide q.s.Example Composition 26: Sulfate-free Shampoo Hybrid H 0.5 %Water 20.0 %Glycerin 1.0 %Hostapon®SG (Clariant) 23.0 % Sodium Cocoyl Glycinate Hostapon®CGN (Clariant) 9.5 % Sodium Cocoyl GlutamateLactic Acid q.s.GenagenTMKB (Clariant) 15.0 % Coco-Betaine Water Ad. 100%Perlogen®SF 3000 (Clariant) 5.0 % Aqua (and) Glycol Distearate (and) Laureth-4 (and) Cocamidopropyl Betaine Velsan®SC (Clariant) 1.0 % Sorbitan Caprylate Genamin®PQ 43 (Clariant) 1.0 % Polyquaternium-43 Nipaguard®CG 43 (Clariant) 0.1 % Methylchloroisothiazolinone (and) Methylisothiazolinone Fragrance q.s.Example Composition 27: Hair Conditioner Water Ad. 100%Glycerin 3.0 %Disodium EDTA 0.1 %Hybrid H 0.5 %Cetyl alcohol 8.0 %Genamin®KDMP (Clariant) 2.0 % Behentrimonium Chloride Plantasens®Olive Squalene (Clariant) 2.0 % Squalene Genamin®CTAC (Clariant) 4.0 % Cetrimonium Chloride Plantasens®Olive LD (Clariant) 2.0 % Hydrogenated Ehtylhexyl Olivate (and) Hydrogenated Olive Oil Unsaponifiables Velsan®SC (Clariant) 1.0 % Sorbitan Caprylate PhenoxetolTM(Clariant) 0.5 % Phenoxyethanol Fragrance q.s.

Claims

Claims1. A hybrid polymer comprising(a) a polysaccharide polymer; and(b) peptide chains comprising an amino acid sequence of general formula(I): X1–A4–A5–A6–X2(I) wherein X1represents –H, A3–, A2–A3– or A1–A2–A3–; X2represents –H, –A7, –A7–A8, –A7–A8–A9, –A7–A8–A9–A10, or –A7–A8–A9–A10–A11; A1and A4represent independently of each other a small neutral amino acid or a neutral hydrophilic amino acid; A2and A5represent independently of each other a neutral amino acid, an aromatic amino acid or an amino acid amide; A3 represents a basic amino acid, a large neutral amino acid, or anamino acid amide; A6 represents an amino acid selected from S, T, C, N, Q, Y, A, G and V;A7and A8represent independently of each other a neutral amino acid; A9 represents a basic amino acid, or an amino acid amide;A10 represents a basic amino acid, or an aromatic amino acid; andA11represents a neutral amino acid, a hydrophilic amino acid, or an amino acid amide.

2. The hybrid polymer according to claim 1, whereinA6 represents an amino acid selected from S, T, C, N and Y.

3. The hybrid polymer according to claim 1 or 2, whereinA6 represents an amino acid selected from S and T.

4. The hybrid polymer according to any of claims 1 to 3, wherein thepolysaccharide polymer is selected from dextran, dextrin, hyaluronic acid,chitosan, xanthan gum, fenugreek gum, tara gum, locust bean gum, carrageenan, guar gum, alginate, agar, agarose, starch, amylose, amylopectin, tragacanth gum, tamarind kernel gum, arabica gum, cherry gum, karaya gum, okra gum, cassia gum, chicle gum, konjac gum, ghatti gum, pectin, sclerotium gum, gellan gum, paramylon, paramylum, curdlan, cellulose, diutan gum, inulin, derivatives thereof and mixtures thereof.

5. The hybrid polymer according to any of claims 1 to 4, whereinA1represents an amino acid selected from G and A; A2represents an amino acid selected from Y, F, and W; A3 represents an amino acid selected from R, K, and L;A4represents an amino acid selected from G and A; A5represents an amino acid selected from I, Y, Q, N, L, and F; A6represents an amino acid selected from S and T; A7represents an amino acid selected from L, I, and V; A8represents an amino acid selected from A, G, and V; A9represents an amino acid selected from K, N, and Q; A10 represents an amino acid selected from W and F; andA11represents an amino acid selected from M, M-NH2, L, I, V, A, and G.

6. The hybrid polymer according to any of claims 1 to 5, whereinA1represents an amino acid selected from G and A; A2represents an amino acid selected from Y and F; A3 represents an amino acid selected from R, K, and L;A4represents an amino acid selected from G and A; A5represents an amino acid selected from I and Y; A6represents an amino acid selected from S and T; A7represents an amino acid selected from L and I; A8represents an amino acid selected from A and G; A9represents an amino acid selected from K and N; A10 represents an amino acid selected from W and F; andA11represents an amino acid selected from M, M-NH2, L, I, and V.

7. The hybrid polymer according to any of claims 1 to 6, whereinA1represents G; A2represents an amino acid selected from Y and F; A3represents an amino acid selected from R, K and L; A4represents G; A5represents an amino acid selected from I and Y; A6represents an amino acid selected from S and T; A7represents L; A8represents A; A9represents an amino acid selected from K and N; A10 represents W; andA11represents an amino acid selected from M, M-NH2, and V.

8. The hybrid polymer according to any of claims 1 to 7, whereinX1 represents A2–A3– or A1–A2–A3–; andX2represents –A7–A8–A9, –A7–A8–A9–A10, or –A7–A8–A9–A10–A11.

9. The hybrid polymer according to any of claims 1 to 8, wherein the peptidechains (b) comprise an amino acid sequence selected from GYLGIS (SEQ IDNO: 2), GISLAN (SEQ ID NO: 3), YRGISLANWM (SEQ ID NO: 4), YRGISLANW (SEQ ID NO: 5), GFRGISLANWM (SEQ ID NO: 6),GYKGISLANWM (SEQ ID NO: 7), GYRGISLANWM (SEQ ID NO: 8), GYRGYSLANWM (SEQ ID NO: 9), GYRGITLANWM (SEQ ID NO: 10), GYRGISLAKWM (SEQ ID NO: 11) GYRGISLANWV (SEQ ID NO: 12), GYLGISLANW (SEQ ID NO: 13), and GYRGISLANWM-NH2(SEQ ID NO: 14).

10. The hybrid polymer according to any of claims 1 to 9, wherein the peptidechains (b) comprise an amino acid sequence selected from CGYLGIS (SEQ ID NO: 15), CGISLAN (SEQ ID NO: 16), CYRGISLANWM (SEQ ID NO: 17), CYRGISLANW (SEQ ID NO: 18), CGFRGISLANWM (SEQ ID NO: 19),CGYKGISLANWM (SEQ ID NO: 20), CGYRGISLANWM (SEQ ID NO: 21), CGYRGYSLANWM (SEQ ID NO: 22), CGYRGITLANWM (SEQ ID NO: 23), CGYRGISLAKWM (SEQ ID NO: 24) CGYRGISLANWV (SEQ ID NO: 25), CGYLGISLANW (SEQ ID NO: 26), and CGYRGISLANWM-NH2 (SEQ ID NO: 27).

11. The hybrid polymer according to any of claims 1 to 10, wherein the peptidechains (b) comprise an amino acid sequence selected from GYLGIS (SEQ ID NO: 2), GISLAN (SEQ ID NO: 3), GYRGISLANWM (SEQ ID NO: 8), CGYLGIS (SEQ ID NO: 15), CGISLAN (SEQ ID NO: 16), and CGYRGISLANWM (SEQID NO: 21).

12. The hybrid polymer according to any of claims 1 to 11, wherein the peptidechains (b) are linked to the polysaccharide polymer (a), optionally through alinker, via the N-terminal amino acid of the peptide chains (b).

13. A blend comprising(a) from 1 to 99 wt-%, preferably from 20 to 80 wt-%, more preferably from30 to 70 wt-%, even more preferably from 40 to 65 wt-%, particularlypreferably from 50 to 60 wt-%, of a hybrid polymer as defined in any ofclaims 1 to 12, based on the total weight of the blend; and (b) from 1 to 99 wt-%, preferably from 20 to 80 wt-%, more preferably from30 to 70 wt-%, even more preferably from 35 to 60 wt-%, particularlypreferably from 40 to 50 wt-%, of one or more polysaccharide polymersand / or one or more peptides, based on the total weight of the blend.

14. Use of a hybrid polymer as defined in any of claims 1 to 12 or a blend asdefined in claim 13 as a rheology modifying agent.

15. A hydrogel comprising a hybrid polymer as defined in any of claims 1 to 12 ora blend as defined in claim 13, water, optionally a pH adjusting agent, andoptionally an ionic strength adjusting agent.

16. The hydrogel according to claim 15, wherein the hydrogel further comprises anactive ingredient, wherein the active ingredient is preferably selected fromvitamins, moisturizing agents, anti-aging agents, anti-wrinkle agents, anti-inflammatory agents, amino acids, peptides, and mixtures thereof.

17. A formulation comprising(a) from 0.1 to 10 wt-%, preferably from 0.2 to 5 wt-%, more preferably from0.3 to 3 wt-%, even more preferably from 0.4 to 2 wt-%, particularlypreferably from 0.5 to 1 wt-%, of a hybrid polymer as defined in any ofclaims 1 to 12 or a blend as defined in claim 13, based on the totalweight of the formulation; and (b) from 90 to 99.9 wt-%, preferably from 95 to 99.8 wt-%, more preferablyfrom 97 to 99.7 wt-%, even more preferably from 98 to 99.6 wt-%,particularly preferably from 99 to 99.5 wt-%, of one or more furthercomponents, based on the total weight of the formulation.

18. The formulation according to claim 17, wherein the formulation is a cosmeticformulation, preferably a skin care formulation or a hair care formulation.