TECHNOLOGY FOCUS - BIOLOGY - Preferred Components: (I) is preferably Leu-Ile-Val-Ala-Gly-Lys-Cys (SEQ ID NO: 43), Leu-Ile-Val-Ala-Gly-Ser-Cys (SEQ ID NO: 44), Leu-Ile-Val-Ala-Gly-Asp-Cys (SEQ ID NO: 45), Ile-Leu-Val-Ala-Gly-Lys-Cys (SEQ ID NO: 46), Ile-Leu-Val-Ala-Gly-Asp-Cys (SEQ ID NO: 47), Leu-Ile-Val-Ala-Gly-Cys (SEQ ID NO: 48), Ala-Ile-Val-Ala-Gly-Cys (SEQ ID NO: 49), Ile-Leu-Val-Ala-Gly-Cys (SEQ ID NO: 50), Ile-Val-Lys-Cys (SEQ ID NO: 51), Ile-Val-Asp-Cys (SEQ ID NO: 52) and Ile-Val-Ser-Cys (SEQ ID NO: 53). The active compound comprises haemostatic agents, antibiotics, antimicrobial agents, anti-fungal agents, anti-inflammatory agents, analgesics, anti-coagulants, antibodies, antigens, growth factors and cytokines. Preferred Composition: The pharmaceutical or cosmetic composition is provided: in the form of a topical gel or cream, a spray, a powder, or a sheet, patch or membrane; and in the form of an injectable solution. The pharmaceutical or cosmetic composition further comprises the active compound, and a carrier.    TECHNOLOGY FOCUS - ORGANIC CHEMISTRY - Preferred Components: The amino acid comprising a thiol group is cysteine and homocysteine. The amphiphilic peptides and/or peptoids are chemically cross-linked via sulfhydryl-to-sulfhydryl cross-linking, sulfhydryl-to-hydroxyl cross-linking, sulfhydryl-to-aldehyde cross-linking, sulfhydryl-to-amine cross-linking, peptidoglycans or photo-induced cross-linking, preferably sulfhydryl-to-sulfhydryl cross-linking. The N-terminal protecting group is a carbonyl compound of formula (-C(O)-R) (II). The N-terminal protecting group and the C-terminal protecting group comprise a peptidomimetic molecule including natural and synthetic amino acid derivatives, where the N-terminus and C-terminus of the peptidomimetic molecule are modified with a functional group comprising carboxylic acid, amide, alcohol, aldehyde, amine, imine, nitrile, an urea analog, thiol, phosphate, carbonate, sulfate, nitrate, maleimide, vinyl sulfone, azide, alkyne, alkene, carbohydrate, imide, peroxide, ester, thioester, aryl, ketone, sulfite, nitrite, phosphonate and silane. The C-terminus of the amphiphilic peptides and/or peptoids comprises an amide compound of formula (-CONHR2) (III) or (-CONR2R1a) (IV), and an ester compound of formula (-CO2R) (V). The aliphatic amino acid, the hydrophilic amino acid and the amino acid comprising a thiol group are either D-amino acids or L-amino acids for a given amphiphilic peptide and/or peptoid. The hydrophilic amino acid has a polar group, which comprises a hydroxyl, an ether, a carboxyl, an imido, an amido, an ester, an amino, a guanidino, a thio, a thioether, a seleno, and a telluro group. The hydrophilic amino acid comprises aspartic acid, asparagine, glutamic acid, glutamine, cysteine, threonine, serine, ornithine, 2,4-diaminobutyric acid, 2,3-diaminopropionic acid, lysine, histidine (all preferred), 5-N-ethyl-glutamine (theanine), citrulline, thio-citrulline, homocysteine, methionine, ethionine, selenomethionine, telluromethionine, allo-threonine, homoserine, arginine, homoarginine, and N(6)-carboxy-methyllysine. The aliphatic amino acid comprises isoleucine, norleucine, leucine, valine, alanine, glycine, homoallylglycine and homopropargylglycine. The aliphatic amino acids arranged in an order of decreasing amino acid size have a sequence, which is a repetitive or non-repetitive sequence, comprising Leu-Ile-Val-Ala-Gly, Ile-Leu-Val-Ala-Gly, Leu-Ile-Val-Ala-Ala, Leu-Ala-Val-Ala-Gly, Ile-Val-Ala-Gly, Leu-Ile-Val-Ala, Leu-Ile-Val-Gly, Ile-Val-Ala and Ile-Val, where optionally, there is an A preceding such sequence at the N-terminus. The portion of the aliphatic amino acids of the amphiphilic peptides and/or peptoids are arranged in an order of decreasing amino acid size in the direction from N- to C-terminus of the amphiphilic peptides and/or peptoids, where the size of: leucine is greater than the valine, which is greater than the alanine; and alanine is greater than the glycine. The amphiphilic peptides and/or peptoids undergo a conformational change during self-assembly, preferably a conformational change from a random coil conformation to a helical intermediate structure to a final beta conformation. The conformational change is dependent on the concentration of the amphiphilic peptides and/or peptoids, dependent on the ionic environment, pH dependent and/or temperature dependent. The amphiphilic peptides and/or peptoids are the same or different. The hydrogel is stable in aqueous solution at ambient temperature for a period of at least 7 days, preferably at least 1-6 months. At least 5%, preferably at least 50% of the amphiphilic peptides and/or peptoids are chemically cross-linked. The hydrogel has: a storage modulus (G') to loss modulus (G") ratio that is greater than 2; a storage modulus (G') of 100-1000000 Pa, preferably 1000-1000000 Pa, at a frequency of 0.02-16 Hz; and an elasticity defined as % strain at linear viscoelasticity limit of above 0.01% strain, preferably above 2% strain. The hydrogel further comprises a non-peptidic polymer, and at least one microorganism, a cell, a virus particle, a peptide, a peptoid, a protein, a nucleic acid, an oligosaccharide, a polysaccharide, a vitamin, an inorganic molecule, a nano- or microparticle, a synthetic polymer, a small organic molecule, a cosmetic agent and/or an active compound that is entrapped by the three- dimensional macromolecular nanofibrous networks, is coupled to the amphiphilic peptides and/or peptoids, preferably via a disulfide bridge and is coupled to the non-peptidic polymer. The hydrogel comprises one or more bioactive therapeutics that stimulate regenerative processes and/or modulate the immune response. The nano- or microparticle is a metal nano- or microparticle, preferably a gold nano- or microparticle. The peptide: comprises a signal sequence, comprising an adhesion or growth signal, such as an integrin binding sequence; and is coupled to the amphiphilic peptides and/or peptoids via a disulfide bridge. The hydrogel is provided in an injectable form and gels in situ. The oxidizing agent is hydrogen peroxide present in a concentration of 0.02-0.3 wt.%, preferably 0.05-0.2 wt.%. The amphiphilic peptides and/or peptoids are dissolved at a concentration of 0.01 g/ml to 50 mg/ml, preferably 5 mg/ml to 12 mg/ml.R = H, optionally substituted alkyls or aryls; andR2, R1a = H, or optionally substituted alkyls or aryls.Preferred Method: In the method-I, the dissolved amphiphilic peptides and/or peptoids in aqueous solution are further exposed to a temperature of 20-90 degrees C, preferably 20-40 degrees C for at least 1 hour, preferably at least 24 hours. The method-I further comprises: exposing the ready-made hydrogel to an aqueous solution not comprising the oxidizing agent, where, if the method comprises exposing the ready-made hydrogel to a solution of the oxidizing agent, the step of exposing the ready-made hydrogel to an aqueous solution not comprising the oxidizing agent is performed after the step of exposing the ready-made hydrogel to a solution of the oxidizing agent; adding the microorganism, the cell, the virus particle, the peptide, the peptoid, the protein, the nucleic acid, the oligosaccharide, the polysaccharide, the vitamin, the inorganic molecule, the nano- or microparticle, the synthetic polymer, the small organic molecule, the cosmetic agent and/or the active compound; adding the non-peptidic polymer; adding at least one gelation enhancer, which is a salt or a solution of a salt; and adding at least one buffer, preferably at least one physiologically acceptable buffer. The step of exposing the ready-made hydrogel to an aqueous solution not comprising the oxidizing agent: is repeated at least once; and occurs for at least 1 hour, preferably at least 6 hours and at a temperature of 30-45 degrees C, preferably 35-40 degrees C. The method-II is performed in vitro, ex vivo (both preferred) or in vivo. In the method-II, the hydrogel is provided at a place in the body of a patient, where tissue regeneration or tissue replacement is intended. In the method-II; the step (a) is performed by injecting the hydrogel or a solution of amphiphilic peptides and/or peptoids at a place in the body of a patient, where tissue regeneration or tissue replacement is intended; and the providing step further comprises the co-injection of a gelation enhancer, preferably of a solution of a salt, and/or the co-injection of an oxidizing agent. In the method-II comprising the step of providing the hydrogel and the step of exposing the hydrogel to cells, the cells from a patient or from a donor are mixed with the hydrogel, and the resulting mixture is provided at a place in the body of a patient where tissue regeneration or tissue replacement is intended. ACTIVITY - Vulnerary; Uropathic.    MECHANISM OF ACTION - None given.    ADMINISTRATION - Administration of the hydrogel is oral, rectal, transmucosal, intestinal, parenteral (including intramuscular, subcutaneous, intravenous and injections), intrathecal, direct intraventricular, intraperitoneal, intranasal, or intraocular injection. No dosage details given.    EXAMPLE - No suitable example given.