TECHNOLOGY FOCUS - BIOTECHNOLOGY - Preferred Peptide: In the hydrophobic peptide and/or peptidomimetic, the aliphatic amino acids and aliphatic amino acid derivatives are either D-amino acids or L-amino acids. The aliphatic amino acids are selected from alanine (Ala, A), homoallylglycine, homopropargylglycine, isoleucine (He, I), norleucine, leucine (Leu, L), valine (Val, V) and glycine (Gly, G), preferably from alanine (Ala, A), isoleucine (Ile, I), leucine (Leu, L), valine (Val, V) and glycine (Gly, G). All or a portion of the aliphatic amino acids are arranged in an order of decreasing amino acid size in the direction from N- to C-terminus, where the size of the aliphatic amino acids is defined as I=L greater than or equal to V greater than or equal to A greater than or equal to G. The first N-terminal amino acid of the aliphatic amino acids is G, V or A. The aliphatic amino acids arranged in an order of decreasing amino acid size have a sequence which is a repetitive or non-repetitive sequence. The aliphatic amino acids have a sequence selected from Ile-Leu-Val-Ala-Gly (SEQ ID NO: 1), Leu-Ile-Val-Ala-Gly (SEQ ID NO: 2), Ile-Val-Ala-Gly (SEQ ID NO: 3), Leu-Val-Ala-Gly (SEQ ID NO: 4), Ile-Leu-Val-Ala (SEQ ID NO: 5), Leu-Ile-Val-Ala (SEQ ID NO: 6), Ile-Val-Gly (SEQ ID NO: 13), Val-Ile-Gly (SEQ ID NO: 14), Ile-Val-Ala (SEQ ID NO: 15), Val-Ile-Ala (SEQ ID NO: 16), Val-Ile (SEQ ID NO: 17) and Ile-Val (SEQ ID NO: 18), where, optionally, there is a Gly, Val or Ala preceding such sequence at the N-terminus, such as Ala-Ile-Val-Ala-Gly (SEQ ID NO: 7), Gle-Ile-Val-Ala-Gly (SEQ ID NO: 8), Val-Ile-Val-Ala-Gly (SEQ ID NO: 9), Ala-Leu-Val-Ala-Gly (SEQ ID NO: 10), Gly-Leu-Val-Ala-Gly (SEQ ID NO: 11), and Val-Leu-Val-Ala-Gly (SEQ ID NO: 12). The (X)a has a sequence selected from SEQ ID NOS: 1-18, preferably the sequence with SEQ ID NO: 1 or SEQ ID NO: 2. The N-terminal protecting group Z has the general formula -C(O)-R, where R is selected from H, unsubstituted or substituted alkyls, and unsubstituted or substituted aryls, where R is preferably selected from methyl, ethyl, propyl, isopropyl, butyl and isobutyl. The N-terminal protecting group is an acetyl group. The N-terminal protecting group Z is a peptidomimetic molecule, including natural and synthetic amino acid derivatives, where the N-terminus of the peptidomimetic molecule may be modified with a functional group selected from carboxylic acid, amide, alcohol, aldehyde, amine, imine, nitrile, an urea analog, phosphate, carbonate, sulfate, nitrate, maleimide, vinyl sulfone, azide, alkyne, alkene, carbohydrate, imide, peroxide, ester, aryl, ketone, sulfite, nitrite, phosphonate, and silane. The C-terminal group Z' is selected from the group of small molecules, functional groups and linkers. The C-terminal group Z' is selected from: functional groups, such as polar or non-polar functional groups, such as (but not limited to) -COOH, -COOR, -COR, -CONHR or -CONRR' with R and R' being selected from H, unsubstituted or substituted alkyls, and unsubstituted or substituted aryls, -NH2, -OH, -SH, -CHO, maleimide, imidoester, carbodiimide ester, isocyanate; small molecules, such as (but not limited to) sugars, alcohols, hydroxy acids, amino acids, vitamins, biotin; linkers terminating in a polar functional group, such as (but not limited to) ethylenediamine, PEG, carbodiimide ester, imidoester; linkers coupled to small molecules or vitamins, such as biotin, sugars, hydroxy acids. The C-terminal group Z' can be used for chemical conjugation or coupling of at least one compound selected from bioactive molecules or moieties, such as growth factors, cytokines, lipids, cell receptor ligands, hormones, prodrugs, drugs, vitamins, antigens, antibodies, antibody fragments, oligonucleotides (including but not limited to DNA, messenger RNA, short hairpin RNA, small interfering RNA, microRNA, peptide nucleic acids, aptamers), saccharides; label(s), dye(s), such as fluorescent or radioactive label(s), imaging contrast agents; pathogens, such as viruses, bacteria and parasites; micro- and nanoparticles or combinations where the chemical conjugation can be canied out before or after self-assembly of the peptide and/or peptidomimetic. The C-terminus of the peptide and/or peptidomimetic is functionalized, such as by chemical conjugation or coupling of at least one compound selected from bioactive molecules or moieties, such as growth factors, cytokines, lipids, cell receptor ligands, hoimones, prodrugs, drugs, vitamins, antigens, antibodies, antibody fragments, oligonucleotides (including but not limited to DNA, messenger RNA, short hairpin RNA, small interfering RNA, microRNA, peptide nucleic acids, aptamers), saccharides; label(s), dye(s), such as fluorescent or radioactive label(s), imaging contrast agents; pathogens, such as viruses, bacteria and parasites; micro- and nanoparticles or combinations where the chemical conjugation can be earned out before or after self-assembly of the peptide and/or peptidomimetic. The C-terminal group Z' is a peptidomimetic molecule, including natural and synthetic amino acid derivatives, where the C-terminus of the peptidomimetic molecule may be modified with a functional group selected from caiboxylic acid, amide, alcohol, aldehyde, amine, imine, nitrile, an urea analog, phosphate, carbonate, sulfate, nitrate, maleimide, vinyl sulfone, azide, alkyne, alkene, carbohydrate, imide, peroxide, ester, aryl, ketone, sulfite, nitrite, phosphonate, and silane. Preferred Hydrogel: The hydrogel is stable in aqueous solution at ambient temperature for a period of at least 7 days, preferably at least 2 to 4 weeks, more preferably at least 1-6 months. The hydrogel is characterized by a storage modulus G' to loss modulus G'' ratio that is greater than 2. The hydrogel is characterized by a storage modulus G' of 100-80000 Pa at a frequency in the range of 0.02-16 Hz. Also, it has a higher mechanical strength than collagen or its hydrolyzed form (gelatin). Alternatively, the hydrogel comprises: (a) at least one hydrophobic peptide and/or peptidomimetic; and (b) at least one hydrophobic peptide and/or peptidomimetic with a non-polar head group. The hydrogel comprises fibers of the hydrophobic peptide and/or peptidomimetic and/or fibers of the hydrophobic peptide and/or peptidomimetic with a non-polar head group, the fibers defining a network that is capable of entrapping at least one of a microorganism, a virus particle, a peptide, a peptoid, a protein, a nucleic acid, an oligosaccharide, a polysaccharide, a vitamin, an inorganic molecule, a synthetic polymer, a micro-or nanoparticle, a small organic molecule or a pharmaceutically active compound. Moreover, the hydrogel comprises at least one of a microorganism, a virus particle, a peptide, a peptoid, a protein, a nucleic acid, an oligosaccharide, a polysaccharide, a vitamin, an inorganic molecule, a synthetic polymer, a small organic molecule, a micro-or nanoparticle, or a pharmaceutically active compound entrapped by the network of fibers of the hydrophobic polymer. The fibers of the hydrophobic polymer are coupled to the at least one of a microorganism, a virus particle, a peptide, a peptoid, a protein, a nucleic acid, an oligosaccharide, a polysaccharide, a vitamin, an inorganic molecule, a synthetic polymer, a small organic molecule, a micro-or nanoparticle, or a pharmaceutically active compound entrapped by the network o fibers of the amphiphilic polymer. The hydrogel is comprised in at least one of a fuel cell, a solar cell, an electronic cell, a biosensing device, a medical device, an implant, a pharmaceutical composition and a cosmetic composition. The hydrogel is injectable. Preferred Method: In preparing the hydrogel, the dissolved hydrophobic peptide and/or peptidomimetic in aqueous solution is further exposed to temperature, where the temperature is in the range of 20-90 degrees C, preferably 20-70 degrees C. The hydrophobic peptide and/or peptidomimetic is dissolved at a concentration of 0.01 mu g/ml to 100 mg/ml, preferably at a concentration of 1-50 mg/ml, preferably 1-20 mg/ml. Alternatively, preparing the hydrogel comprises dissolving a hydrophobic peptide and/or peptidomimetic and a hydrophobic peptide and/or peptidomimetic with a non-polar head group in an aqueous solution. In the in vitro or in vivo method of tissue regeneration, is performed in vivo, where, in step (a), the hydrogel is provided at a place in a body where tissue regeneration is intended, where the step (a) is preferably performed by injecting the hydrogel at a place in the body where tissue regeneration is intended. Preferred Composition: The pharmaceutical and/or cosmetic composition further comprises a pharmaceutically active compound, and where the pharmaceutical and/or cosmetic composition is provided in the form of a topical gel or cream, a spray, a powder, or a sheet, patch or membrane, or where the pharmaceutical and/or cosmetic composition is provided in the form of an injectable solution. Preferred Kit: The kit further comprises a third container with the hydrophobic peptide and/or peptidomimetic with the non-polar head group. The aqueous solution of the second container further comprises a pharmaceutically active compound; and/or where the first and/or third container with a hydrophobic peptide and/or peptidomimetic further comprises a pharmaceutically active compound. ACTIVITY - Vulnerary. No biological data given.    MECHANISM OF ACTION - Gene Therapy; Cell Therapy.    ADMINISTRATION - Administration is through oral (claimed), parenteral, intramuscular, rectal, transmucosal, intestinal, subcutaneous, intravenous, intramedullary, intrathecal, intraventricular, intraperitoneal, intranasal, or intraocular route. No dosage details given.    EXAMPLE - No suitable example given.