TECHNOLOGY FOCUS - BIOTECHNOLOGY - Preparation: No preparation method given. Preferred Peptide: The amphiphilic peptide and/or peptoid have a C-terminus and an N-terminus, where the N-terminus is protected by a protecting group. The protecting group is an acetyl group. The amphiphilic peptide and/or peptoid are amidated if a basic polar amino acid is located at its C-terminus. The n is 2-6 and m is 1-2. The amphiphilic peptide and/or peptoid comprise o amphiphilic sequences, where the amphiphilic sequences are linked to each other and o is 1-50. The aliphatic amino acids and the hydrophilic amino acids are D-amino acids or L-amino acids. Each of the hydrophilic amino acids has a polar group chosen from hydroxyl, ether, carboxyl, imido, amido, ester, amino, guanidino, thio, thio- ther, seleno, and telluro group. The polar moiety of the hydrophilic sequence stretch comprises m adjacent hydrophilic amino acids chosen from aspartic acid, asparagine, glutamic acid, glutamine, 5-N-ethyl-glutamine (theanine), citrulline, thio-citrulline, cysteine, homocysteine, methionine, ethionine, selenomethionine, telluromethionine, threonine, allo-threonine, serine, homoserine, arginine, homoarginine, ornithine, lysine N(6) carboxymethyllysine, and histidine. The hydrophobic sequence stretch comprises n aliphatic amino acids chosen from isoleucine, norleucine, leucine, valine, alanine, glycine, homoallylglycine, and homopropargylglycine. The polar moiety comprises two identical amino acids when m is 2, and comprises any one of aspartic acid, asparagine, glutamic acid, glutamine, serine, threonine, cysteine, methionine, lysine or histidine when m is 1. The polar moiety is adjacent to the hydrophobic sequence stretch of n aliphatic amino acids. The polar moiety has a sequence chosen from Asp, Asn, Glu, Gln, Ser, Thr, Cys, Met, Lys, His, Asn-Asn, Asp-Asp, Glu-Glu, Gln-Gln, Asn-Gln, Gln-Asn, Asp-Gln, Gln-Asp, Asn-Glu, Glu-Asn, Asp- Glu, Glu-Asp, Gln-Glu, Glu-Gln, Asp-Asn, Asn-Asp Thr-Thr, Ser-Ser, Thr-Ser, Ser-Thr, Asp- Ser, Ser-Asp, Ser-Asn, Asn-Ser, Gln-Ser, Ser-Gln, Glu-Ser, Ser-Glu, Asp-Thr, Thr-Asp, Thr-Asn, Asn-Thr, Gln-Thr, Thr-Gln, Glu-Thr, and Thr-Glu. The polar moiety comprises (a) the C-terminus of the amphiphilic peptide and/or peptoid, or the N-terminus of the amphiphilic peptide and/or peptoid, where both the C-terminus and the N-terminus do not carry any protecting groups attached to them, (b) the C-terminus of the amphiphilic peptide and/or peptoid, where both the C-terminus and the N-terminus do not carry any protecting groups attached to them, (c) the C-terminus of the amphiphilic peptide and/or peptoid, where the C-terminus does not carry any protecting group, and the N-terminus carries a protecting group (G1) and the protecting group (G1) is an acetyl group attached to the amino-group of the N-terminus, (d) the C-terminus of the amphiphilic peptide and/or peptide, where the C-terminus carries a protecting group (G2) and the protecting group (G2) is an amido-group attached to the carboxyl group of the C-terminus, and the N-terminus does not carry any protecting group, or (e) the C-terminus of the amphiphilic peptide and/or peptoid, where both the C- terminus and N-terminus carry a protecting group, and the C-terminus protecting group is protecting group (G2) and the N-terminus protecting group is protecting group (G1). The polar moiety consists of at least one amino acid positioned at the C-terminus of the amphiphilic peptide and/or peptoid. The hydrophobic sequence stretch comprises and/or forms the N-terminus of the amphiphilic peptide and/or peptoid. All or a portion of the aliphatic amino acids of the hydrophobic sequence stretch are arranged in an order of decreasing amino acid size in the direction from N- to C-terminus of the amphiphilic peptide and/or peptide, where the size of the aliphatic amino acids is represented as I = leucine not greater than valine not greater than alanine not greater than glycine. The aliphatic amino acids arranged in an order of decreasing amino acid size have a sequence which is a repetitive or non-repetitive sequence of length 2-7, preferably 2-5 amino acids. The aliphatic amino acids arranged in an order of decreasing amino acid size have a sequence chosen from 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 there is an A preceding sequence at the N-terminus optionally. All or a portion of the aliphatic amino acids of the hydrophobic sequence stretch are arranged in an order of identical amino acid size in the amphiphilic peptide and/or peptide. The aliphatic amino acids arranged in order of identical amino acid size have a sequence with a length of 2-4 amino acids. The aliphatic amino acids arranged in an order of identical size have a sequence chosen from Leu-Leu-Leu-Leu, Leu-Leu-Leu, Leu-Leu, Ile-Ile-Ile-Ile, Ile-Ile-Ile, Ile-Ile, Try-Try, Try-Val, Val-Val, Ala-Ala-Ala-Ala, Ala-Ala-Ala, Ala-Ala, Gly-Gly-Gly-Gly, Gly-Gly-Gly, and Gly-Gly. The amphiphilic sequence undergoes a conformational change during self-assembly, where the conformational change is preferably a conformational change from a random coil conformation to a helical intermediate structure to a final beta conformation and the conformational change is concentration dependent. The amphiphilic linear sequence comprises a single hydrophilic and at least two aliphatic amino acids. The amphiphilic sequence comprises an amino acid sequence of either of SEQ ID NOs: 1-42. The amphiphilic peptide and/or peptoid are stable in aqueous solution at physiological conditions at ambient temperature for 1 day to at least 6, preferably 12 months. The amphiphilic peptide and/or peptoid is stable in aqueous solution at physiological conditions at a temperature upto 90 degrees C for at least 1 hour. Preferred Gel: The hydrogel is stable in aqueous solution at ambient temperature for at least 7 days, preferably 1-6 months. The hydrogel has storage modulus G' to loss modulus G" ratio which is greater than 2. The hydrogel has storage modulus G' from 100-80000 Pa at a frequency of 0.02-16 Hz. The hydrogel comprises fibers of the amphiphilic peptide and/or peptoid, where the fibers are network and hydrogel comprises at least one of microorganism, virus particle, peptide, protein, nucleic acid, oligosaccharide, polysaccharide, vitamin, inorganic molecule, synthetic polymer, small organic molecule or pharmaceutically active compound entrapped by the network of fibers of the amphiphilic polymer. The hydrogel is injectable. Preferred Method: The method (M1) further involves exposing the dissolved amphiphilic peptide and/or peptoid aqueous solution to temperature of 20-90 degrees C, preferably 20-70 degrees C. The amphiphilic peptide and/or peptoid is dissolved at a concentration of 0.01 mu g/ml-100 mg/ml, preferably 1-20 mg/ml. The pharmaceutical, cosmetic composition, the biomedical device, and/or the electronic devices further comprise a pharmaceutically active compound, where the pharmaceutical and/or cosmetic composition further comprise a carrier in combination with the pharmaceutically active compound. The method (M2) is performed in vitro or in vivo. The step (a) of method (M2) involves providing hydrogel is at a place in a body where tissue regeneration is required when the method (M2) is performed in vivo. The step (a) is performed by injecting the hydrogel. Preferred Kit: The aqueous solution of the second container of the kit further comprises a pharmaceutically active compound and the first container with an amphiphilic peptide and/or peptoid further comprises a pharmaceutically active compound. Ac-Leu-Ile-Val-Ala-Gly-Asp-Asp-COOH (L) (SEQ ID NO: 1), Ac-Leu-Ile-Val-Ala-Gly-Asp-COOH (L) (SEQ ID NO: 2), Ac-Leu-Ile-Val-Ala-Gly-Asp-COOH (D) (SEQ ID NO: 3), Ac-Ala-Ile-Val-Ala-Gly-Asp-COOH (L) (SEQ ID NO: 4), Ac-Ala-Ile-Val-Ala-Gly-Asp-COOH (D) (SEQ ID NO: 5), Ac-Ile-Leu-Val-Ala-Gly-Asp-COOH (L) (SEQ ID NO: 6), Ac-Ile-Leu-Val-Ala-Gly-Asp-COOH (D) (SEQ ID NO: 7), Ac-Leu-Ala-Val-Ala-Gly-Asp-COOH (L) (SEQ ID NO: 8), Ac-Leu-Ile-Val-Ala-Ala-Asp-COOH (L) (SEQ ID NO: 9), Ac-Leu-Ile-Val-Ala-Gly-Ser-COOH (L) (SEQ ID NO: 10), Ac-Leu-Ile-Val-Ala-Gly-Ser-COOH (D) (SEQ ID NO: 11), Ac-Ala-Ile-Val-Ala-Gly-Ser-COOH (L) (SEQ ID NO: 12), Ac-Ile-Leu-Val-Ala-Gly-Ser-COOH (L) (SEQ ID NO: 13), Ac-Leu-Ile-Val-Ala-Gly-Thr-COOH (L) (SEQ ID NO: 14), Ac-Ala-Ile-Val-Ala-Gly-Thr-COOH (L) (SEQ ID NO: 15), Ac-Leu-Ile-Val-Ala-Gly-Glu-Glu-COOH (L) (SEQ ID NO: 16), Ac-Leu-Ile-Val-Ala-Gly-Glu-COOH (L) (SEQ ID NO: 17), Ac-Leu-Ile-Val-Ala-Gly-Glu-COOH (D) (SEQ ID NO: 18), Ac-Leu-Ile-Val-Ala-Gly-Lys-CONH2 (L) (SEQ ID NO: 19), Ac-Leu-Ile-Val-Ala-Asp-COOH (L) (SEQ ID NO: 20), Ac-Leu-Ile-Val-Gly-Asp-COOH (L) (SEQ ID NO: 21), Ac-Ile-Val-Ala-Asp-COOH (L) (SEQ ID NO: 22), Ac-Ile-Val-Ala-Asp-COOH (L) (SEQ ID NO: 23), and Ac-Ile-Val-Asp-COOH (L) (SEQ ID NO: 24). ACTIVITY - Vulnerary. No biological data given.    MECHANISM OF ACTION - Cell therapy; Gene therapy.    ADMINISTRATION - The hydrogel in the form of capsule, tablet, injection, spray, suspension, patch, composite material, or plaster is administered by oral, rectal, transmucosal, enteric, parenteral delivery, preferably intramuscular, subcutaneous, intravenous, intramedullar, intrathecal, direct intraventricular, intraperitoneal, intranasal, or intraocular route. No dosage details given.    EXAMPLE - No suitable example given.