TECHNOLOGY FOCUS - BIOTECHNOLOGY - Recombinant Methods (Disclosed): The amphiphilic peptide and/or peptoid is prepared by standard recombinant techniques. Preferred Peptide: The amphiphilic peptide and/or peptoid has C-terminus and an N-terminus, where the N-terminus is protected by an N-terminal protecting group. The amphiphilic peptide and/or peptoid has C-terminus and an N-terminus, where the C-terminus is protected by a C-terminal protecting group. The amphiphilic peptide and/or peptoid consist of 'o' amphiphilic sequences, which amphiphilic sequences are linked to each other. For a given amphiphilic peptide and/or peptoid, the aliphatic amino acids and the hydrophilic amino acids are either D-amino acids or L-amino acids. The amphiphilic peptide and/or peptoid is of formula: Zp-(X)n'-(Y')m'-Z'q. The amphiphilic peptide and/or peptoid has an amidated C-terminus. The amphiphilic peptide and/or peptoid has an acetylated N-terminus, where the N-terminal amino acid of the amphiphilic peptide and/or peptoid is an isoleucine (I).o=1 to 50;Z=N-terminal protecting group;X=aliphatic amino acid;Y'=hydrophilic amino acid;Z'=C-terminal protecting group;n'=2 to 6, preferably 2 to 5;m'=1-2 (preferably 1);p and q=0-1 (preferably 1).Preferred Components: The N-terminal protecting group is of formula -C(O)-R. The N-terminal protecting group is an acetyl group. The N-terminal protecting group 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, 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-terminal protecting group is an amide group. The C-terminus of the amphiphilic peptide and/or peptoid is of formula -CONHR or -CONRR'. The C-terminal protecting group is an ester group. The C-terminus of the amphiphilic peptide and/or peptoid is of formula -CO2R. The C-terminal protecting group is a peptidomimetic molecule, including natural and synthetic amino acid derivatives, where the C-terminal of the peptidomimetic molecule may be modified with a functional group selected from 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. Each of the hydrophilic amino acids has a polar group which is selected from a hydroxyl, ether, a carboxyl, an imido, an amido, an ester, an amino, a guanidino, a thio, a thioether, a seleno, and a telluro group. The polar moiety of the hydrophilic sequence stretch comprises m adjacent hydrophilic amino acids, where the hydrophilic amino acids are selected 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 (Orn), 2,4-diaminobutyric acid (Dab), 2,3-diaminopropionic acid (Dap), lysine and N(6)-carboxymethyllysine, histidine, where the hydrophobic sequence stretch comprises n aliphatic amino acids, where the aliphatic amino acids are selected from isoleucine, norleucine, leucine, valine, alanine, glycine, homoallylglycine and homopropargylglycine. When m is 2, the polar moiety comprises two identical amino acids, or when m is 1, the polar moiety comprises any one of aspartic acid, asparagine, glutamic acid, glutamine, serine, threonine, cysteine, methionine, lysine, ornithine (Orn), 2,4-diaminobutyric acid (Dab), 2,3-diaminopropionic acid (Dap) and histidine. The polar moiety is adjacent to the hydrophobic sequence stretch of n aliphatic amino acids. The polar moiety has a sequence selected from Asp, Asn, Glu, Gln, Ser, Thr, Cys, Met, Lys, Orn, Dab, Dap, 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, Thr-Glu, Cys-Asp, Cys-Lys, Cys-Ser, Cys-Thr, Cys-Orn, Cys-Dab, Cys-Dap, Lys-Lys, Lys-Ser, Lys-Thr, Lys-Orn, Lys-Dab, Lys-Dap, Ser-Lys, Ser-Orn, Ser-Dab, Ser-Dap, Orn-Lys, Orn-Orn, Orn-Ser, Orn-Thr, Orn-Dab, Orn-Dap, Dab-Lys, Dab-Ser, Dab-Thr, Dab-Orn, Dab-Dab, Dab-Dap, Dap-Lys, Dap-Ser, Dap-Thr, Dap-Orn, Dap-Dab, and Dap-Dap. The polar moiety comprises the C-terminus of the amphiphilic peptide and/or peptoid, or the polar moiety comprises the N-terminus of the amphiphilic peptide and/or peptoid. The polar moiety comprises the C-terminus of the amphiphilic peptide and/or peptoid. 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 peptoid, where the size of the aliphatic amino acids is defined as: Ile=Leu greater than Val greater than Ala greater than Gly. 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 arranged in order of decreasing amino acid size have a sequence with a length of 2 to 7, preferably 2 to 6, especially 2 to 5 amino acids. The aliphatic amino acids arranged in an order of decreasing amino acid size have a sequence selected from Leu-Ile-Val-Ala-Gly (SEQ ID No.: not defined), Ile-Leu-Val-Ala-Gly (SEQ ID No.: not defined), Leu-Ile-Val-Ala-Ala (SEQ ID No.: not defined), Leu-Ala-Val-Ala-Gly (SEQ ID No.: not defined), Ile-Val-Ala-Gly (SEQ ID No.: not defined), Leu-Ile-Val-Ala (SEQ ID No.: not defined), Leu-Ile-Val-Gly (SEQ ID No.: not defined), Ile-Val-Ala (SEQ ID No.: not defined) and Ile-Val (SEQ ID No.: not defined), where optionally there is an Ala preceding such sequence at the N-terminus. 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 peptoid. The aliphatic amino acids arranged in order of identical amino acid size have a sequence with a length of 2 to 4 amino acids. The aliphatic amino acids arranged in an order of identical size have a sequence selected from Leu-Leu-Leu-Leu (SEQ ID No.: not defined), Leu-Lue-Leu (SEQ ID No.: not defined), Leu-Leu (SEQ ID No.: not defined), Ile-Ile-Ile-Ile (SEQ ID No.: not defined), Ile-Ile-Ile (SEQ ID No.: not defined), Ile-Ile (SEQ ID No.: not defined), Trp-Trp (SEQ ID No.: not defined), Val-Trp (SEQ ID No.: not defined), Trp (SEQ ID No.: not defined), Ala-Ala-Ala-Ala (SEQ ID No.: not defined), Ala-Ala-Ala (SEQ ID No.: not defined), Ala-Ala (SEQ ID No.: not defined), Gly-Gly-Gly-Gly (SEQ ID No.: not defined), Gly-Gly-Gly (SEQ ID No.: not defined), and Gly-Gly (SEQ ID No.: not defined). The amphiphilic sequence undergoes 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 peptide and/or peptoid, dependent on the ionic environment, pH dependent and/or temperature dependent. The amphiphilic linear sequence comprises a single hydrophilic and at least two aliphatic amino acids. The amphiphilic sequence is one of SEQ ID No. 1 to 18, as available on WIPO website. The C-terminal amino acid of the amphiphilic peptide and/or peptoid is selected from lysine (K), an ornithine (Orn), a 2,4-diaminobutyric acid (Dab) and a 2,4-diaminopropionic acid (Dap).R=H, optionally substituted alkyl, or optionally substituted aryl;R and R'=H, optionally substituted alkyls or optionally substituted aryls.Preferred Hydrogel: The hydrogel further comprises a non-peptidic polymer. The hydrogel comprises fibers of the at least one amphiphilic peptide and/or peptoid, where the fibers define a network that is capable of entrapping at least one of a 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 or a pharmaceutical active compound. The hydrogel comprises at least one of a 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 or a pharmaceutical active compound entrapped by the network of fibers of the amphiphilic peptide and/or peptoid. In the hydrogel, the fibers of the amphiphilic peptide and/or peptoid are coupled to the at least one of a 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 or a pharmaceutical active compound. The hydrogel is provided in an injectable form and gels in situ. The hydrogel in method (M2) comprises at least one amphiphilic peptide and/or peptoid and the hydrogel functions as a hemostatic agent or as an antiinflammatory agent, which acts by scavenging extracellular nucleic acids that stimulate the innate immune system. The hydrogel in method (M2) comprises at least one bioactive therapeutic that diffuses into the wound and facilitate the healing response by modulating the inflammatory response and/or stimulating regenerative processes.    TECHNOLOGY FOCUS - PHARMACEUTICALS - Preferred Components: The at least one of a 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 or a pharmaceutical active compound is coupled to the non-peptidic polymer. The pharmaceutical active compound is selected from hemostatic agents, antibiotics, antimicrobial agents, antifungal agents, antiinflammatory agents, analgesics, anticoagulants, antibodies, antigens, growth factors and cytokines. Preferred Composition: The pharmaceutical and/or cosmetic composition and/or the biomedical device, and/or the electronic devices further comprise a pharmaceutical active compound. The pharmaceutical and/or cosmetic composition further comprises carrier. The composition of peptide is injectable. Preferred Method: The dissolved amphiphilic peptide and/or peptoid in aqueous solution is further exposed to temperature, where the temperature is 20 degrees C to 90 degrees C, preferably 20 degrees C to 70 degrees C. The dissolved amphiphilic peptide and/or peptoid in aqueous solution is exposed to a temperature of 35 degrees C to 40 degrees C. The at least one amphiphilic peptide and/or peptoid is dissolved at a concentration of 0.01 mu g/ml to 100 mg/ml, preferably at a concentration of 1 mg/ml to 50 mg/ml, especially at a concentration of 1 mg/ml to about 20 mg/ml. The method further involves at least one of the steps of: adding at least one bioactive agent; adding at least one non-peptidic polymer; adding at least one gelation enhancer; adding at least one buffer, preferably at least one physiological buffer, where the gelation enhancer is a salt or a solution of a salt or the gelation enhancer is a crosslinking agent. The step of adding at least one non-peptidic polymer further involves mixing or crosslinking the at least one non-peptidic polymer with the at least one amphiphilic peptide and/or peptoid. The method (M1) is performed in vitro or in vivo or ex vivo. When the method (M1) is performed in vivo, in step (a), the hydrogel is provided at a place in the body of a patient where tissue regeneration or tissue replacement is intended. In method (M1), the step (a) is performed by injecting the hydrogel or a solution of at least one amphiphilic peptide and/or peptoid, at a place in the body of a patient where tissue regeneration or tissue replacement is intended. In method (M1), the step (a) further involves the co-injection of a gelation enhancer, preferably of a solution of a salt. When method (M1) is performed ex vivo, in step (a) or (b), 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. In method (M1), the hydrogel comprises at least one bioactive therapeutic that stimulates regenerative processes and/or modulate the immune response. In step (a1), the hydrogel is mixed with cells that repopulate the wound and expedite wound healing. Preferred Kit: In the kit (K1), the aqueous solution of the second container further comprises pharmaceutical active compound. In the kit (K1), the first container with at least one amphiphilic peptide and/or peptoid further comprises a pharmaceutical active compound. The kit of parts (K1) further comprises a third container with a gelation enhancer, where the gelation enhancer is a salt or a solution of a salt. In the kit of parts, at least one of the first, second or third container is provided as a spray bottle or a syringe. In the kit of parts (K2), the first container further comprises a pharmaceutical active compound. In the kit of parts (K2), at least one of the first and the second container is provided as a spray bottle or a syringe. Preferred Definitions:    n=2 to 6, preferably 2 to 5;    m=1-2.    ACTIVITY - Vulnerary; Dermatological; Antiinflammatory; Hemostatic; Immunosuppressive. Hydrogels Ac-LK6 (Ac-Leu-Ile-Val-Ala-Gly-Lys-NH2) and Ac-IK6 (Ac-Ile-Leu-Val-Ala-Gly-Lys-NH2) were evaluated for efficacy in wound healing in rat models. About 10 second exposure, to 1 cm diameter stainless steel rod heated to 100 degrees C in boiling water for 5 minutes, generated consistent mid partial thickness burns on shaved rat dorsum. Three injuries inflicted on each rat were dressed with ultrashort peptide hydrogels and Mepitel (RTM: silicone-coated polyamide net). Polydimethysiloxane supports were used to maintain integrity of soft disc-shaped hydrogels. After positioning dressings, water-proof Tegarderm (RTM: adhesive films), gauze and crepe bandages were used to secure dressings. Histological analysis of skin samples taken at day 7 corroborated completion of autolytic debridement for wounds dressed with peptide hydrogels. The loss of necrotic epidermal layer for burnt area treated with Ac-IK6 and Ac-LK6 hydrogels, was contrasted with remnants of epidermal tissue adhered to the dermis for the wounds dressed with Mepitel. Wound closure was in part facilitated by the rapid onset of autolytic debridement. It was observed that 56.96% and 55.16% wound contracture was observed for Ac-IK6 and Ac-LK6 hydrogels respectively by day 10. In contrast, only 46.67% of the wound area had healed for Mepitel-dressed wounds. By day 14, 85.09% and 92.95% coverage of the burn was achieved for hydrogels, which was dramatically higher than the 62.46% for Mepitel dressings.    MECHANISM OF ACTION - None given.    ADMINISTRATION - The pharmaceutical and/or cosmetic composition is applied topically or is administered orally, transdermally, parenterally (including intramuscularly, subcutaneously, intravenously, by intramedullary injections, intrathecally, intraventricularly, intraperitoneally, intranasally, or by intraocular injection), by spraying, by injection, rectally, transmucosally, or intestinally. No dosage details given.    SPECIFIC PEPTIDES - 24 Sequences are specifically claimed as the amphiphilic peptide and/or peptoid e.g. a peptide having sequence Leu-Ile-Val-Ala-Gly-Lys (SEQ ID No. 19 or 39), a peptide having sequence Leu-Ile-Val-Ala-Gly(Orn) (SEQ ID No. 43 or 44), a peptide having sequence Leu-Ile-Val-Ala-Gly(Dab) (SEQ ID No. 45 or 46), a peptide having sequence Leu-Ile-Val-Ala-Gly(Dap) (SEQ ID No. 47 or 48), and a peptide having sequence Ile-Leu-Val-Ala-Gly-Lys (SEQ ID No. 49 or 50).    EXAMPLE - No suitable example given.