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. 2021 Aug 24;17(35):8001–8021. doi: 10.1039/d1sm00839k

Fig. 3. Examples of peptide hydrogel systems (ai) mechanism of folding and self-assembly for MAX1 β-hairpin hydrogel formation. Resulting gels are self-supporting as image at far right shows. (aii) Sequence of MAX1 β-hairpin. Adapted with permission from ref. 42. Copyright (2007) American Chemical Society. (b) Chemical Structures of the lipids and surfactant like peptides used to form the vesicle shown. Adapted with permission from ref. 48. Copyright (2018) American Chemical Society. (c) Chemical structure of an ultrashort peptide composed of a naphthalene (Nap) protecting group and a diphenylalanine (FF) peptide chain. (d) Colour-coded chemical structure of a multidomain peptide that can be designed to contain variable numbers of lysine residues and (QL) repeating units for the investigation of both molecular and supramolecular structure-dependent cytotoxicity and antimicrobial activity. Red: leucine; green: glutamine; grey: lysine. Adapted from with permission from ref. 45, The Royal Society of Chemistry.

Fig. 3