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. Author manuscript; available in PMC: 2024 Dec 6.
Published in final edited form as: Nat Rev Chem. 2020 Sep 15;4(11):615–634. doi: 10.1038/s41570-020-0215-y

Fig. 4. Self-assembling biomimetic-peptide-based antimicrobial nanostructures.

Fig. 4

a | Different peptide-membrane interactions are proposed to give rise to antibacterial functions. b | The MAX1 peptide undergoes environmentally triggered folding, selfassembly and non-covalent fibril-crosslinking processes to give a hydrogel114. c | The supramolecular nanofibres formed by self-assembling peptide amphiphiles present cationic peptide sequences that are essential to their proposed mode of action140. d | Scanning electron micrographs of Escherichia coli with and without diphenylalanine. This dipeptide forms nanostructures that have clear effects on bacterial morphology141. FF, diphenylalanine. Part b adapted from REF.113, Springer Nature Limited. Part c adapted with permission from REF.140, American Chemical Society. Part d adapted from REF.141, CC BY 4.0.