Antibacterial Gel Coatings Inspired by the Cryptic Function of a Mussel Byssal Peptide

Galit Fichman, Caroline Andrews, Nimit L. Patel, Joel P. Schneider*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

48 Scopus citations

Abstract

Although the adhesive and cohesive nature of mussel byssal proteins have long served to inspire the design of materials embodying these properties, their characteristic amino acid compositions suggest that they might also serve to inspire an unrelated material function not yet associated with this class of protein. Herein, it is demonstrated that a peptide derived from mussel foot protein-5, a key protein in mussel adhesion, displays antibacterial properties, a yet unreported activity. This cryptic function serves as inspiration for the design of a new class of peptide-based antibacterial adhesive hydrogels prepared via self-assembly, which are active against drug-resistant Gram-positive bacteria. The gels exert two mechanisms of action, surface-contact membrane disruption and oxidative killing affected by material-produced H2O2. Detailed studies relating amino acid composition and sequence to material mechanical adhesion/cohesion and antibacterial activity affords the MIKA2 adhesive gel, a material with a superior activity that is shown to inhibit colonization of titanium implants in mice.

Original languageAmerican English
Article number2103677
JournalAdvanced Materials
Volume33
Issue number40
DOIs
StatePublished - 7 Oct 2021
Externally publishedYes

Bibliographical note

Publisher Copyright:
© 2021 Wiley-VCH GmbH. This article has been contributed to by US Government employees and their work is in the public domain in the USA

Keywords

  • antibacterial
  • bioinspired
  • hydrogels
  • peptides
  • self-assembly

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