Turning a Killing Mechanism into an Adhesion and Antifouling Advantage

  Peptides that bind to a polymer Copyright: © Adv. Mater. Interfaces A bacterial killing mechanism based on amphiphilic antimicrobial peptides is turned into an adhesion advantage. Liquid chromatography peak I (LCI) peptide is exploited to achieve irreversible binding of a protein-peptide hybrid to polymeric surfaces.

The introduction of functionalities on polymeric surfaces remains a challenge. We exploited a bacterial killing mechanism based on amphiphilic antimicrobial peptides to introduce antifouling properties on diverse materials, which are applied in e.g. medical sectors. A protein polymer-hybrid consisting of two building blocks was generated: a surface affine block, the antimicrobial peptide LCI, and a functional block consisting of enhanced green fluorescent protein from which the different antifouling polymer chains poly-carboxybetaine methacrylamide or poly-N‐(2‐hydroxypropyl) methacrylamide were grafted. The protein-polymer hybrids attached to diverse natural and artificial surfaces ranging from e.g. hair and teeth to polystyrene, poly-4‐methyl‐1‐pentene, and polydimethylsiloxane. Binding kinetics and antifouling properties of the protein-polymer hybrids were determined by surface plasmon resonance spectroscopy on a gold surface. Notably, the fusion protein modified with poly-N‐(2‐hydroxypropyl) methacrylamide completely prevented the fouling from human blood plasma on the target surface. With this newly developed strategy, it is possible to achieve antifouling properties on natural and artificial materials.

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Dedisch, S.*, Obstals, F.*, de los Santos Pereira, A., Bruns, M., Jakob, F., Schwaneberg, U., Rodriguez‐Emmenegger, C. 2019, Adv. Mater. Interfaces 6(18): 1900847; DOI: 10.1002/admi.201900847 * shared co-authorship.