Journal
ACTA BIOMATERIALIA
Volume 9, Issue 4, Pages 6236-6244Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.actbio.2012.11.026
Keywords
Peptide; Biofilm formation; Protease resistance; Stainless steel; Electron work function
Funding
- Natural Sciences and Engineering Research Council of Canada
- [AUT021]
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Three protease-resistant bioorganic 304 stainless steel surfaces were created through the reaction of synthetic peptides consisting of the D-enantiomeric isomer (D-K122-4), the retro-inverso D-enantiomeric isomer (RI-K122-4), and a combination of the two peptides (D + RI) of the Pseudomonas aeruginosa PilA receptor binding domain with steel surfaces. The peptides used to produce the new materials differ only in handedness of their three-dimensional structure, but they reacted with the steel to yield materials that differed in their surface electron work function (EWF) while displaying an identical chemical composition and equivalent surface adhesive force properties. These surfaces allowed for an assessment of the relative role of surface EWF in initial biofilm formation. We examined the ability of various bacteria (selected strains of Listeria monogtogenes, L. innocua, Staphylococcus aureus and S. epidermidis) to initiate biofilm formation. The D-K1224 generated surface displayed the lowest EWF (classically associated with greater molecular interactions and more extensive biofilm formation) but was observed to be least effectively colonized by bacteria (>50% decrease in bacterial adherence of all strains). The highest surface EWF with the lowest surface free energy (RI-K122-4 generated) was more extensively colonized by bacteria, with the binding of some strains being equivalent to unmodified steel. The D + RI generated surface was least effective in minimizing biofilm formation, where some strains displayed enhanced bacterial colonization. Fluorescent microscopy revealed that the D and RI peptides displayed similar but clearly different binding patterns, suggesting that the peptides recognized different sites on the steel, and that differential binding of the peptides to the steel surfaces influences the binding of different bacterial strains and species. We have demonstrated that stainless steel surfaces can be easily modified by peptides to generate surfaces with new physiochemical properties. The D-K122-4-modified surface substantially decreases biofilm formation compared to the RI-K122-4 and D + RI surfaces. (C) 2012 Acta Materialia Inc. Published by Elsevier Ltd. All rights reserved.
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