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Characterization of chemoselective surface attachment of the cationic peptide melimine and its effects on antimicrobial activity

Paper ID Volume ID Publish Year Pages File Format Full-Text
353 38 2012 9 PDF Available
Title
Characterization of chemoselective surface attachment of the cationic peptide melimine and its effects on antimicrobial activity
Abstract

Antimicrobial peptides (AMPs) are promising alternatives to current treatments for bacterial infections. However, our understanding of the structural–functional relationship of tethered AMPs still requires further investigation to establish a general approach for obtaining consistent antimicrobial surfaces. In this study, we have systematically examined the effects of surface orientation of a broad-spectrum synthetic cationic peptide, melimine, on its antibacterial activity against Gram-positive and Gram-negative bacteria. The attachment of melimine to maleimide-functionalized glass was facilitated by addition of a single cysteine amino acid into the peptide sequence at the N-terminus (CysN) or C-terminus (CysC), or at position 13 (Cys13, approximately central). The successful attachment of the modified melimine was monitored using X-ray photoelectron spectroscopy and time-of-flight secondary ion mass spectrometry (ToF-SIMS) with principle component analysis. The ToF-SIMS analysis clearly demonstrated structural difference between the three orientations. The peptide density for the modified surfaces was found to be between 3.5–4.0 × 10−9 mol cm−2 using a modified Bradford assay. The ability of the surfaces to resist Pseudomonas aeruginosa and Staphylococcus aureus colonization was compared using fluorescence confocal microscopy. Reductions in total P. aeruginosa and S. aureus adhesion of 70% (p < 0.001) and 83% (p < 0.001), respectively, after 48 h were observed for the melimine samples when compared to the blank control. We found that melimine attached via the N-terminus was the most effective in reducing total bacterial adhesion and bacterial viability with two- and four times (p < 0.001) more activity than melimine attached via the C-terminus for P. aeruginosa and S. aureus, respectively. Furthermore, for Cys13, despite having the highest measured peptide density of the three surfaces, the higher concentration did not confer the greatest antibacterial effect. This highlights the importance of orientation of the peptides on the surface to efficacy. Our results suggest that the optimal orientation of the cationic residues is essential for maximum surface activity, whereby the optimal activity is obtained when the cationic portion is more available to interact with colonizing bacteria.

Keywords
Antimicrobial; Bacterial adhesion; Biofilm; Peptide; SIMS
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Characterization of chemoselective surface attachment of the cationic peptide melimine and its effects on antimicrobial activity
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Publisher
Database: Elsevier - ScienceDirect
Journal: Acta Biomaterialia - Volume 8, Issue 12, December 2012, Pages 4371–4379
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us