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Surface Design for Immobilization of an Antimicrobial Peptide Mimic for Efficient Anti-Biofouling.

Published on Feb 14, 2020in Chemistry: A European Journal5.16
· DOI :10.1002/CHEM.202000746
Abshar Hasan12
Estimated H-index: 12
(University of Strathclyde),
Kyueui Lee6
Estimated H-index: 6
(University of California, Berkeley)
+ 5 AuthorsKing Hang Aaron Lau20
Estimated H-index: 20
(University of Strathclyde)
Abstract
Microbial surface attachment negatively impacts a wide range of devices from water purification membranes to biomedical implants. Mimics of antimicrobial peptides (AMPs) constituted from poly(N‐substituted glycine) “peptoids” are of great interest as they resist proteolysis and can inhibit a wide spectrum of microbes. We investigate how terminal modification of a peptoid AMP‐mimic and its surface immobilization affect antimicrobial activity. We also demonstrate a convenient surface modification scheme for enabling alkyne‐azide “click” coupling on amino‐functionalized surfaces. Our results verified that the N‐ and C‐terminal peptoid structures are not required for antimicrobial activity. Moreover, our peptoid immobilization density and choice of PEG tether resulted in a “volumetric” spatial separation between AMPs that, compared to past studies, enabled the highest AMP surface activity relative to bacterial attachment. Our analysis suggests the importance of spatial flexibility for membrane activity and that AMP separation may be a controlling parameter for optimizing surface anti‐biofouling.
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Poly(N-substituted glycine) “peptoids” are an interesting class of peptidomimics that can resist proteolysis and mimic naturally found antimicrobial peptides (AMPs), which exhibit wide spectrum activity against bacteria. This work investigates the possibility of modifying peptoid AMP mimics (AMPMs) with aliphatic lipid “tails” to generate “lipopeptoids” that can assemble into micellar nanostructures, and evaluates their antimicrobial activities. Two families of AMPMs with different distributions...
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