Journal
CHEMISTRY-A EUROPEAN JOURNAL
Volume 26, Issue 26, Pages 5789-5793Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/chem.202000746
Keywords
antimicrobial peptides; bacterial attachment; biointerfaces; click chemistry; peptoids
Categories
Funding
- Commonwealth Scholarship Commission for a Split Site award [INCN-2017-50]
- EPSRC [EP/N010914/1]
- Stewart fund at Strathclyde PAC
- Tenovus Scotland [S15/29]
- BBSRC [BB/R00899X/1]
- BBSRC [BB/R00899X/1] Funding Source: UKRI
- EPSRC [EP/N010914/1] Funding Source: UKRI
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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 strategy 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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