Surface design for immobilization of an antimicrobial peptide mimic for efficient anti‐biofouling

Hasan, Abshar and Lee, Kyueui and Tewari, Kunal and Pandey, Lalit M. and Messersmith, Phillip B. and Faulds, Karen and MacLean, Michelle and Lau, King Hang Aaron (2020) Surface design for immobilization of an antimicrobial peptide mimic for efficient anti‐biofouling. Chemistry - A European Journal, 26 (26). pp. 5789-5793. ISSN 1521-3765 (https://doi.org/10.1002/chem.202000746)

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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.

ORCID iDs

Hasan, Abshar, Lee, Kyueui, Tewari, Kunal, Pandey, Lalit M., Messersmith, Phillip B., Faulds, Karen ORCID logoORCID: https://orcid.org/0000-0002-5567-7399, MacLean, Michelle ORCID logoORCID: https://orcid.org/0000-0001-5750-0397 and Lau, King Hang Aaron ORCID logoORCID: https://orcid.org/0000-0003-3676-9228;
CORE (COnnecting REpositories)