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

Abshar Hasan, Kyueui Lee, Kunal Tewari, Lalit M. Pandey, Phillip B. Messersmith, Karen Faulds, Michelle MacLean, King Hang Aaron Lau

Research output: Contribution to journalArticlepeer-review

19 Citations (Scopus)
15 Downloads (Pure)


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.
Original languageEnglish
Pages (from-to)5789-5793
Number of pages5
JournalChemistry - A European Journal
Issue number26
Early online date14 Feb 2020
Publication statusPublished - 7 May 2020


  • biointerfaces
  • antimicrobial peptides
  • peptidomimetics
  • peptoids
  • bacterial attachment
  • click chemistry


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