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The Role of Hydrogen Bonding in Peptoid-Based Marine Antifouling Coatings

Barry, Mikayla E., Davidson, Emily C., Zhang, Chengcheng, Patterson, Anastasia L., Yu, Beihang, Leonardi, Amanda K., Duzen, Nilay, Malaviya, Ketaki, Clarke, Jessica L., Finlay, John A., Clare, Anthony S., Chen, Zhan, Ober, Christopher K., Segalman, Rachel A.
Macromolecules 2019 v.52 no.3 pp. 1287-1295
N-substituted glycines, Navicula, Ulva, adhesion, algae, antifouling activities, antifouling agents, bioassays, coatings, fouling, hydrogen bonding, moieties, peptides, polymers, spectroscopy
The benefits of incorporating amphiphilic properties into antifouling and fouling-release coatings are well-established. The use of sequence-defined peptides and peptoids in these coatings allows precise control over the spacing and chemistry of the amphiphilic groups, but amphiphilic peptoids have generally outperformed analogous peptides for reasons attributed to differences in backbone structure. The present work demonstrates that the superior properties of peptoids relative to peptides are primarily attributable to a lack of hydrogen bond donors rather than to their secondary structure. A new amphiphilic peptoid was designed containing functional groups similar to those typically found on a hydrogen-bonding peptide backbone. This peptoid and a non-hydrogen-bonding peptoid analogue were incorporated as side chains in PDMS-based polymer scaffolds. Bioassays with the soft algal fouling organisms Ulva linza and Navicula incerta indicate that hydrogen bonding largely determines the differences seen between similar peptide and peptoid species, while sum frequency generation vibrational spectroscopy suggests that the presence of hydrogen bond donors enhances interfacial water structuring. This reduced initial U. linza adhesion, but attached algae were more strongly bound by hydrogen-bonding interactions. Consequently, amphiphilic peptoid materials lacking hydrogen bond donors are better suited to resist marine fouling, with enhanced release of U. linza and similar performance against N. incerta relative to hydrogen-bonding analogues.