Impact of coverage and guest residue on polyproline II helix peptide antifouling

Polyproline II (PPII) peptide sequences are recognized as promising biomaterials because of their attractive antifouling properties. However, the mechanisms behind their antifouling behavior have not been fully characterized. In this work we show that PPII peptide coverage, controlled by adsorption time, significantly reduces the fouling of bovine serum albumin (BSA, a model foulant). In addition, guest residues introduced into the PPII sequence are shown to significantly impact BSA adsorption as well as human mesenchymal stem cell (hMSC) spreading. This research will help guide future PPII peptide designs for incorporation into novel biomaterials.

Graphical abstract: A guest residue system was utilized to understand properties that impact the ability of polyproline II helix peptide monolayers to resist the fouling of BSA and influence human mesenchymal cell spreading.

Supplementary information: The online version contains supplementary material available at 10.1557/s43579-024-00674-w.