Document Type
Article
Publication Date
11-11-2024
Abstract
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.
Keywords
adhesion, adsorption, biomaterial, coating, surface chemistry
Language
English
Publication Title
MRS Communications
Grant
2026259
Rights
© The Author(s) 2024. This is an Open Access work distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/) which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Creative Commons License
This work is licensed under a Creative Commons Attribution 4.0 International License.
Recommended Citation
Ahn, R.S., Grome, H.T., Asaei, S. et al. Impact of coverage and guest residue on polyproline II helix peptide antifouling. MRS Communications 14, 1134–1141 (2024). https://doi.org/10.1557/s43579-024-00674-w
Manuscript Version
Final Publisher Version