Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/141498
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dc.contributor.authorLi, Chuanxien_US
dc.contributor.authorLiu, Chunjiangen_US
dc.contributor.authorLi, Minglunen_US
dc.contributor.authorXu, Xinen_US
dc.contributor.authorLi, Shuzhouen_US
dc.contributor.authorQi, Weien_US
dc.contributor.authorSu, Rongxinen_US
dc.contributor.authorYu, Jingen_US
dc.date.accessioned2020-06-09T01:42:14Z-
dc.date.available2020-06-09T01:42:14Z-
dc.date.issued2020-
dc.identifier.citationLi, C. Liu, C., Li, M., Xu, X., Li, S., Qi, W., . . . Yu, J. (2020). Structures and antifouling properties of self-assembled zwitterionic peptide monolayers : effects of peptide charge distributions and divalent Cations. Biomacromolecules, 21(6), 2087-2095. doi:10.1021/acs.biomac.0c00062en_US
dc.identifier.issn1525-7797en_US
dc.identifier.urihttps://hdl.handle.net/10356/141498-
dc.description.abstractZwitterionic peptides are great candidates as antifouling coating materials in many biomedical applications. We investigated the structure and antifouling properties of surface-tethered zwitterionic peptide monolayers with different peptide chain lengths and charge distributions using a combination of surface plasma resonance, atomic force microscopy, and all atomistic molecular dynamics (MD) simulation techniques. Our results demonstrate that zwitterionic peptides with more zwitterionic lysine (K) and glutamic acid (E) repeating units exhibit better antifouling performance. The block charge distributions of the positive and negative charges in the peptides (having multiple positive charges next to the same amount of negative charges), although affecting the structure of the peptide molecules, do not significantly change the antifouling properties of the peptide monolayers in the solutions containing monovalent ions. However, divalent cations, Ca2+ and Mg2+, in solution can significantly alter the structure and lower the antifouling performance of the zwitterionic peptide monolayers, especially with the sequences of block charges. All atomistic MD simulations quantitatively reveal that the divalent cations in solution lead to more interchain electrostatic cross-links between peptide chains, especially for peptides with block charges, which causes dehydration of the zwitterionic peptides and diminishes their antifouling performances.en_US
dc.description.sponsorshipNRF (Natl Research Foundation, S’pore)en_US
dc.description.sponsorshipMOE (Min. of Education, S’pore)en_US
dc.language.isoenen_US
dc.relation.ispartofBiomacromoleculesen_US
dc.rightsThis document is the Accepted Manuscript version of a Published Work that appeared in final form in Biomacromolecules, copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see https://doi.org/10.1021/acs.biomac.0c00062en_US
dc.subjectEngineering::Materialsen_US
dc.titleStructures and antifouling properties of self-assembled zwitterionic peptide monolayers : effects of peptide charge distributions and divalent cationsen_US
dc.typeJournal Articleen
dc.contributor.schoolSchool of Materials Science and Engineeringen_US
dc.identifier.doi10.1021/acs.biomac.0c00062-
dc.description.versionAccepted versionen_US
dc.identifier.pmid32267674-
dc.identifier.issue6en_US
dc.identifier.volume21en_US
dc.identifier.spage2087en_US
dc.identifier.epage2095en_US
dc.subject.keywordsPeptides and Proteinsen_US
dc.subject.keywordsAntifoulingen_US
item.grantfulltextopen-
item.fulltextWith Fulltext-
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