Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/152733
Title: Effect of hydrophobicity and charge separation on the antifouling properties of surface-tethered zwitterionic peptides
Authors: Li, Chuanxi
Li, Minglun
Qi, Wei
Su, Rongxin
Yu, Jing
Keywords: Science::Chemistry::Biochemistry
Issue Date: 2021
Source: Li, C., Li, M., Qi, W., Su, R. & Yu, J. (2021). Effect of hydrophobicity and charge separation on the antifouling properties of surface-tethered zwitterionic peptides. Langmuir, 37(28), 8455-8462. https://dx.doi.org/10.1021/acs.langmuir.1c00803
Project: RG7/19
NRF-NRFF11-2019-0004
Journal: Langmuir 
Abstract: Zwitterionic peptides emerge as a class of highly effective antifouling materials in a wide range of applications such as biosensor, biomedical devices, and implants. We incorporated neutral amino acid spacers with different hydrophobicities, including serine (Ser), glycine (Gly), and leucine (Leu), into zwitterionic peptides with KE repeating units and investigated the structure and antifouling performance of the zwitterionic peptide brushes using surface plasma resonance (SPR), surface force apparatus (SFA), and all atomistic molecular dynamics (MD) simulation techniques. Our results demonstrate that the hydrophilicity of neutral spacers alters the structure and antifouling performance of the peptide-modified surface. Hydrophilic Ser inserted peptides reduced the interaction between the peptide monolayer and protein foulants while hydrophobic Leu significantly increased the protein adhesion. SFA force measurements shows that the presence of more spacers would increase the adhesion between the peptide monolayer and the modeling foulant lysozyme, especially for the hydrophobic spacers. MD simulations reveal that hydrophilic Ser spacers retain the hydrophilicity of the peptide monolayer and improve the antifouling performance, and Gly spacers give rise to more inter-chain crosslinks. Leu spacers result in a more hydrophobic peptide monolayer which lead to dehydration of the peptide monolayer and reduces the antifouling performances.
URI: https://hdl.handle.net/10356/152733
ISSN: 0743-7463
DOI: 10.1021/acs.langmuir.1c00803
Rights: This document is the Accepted Manuscript version of a Published Work that appeared in final form in Langmuir, 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/http://doi.org/10.1021/acs.langmuir.1c00803.
Fulltext Permission: embargo_20220727
Fulltext Availability: With Fulltext
Appears in Collections:MSE Journal Articles

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