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Zwitterionic Polypeptoids: A Promising Class of Antifouling Bioinspired Materials.

ABSTRACT: Biofouling caused by protein adsorption and microbial colonization remains a great challenge in many applications. In this work, we synthesized a new type of zwitterionic polypeptoid containing carboxybetaine (CB) moieties (PeptoidCB) through thiol-ene chemistry of poly(N-allylglycine) (PNAG). The zwitterionic antifouling hydrogel was subsequently prepared by co-mixing PeptoidCB with agarose, which exhibited excellent resistance to non-specific protein adsorption and bacterial adhesion. Further, PeptoidCB-modified block copolypeptoids with amphiphilic structure were synthesized to form nanoparticles in an aqueous solution with neglected protein adsorption. The ability of PeptoidCB to resist non-specific protein adsorption and bacterial adhesion makes it a promising candidate for biomedical and industrial applications.

SUBMITTER: Ding J

PROVIDER: S-EPMC9267628 | biostudies-literature | 2022 Jun

REPOSITORIES: biostudies-literature

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Zwitterionic Polypeptoids: A Promising Class of Antifouling Bioinspired Materials.

Ding Jian J Ding Xiangmin X Sun Jing J

Materials (Basel, Switzerland) 20220626 13

Biofouling caused by protein adsorption and microbial colonization remains a great challenge in many applications. In this work, we synthesized a new type of zwitterionic polypeptoid containing carboxybetaine (CB) moieties (PeptoidCB) through thiol-ene chemistry of poly(N-allylglycine) (PNAG). The zwitterionic antifouling hydrogel was subsequently prepared by co-mixing PeptoidCB with agarose, which exhibited excellent resistance to non-specific protein adsorption and bacterial adhesion. Further, ...[more]

PMID: 35806622

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Project description:Polypeptoid-coated surfaces and many surface-grafted hydrophilic polymer brushes have been proven efficient in antifouling-the prevention of nonspecific biomolecular adsorption and cell attachment. Protein adsorption, in particular, is known to mediate subsequent cell-surface interactions. However, the detailed antifouling mechanism of polypeptoid and other polymer brush coatings at the molecular level is not well understood. Moreover, most adsorption studies focus only on measuring a single adsorbed mass value, and few techniques are capable of characterizing the hydrated in situ layer structure of either the antifouling coating or adsorbed proteins. In this study, interfacial assembly of polypeptoid brushes with different chain lengths has been investigated in situ using neutron reflection (NR). Consistent with past simulation results, NR revealed a common two-step structure for grafted polypeptoids consisting of a dense inner region that included a mussel adhesive-inspired oligopeptide for grafting polypeptoid chains and a highly hydrated upper region with very low polymer density (molecular brush). Protein adsorption was studied with human serum albumin (HSA) and fibrinogen (FIB), two common serum proteins of different sizes but similar isoelectric points (IEPs). In contrast to controls, we observed higher resistance by grafted polypeptoid against adsorption of the larger FIB, especially for longer chain lengths. Changing the pH to close to the IEPs of the proteins, which generally promotes adsorption, also did not significantly affect the antifouling effect against FIB, which was corroborated by atomic force microscopy imaging. Moreover, NR enabled characterization of the in situ hydrated layer structures of the polypeptoids together with proteins adsorbed under selected conditions. While adsorption on bare SiO2 controls resulted in surface-induced protein denaturation, this was not observed on polypeptoids. Our current results therefore highlight the detailed in situ view that NR may provide for characterizing protein adsorption on polymer brushes as well as the excellent antifouling behavior of polypeptoids.

Dataset Information

Zwitterionic Polypeptoids: A Promising Class of Antifouling Bioinspired Materials.

Publications

Zwitterionic Polypeptoids: A Promising Class of Antifouling Bioinspired Materials.

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