Issue 45, 2012

Protein resistant properties of polymers with different branched architecture on a gold surface

Abstract

To elucidate the effect of polymeric branched architecture on the protein resistant properties, the protein adsorption behaviour of polymers with different branched architectures on a gold surface was investigated. A series of poly((S-(4-vinyl) benzyl S′-propyltrithiocarbonate)-co-(poly(ethylene glycol) methacrylate))s (poly(VBPT-co-PEGMA)s) with different branched architecture were prepared by reversible addition-fragmentation chain transfer (RAFT) copolymerization, and then grafted onto a gold surface via thiols obtained from aminolysis reaction. With the increase of polymeric branched architecture, the thiol content of poly(VBPT-co-PEGMA)s increased, resulting in the formation of a highly uniform film with high stability and multifunctionality on the gold substrate. On the other hand, incubation of the poly(VBPT-co-PEGMA)-coated surface with bovine serum albumin (BSA) and immunoglobulin (IgG) showed that the protein resistant properties of the polymer-coated surface were enhanced with the decrease of branched architecture. After surface coating with branched poly(VBPT-co-PEGMA) onto a gold surface, the adhesion and proliferation of Hela cells were inhibited efficiently. By only adjusting the branched architecture of polymers on a substrate, the high protein resistance and multifunctionality can be integrated together, realizing the optimization of nonfouling properties of polymer-coated surface.

Graphical abstract: Protein resistant properties of polymers with different branched architecture on a gold surface

Supplementary files

Article information

Article type
Paper
Submitted
03 Jul 2012
Accepted
24 Sep 2012
First published
25 Sep 2012

J. Mater. Chem., 2012,22, 23852-23860

Protein resistant properties of polymers with different branched architecture on a gold surface

Y. Zhuang, Q. Zhu, C. Tu, D. Wang, J. Wu, Y. Xia, G. Tong, L. He, B. Zhu, D. Yan and X. Zhu, J. Mater. Chem., 2012, 22, 23852 DOI: 10.1039/C2JM34306A

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