Block copolymer arrangement and composition effects on protein conformation using atomic force microscope-based antigen-antibody adhesion.

Block copolymer arrangement and composition effects on protein conformation using atomic force microscope-based antigen-antibody adhesion.
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DOI:
10.1002/jbm.a.34033
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发表时间:
2012-04
影响因子:
4.9
通讯作者:
Bhushan, B.
Bhushan, B.
中科院分区:
工程技术3区
文献类型:
--
作者:
Palacio, M. L. B.;Schricker, S. R.;Bhushan, B.

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The conformational changes of fibronectin deposited on various block copolymers where one block is composed of poly(methyl methacrylate) (PMMA) and the other block is either poly(acrylic acid) (PAA) or poly(2-hydroxyethyl methacrylate) (PHEMA) were investigated using a functionalized atomic force microscope (AFM) tip. The tip was modified with an antibody sensitive to the exposure of the arginine-glycine-aspartic acid (RGD) groups in fibronectin. By studying the adhesive interactions between the antibody and the proteins adsorbed on the block copolymer surface and phase imaging, it was found that the triblock copolymers PAA-b-PMMA-b-PAA and PMMA-b-PHEMA-b-PMMA, which both have large domain sizes, are conducive to the exposure of the fibronectin RGD groups on the surface. Based on these results, it is concluded that the surface chemistry as well as the nanomorphology dictated by the block copolymer arrangement could both tune protein conformation and orientation and optimize cell adhesion to the biomaterial surface.
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