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Block copolymer arrangement and composition effects on protein conformation using atomic force microscope‐based antigen–antibody adhesion
Author(s) -
Palacio M. L. B.,
Schricker S. R.,
Bhushan B.
Publication year - 2012
Publication title -
journal of biomedical materials research part a
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.849
H-Index - 150
eISSN - 1552-4965
pISSN - 1549-3296
DOI - 10.1002/jbm.a.34033
Subject(s) - copolymer , materials science , adhesion , methacrylate , acrylic acid , polymer chemistry , methyl methacrylate , protein adsorption , surface modification , chemical engineering , polymer , composite material , engineering
The conformational changes of fibronectin (FN) 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 FN. 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 FN RGD groups on the surface. On the basis of 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. © 2012 Wiley Periodicals, Inc. J Biomed Mater Res Part A:, 2012.