Protein conformation changes on block copolymer surfaces detected by antibody-functionalized atomic force microscope tips

Authors

  • Manuel L. B. Palacio,

    1. Nanoprobe Laboratory for Bio- & Nanotechnology and Biomimetics, The Ohio State University, Columbus, Ohio 43210
    Search for more papers by this author
  • Scott R. Schricker,

    1. Restorative and Prosthetic Dentistry Section, College of Dentistry, The Ohio State University, Columbus, Ohio 43210
    Search for more papers by this author
  • Bharat Bhushan

    Corresponding author
    1. Nanoprobe Laboratory for Bio- & Nanotechnology and Biomimetics, The Ohio State University, Columbus, Ohio 43210
    • Nanoprobe Laboratory for Bio- and Nanotechnology and Biomimetics, The Ohio State University, Columbus, OH 43210, USA
    Search for more papers by this author

  • How to cite this article: Palacio MLB, Schricker SR, Bhushan B. 2012. Protein conformation changes on block copolymer surfaces detected by antibody-functionalized atomic force microscope tips. J Biomed Mater Res Part A2012:100A:18–25.

Abstract

Conformational changes of fibronectin (Fn) deposited on poly(methyl methacrylate) and poly(acrylic acid) block copolymers with identical chemical compositions were detected using an antibody-functionalized atomic force microscope (AFM) tip. Based on the antibody-protein adhesive force maps and phase imaging, it was found that the nanomorphology of the triblock copolymer is conducive to the exposure of the arginine-glycine-aspartic acid (RGD) groups in Fn. For the first time, X-ray photoelectron spectroscopy was used to elucidate surface chemical composition and confirm AFM results. The findings demonstrate that block copolymer nanomorphology can be used to regulate protein conformation and potentially cellular response. © 2011 Wiley Periodicals, Inc. J Biomed Mater Res Part A:, 2012.

Ancillary