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Covalent Immobilization of Proteins for the Single Molecule Force Spectroscopy
Published on: August 20, 2018
Block copolymer arrangement and composition effects on protein conformation using atomic force microscope-based
M L B Palacio1, S R Schricker, B Bhushan
1Nanoprobe Laboratory for Bio- & Nanotechnology and Biomimetics, The Ohio State University, Columbus, Ohio 43210, USA.
Journal of Biomedical Materials Research. Part A
|January 27, 2012
Summary
Researchers studied how fibronectin (FN) changes shape on block copolymers. Large domain triblock copolymers promote the exposure of FN
Area of Science:
- Biomaterials Science
- Surface Chemistry
- Polymer Science
Background:
- Fibronectin (FN) is a crucial extracellular matrix protein involved in cell adhesion.
- Understanding protein conformation on biomaterials is key to controlling cell behavior.
- Block copolymers offer tunable surface properties for biomaterial applications.
Purpose of the Study:
- To investigate the conformational changes of fibronectin (FN) on poly(methyl methacrylate) (PMMA) based block copolymers.
- To determine how surface chemistry and nanomorphology influence FN conformation and RGD group exposure.
Main Methods:
- Utilized a functionalized atomic force microscope (AFM) tip with an antibody specific to the arginine-glycine-aspartic acid (RGD) epitope of FN.
- Analyzed adhesive interactions between the antibody and adsorbed FN.
- Employed phase imaging to correlate surface nanomorphology with protein conformation.
Main Results:
- Triblock copolymers with large domain sizes, specifically PAA-b-PMMA-b-PAA and PMMA-b-PHEMA-b-PMMA, significantly enhanced the exposure of FN's RGD groups.
- Surface chemistry and nanomorphology independently and collectively influence FN conformation.
- Protein orientation and RGD exposure were modulated by the block copolymer architecture.
Conclusions:
- Surface chemistry and nanomorphology of block copolymers can be engineered to control fibronectin conformation.
- Optimized block copolymer arrangements promote RGD exposure, potentially enhancing cell adhesion.
- This study provides insights into designing biomaterials with tailored protein interactions for improved biocompatibility.
