抗体功能化原子力显微镜探针检测嵌段共聚物表面的蛋白质构象变化。
Protein conformation changes on block copolymer surfaces detected by antibody-functionalized atomic force microscope tips.
机构信息
Nanoprobe Laboratory for Bio- & Nanotechnology and Biomimetics, The Ohio State University, Columbus, Ohio 43210, USA.
出版信息
J Biomed Mater Res A. 2012 Jan;100(1):18-25. doi: 10.1002/jbm.a.33219. Epub 2011 Oct 4.
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.
摘要
使用抗体功能化原子力显微镜 (AFM) 探针检测了沉积在具有相同化学成分的聚甲基丙烯酸甲酯和聚丙烯酸嵌段共聚物上的纤维连接蛋白 (Fn) 的构象变化。基于抗体-蛋白质粘附力图谱和相成像，发现三嵌段共聚物的纳米形态有利于 Fn 中精氨酸-甘氨酸-天冬氨酸 (RGD) 基团的暴露。首次使用 X 射线光电子能谱阐明了表面化学成分并证实了 AFM 的结果。研究结果表明，嵌段共聚物纳米形态可用于调节蛋白质构象并可能影响细胞反应。
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