A material-based platform to modulate fibronectin activity and focal adhesion assembly

Frankie A. Vanterpool, Marco Cantini, F. Philipp Seib, Manuel Salmerón-Sánchez

研究成果: Contribution to journalArticle査読

29 被引用数 (Scopus)

抄録

We present a detailed characterization of fibronectin (FN) adsorption and cell adhesion on poly(ethyl acrylate) (PEA) and poly(methyl acrylate) (PMA), two polymers with very similar physicochemical properties and chemical structure, which differ in one single methyl group in the lateral chain of the polymer. The globular solution conformation of FN was retained following adsorption onto PMA, whereas spontaneous organization of FN into protein (nano) networks occurred on PEA. This distinct distribution of FN at the material interface promoted a different availability, measured via monoclonal antibody binding, of two domains that facilitated integrin binding to FN: FNIII10 (RGD sequence) and FNIII9 (PHSRN synergy sequence). The enhanced exposure of the synergy domain on PEA compared to PMA triggered different focal adhesion assemblies: L929 fibroblasts showed a higher fraction of smaller focal plaques on PMA (40%) than on PEA (20%). Blocking experiments with monoclonal antibodies against FNIII10 (HFN7.1) and FNIII9 (mAb1937) confirmed the ability of these polymeric substrates to modulate FN conformation. Overall, we propose a simple and versatile material platform that can be used to tune the presentation of a main extracellular matrix protein (FN) to cells, for applications than span from tissue engineering to disease biology.

本文言語英語
ページ(範囲)286-296
ページ数11
ジャーナルBioResearch Open Access
3
6
DOI
出版ステータス出版済み - 12 1 2014

All Science Journal Classification (ASJC) codes

  • 生化学、遺伝学、分子生物学(全般)

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