Surface chemistry modulates fibronectin conformation and directs integrin binding and specificity to control cell adhesion
Georgia Institute of Technology
Indexed incrossrefpubmed
Abstract
Integrin-mediated cell adhesion to proteins adsorbed onto synthetic surfaces anchors cells and triggers signals that direct cell function. In the case of fibronectin (Fn), adsorption onto substrates of varying properties alters its conformation/structure and its ability to support cell adhesion. In the present study, self-assembled monolayers (SAMs) of alkanethiols on gold were used as model surfaces to investigate the effects of surface chemistry on Fn adsorption, integrin binding, and cell adhesion. SAMs presenting terminal CH(3), OH, COOH, and NH(2) functionalities modulated adsorbed Fn conformation as determined through differences in the binding affinities of monoclonal antibodies raised against the…
Citation impact
919
total citations
- FWCI
- 18.95
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- 100%
- References
- 63
Citations per year
Authors
3Topics & keywords
Topics
Keywords
- Integrin
- Fibronectin
- Adhesion
- Cell adhesion
- Chemistry
- Biophysics
- Adsorption
- Binding site
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