Surface chemistry modulates fibronectin conformation and directs integrin binding and specificity to control cell adhesion
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 central cell-binding domain (OH > COOH = NH(2) > CH(3)). Binding of alpha(5)beta(1) integrin to adsorbed Fn was controlled by SAM surface chemistry in a manner consistent with antibody binding (OH > COOH = NH(2) > CH(3)), whereas alpha(V) integrin binding followed the trend: COOH >> OH = NH(2) = CH(3), demonstrating alpha(5)beta(1) integrin specificity for Fn adsorbed onto the NH(2) and OH SAMs. Cell adhesion strength to Fn-coated SAMs correlated with alpha(5)beta(1) integrin binding (OH > COOH = NH(2) > CH(3)), and experiments with function-perturbing antibodies demonstrated that this receptor provides the dominant adhesion mechanism in this cell model. This work establishes an experimental framework to analyze adhesive mechanisms controlling cell-surface interactions and pr…
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Surfaces with varying properties promote differential cellular integrin binding to the absorbed protein layer.
“Surfaces with varying properties promote differential cellular integrin binding to the absorbed protein layer[43–46]”
From Foreign body reaction to biomaterials (2008) · cites this paper as [46]
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- Authors
- Keselowsky, B. G., Collard, D. M., & García, A. J.
- Affiliations
- Georgia Institute of Technology (US)
- Venue
- Journal of Biomedical Materials Research Part A
- Publisher
- Wiley
- Published
- 2003-07-08
- Volume
- 66A
- Issue
- 2
- Pages
- 247-259
- ISSN
- 1549-3296 (ISSN-L)
- 1552-4965
- OpenAlex
- W2032275376
- Cited by
- 949
- References
- 0
- Citations by year
- 2026: 33 · 2025: 18 · 2024: 13 · 2023: 15 · 2022: 30 · 2021: 36 · 2020: 42 · 2019: 40 · 2018: 50 · 2017: 47 · 2016: 61 · 2015: 55 · 2014: 57 · 2013: 55 · 2012: 72
- FWCI
- 13.70
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Biomedical Materials Research Part A (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Whitaker Foundation
- Georgia Tech/Emory NSF ERC on the Engineering of Living Tissues (EEC-9731643)
- National Science Foundation Graduate Research Fellowship (to B.G.K.)
- Topics
- Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
- Physical Sciences › Materials Science › Surfaces, Coatings and Films › Polymer Surface Interaction Studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Keywords
- fibronectin, integrin binding, cell adhesion, surface chemistry, self-assembled monolayers, alkanethiol monolayers, gold surfaces, alpha5beta1 integrin, ITGAV, protein adsorption, cell-binding domain, monoclonal antibodies
- MeSH terms
- Animals, Cell Adhesion, Extracellular Matrix, Fibronectins, Fluorescent Antibody Technique, Models, Biological, Protein Binding, Protein Conformation, Integrins, Mice
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