Lateral chain length in polyalkyl acrylates determines the mobility of fibronectin at the cell/material interface

Bathawab, F., Bennett, M., Cantini, M. , Reboud, J., Dalby, M. and Salmeron-Sanchez, M. (2016) Lateral chain length in polyalkyl acrylates determines the mobility of fibronectin at the cell/material interface. Langmuir, 32(3), pp. 800-809. (doi:10.1021/acs.langmuir.5b03259) (PMID:26715432) (PMCID:PMC4732669)

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Abstract

Cells, by interacting with surfaces indirectly through a layer of extracellular matrix proteins, can respond to a variety of physical properties, such as topography or stiffness. Polymer surface mobility is another physical property that is less well understood but has been indicated to hold the potential to modulate cell behavior. Polymer mobility is related to the glass-transition temperature (Tg) of the system, the point at which a polymer transitions from an amorphous solid to a more liquid-like state. This work shows that changes in polymer mobility translate to interfacial mobility of extracellular matrix proteins adsorbed on the material surface. This study has utilized a family of polyalkyl acrylates with similar chemistry but different degrees of mobility, obtained through increasing length of the side chain. These materials are used, in conjunction with fluorescent fibronectin, to determine the mobility of this interfacial layer of protein that constitutes the initial cell–material interface. Furthermore, the extent of fibronectin domain availability (III9, III10, - the integrin binding site), cell-mediated reorganization, and cell differentiation was also determined. A nonmonotonic dependence of fibronectin mobility on polymer surface mobility was observed, with a similar trend noted in cell-mediated reorganization of the protein layer by L929 fibroblasts. The availability of the integrin-binding site was higher on the more mobile surfaces, where a similar organization of the protein into networks at the material interface was observed. Finally, differentiation of C2C12 myoblasts was seen to be highly sensitive to surface mobility upon inhibition of cell contractility. Altogether, these findings show that polymer mobility is a subtle influence that translates to the cell/material interface through the protein layer to alter the biological activity of the surface.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Salmeron-Sanchez, Professor Manuel and Reboud, Dr Julien and Cantini, Dr Marco and Dalby, Professor Matthew
Authors: Bathawab, F., Bennett, M., Cantini, M., Reboud, J., Dalby, M., and Salmeron-Sanchez, M.
College/School:College of Medical Veterinary and Life Sciences > Institute of Molecular Cell and Systems Biology
College of Science and Engineering > School of Engineering > Biomedical Engineering
Journal Name:Langmuir
Publisher:American Chemical Society
ISSN:0743-7463
ISSN (Online):1520-5827
Published Online:29 December 2015
Copyright Holders:Copyright © 2015 American Chemical Society
First Published:First published in Langmuir 32(3): 800-809
Publisher Policy:Reproduced under a Creative Commons License

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Project CodeAward NoProject NamePrincipal InvestigatorFunder's NameFunder RefLead Dept
653731Synergistic microenvironments for non-union bone defectsMatthew DalbyMedical Research Council (MRC)MR/L0022710/1RI MOLECULAR CELL & SYSTEMS BIOLOGY
626901HEALINSYNERGY - Material-driven fibronectin fibrillogenesis to engineer synergistic growth factor microenvironmentsManuel Salmeron-SanchezEuropean Research Council (ERC)306990ENG - BIOMEDICAL ENGINEERING