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Published November 2008 | Accepted Version + Supplemental Material
Journal Article Open

Cell response to RGD density in cross-linked artificial extracellular matrix protein films

Abstract

This study examines the adhesion, spreading, and migration of human umbilical vein endothelial cells on cross-linked films of artificial extracellular matrix (aECM) proteins. The aECM proteins described here were designed for application in small-diameter grafts and are composed of elastin-like structural repeats and fibronectin cell-binding domains. aECM-RGD contains the RGD sequence derived from fibronectin; the negative control protein aECM-RDG contains a scrambled cell-binding domain. The covalent attachment of poly(ethylene glycol) (PEG) to aECM substrates reduced nonspecific cell adhesion to aECM-RDG-PEG but did not preclude sequence-specific adhesion of endothelial cells to aECM-RGD-PEG. Variation in ligand density was accomplished by the mixing of aECM-RGD-PEG and aECM-RDG-PEG prior to cross-linking. Increasing the density of RGD domains in cross-linked films resulted in more robust cell adhesion and spreading but did not affect cell migration speed. Control of cell-binding domain density in aECM proteins can thus be used to modulate cell adhesion and spreading and will serve as an important design tool as these materials are further developed for use in surgery, tissue engineering, and regenerative medicine.

Additional Information

© 2008 American Chemical Society. Received April 29, 2008; Revised Manuscript Received August 18, 2008. We thank Paul Nowatzki for performing the AFM study, Elizabeth Jones and David Koos for advice on cell migration studies, Marissa Mock for helpful discussions on spin-coating protein films, Scott Fraser for help with fluorescence microscopy, and the Molecular Materials Research Center of the Caltech Beckman Institute for help with XPS. This work was supported by a Whitaker graduate fellowship to J.C.L., by NIH grant EB1971, and by the NSF Center for the Science and Engineering of Materials at the California Institute of Technology.

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Accepted Version - nihms97121.pdf

Supplemental Material - LIUbm08supp.pdf

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August 19, 2023
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