Enzymatic formation of modular cell-instructive fibrin analogs for tissue engineering

Ehrbar, Martin; Rizzi, Simone C; Hlushchuk, Ruslan; Djonov, Valentin; Zisch, Andreas H; Hubbell, Jeffrey A; Weber, Franz E; Lutolf, Matthias P (2007). Enzymatic formation of modular cell-instructive fibrin analogs for tissue engineering. Biomaterials, 28(26), pp. 3856-66. Oxford: Elsevier 10.1016/j.biomaterials.2007.03.027

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The molecular engineering of cell-instructive artificial extracellular matrices is a powerful means to control cell behavior and enable complex processes of tissue formation and regeneration. This work reports on a novel method to produce such smart biomaterials by recapitulating the crosslinking chemistry and the biomolecular characteristics of the biopolymer fibrin in a synthetic analog. We use activated coagulation transglutaminase factor XIIIa for site-specific coupling of cell adhesion ligands and engineered growth factor proteins to multiarm poly(ethylene glycol) macromers that simultaneously form proteolytically sensitive hydrogel networks in the same enzyme-catalyzed reaction. Growth factor proteins are quantitatively incorporated and released upon cell-derived proteolytic degradation of the gels. Primary stromal cells can invade and proteolytically remodel these networks both in an in vitro and in vivo setting. The synthetic ease and potential to engineer their physicochemical and bioactive characteristics makes these hybrid networks true alternatives for fibrin as provisional drug delivery platforms in tissue engineering.

Item Type:

Journal Article (Original Article)

Division/Institute:

04 Faculty of Medicine > Pre-clinic Human Medicine > Institute of Anatomy

UniBE Contributor:

Hlushchuk, Ruslan and Djonov, Valentin

ISSN:

0142-9612

ISBN:

17568666

Publisher:

Elsevier

Language:

English

Submitter:

Factscience Import

Date Deposited:

04 Oct 2013 14:56

Last Modified:

04 May 2014 23:16

Publisher DOI:

10.1016/j.biomaterials.2007.03.027

PubMed ID:

17568666

Web of Science ID:

000248875300010

URI:

https://boris.unibe.ch/id/eprint/23710 (FactScience: 43546)

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