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Issue 45, 2015
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Glycosaminoglycan functionalization of mechanically and topologically defined collagen I matrices

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Abstract

Collagen I and glycosaminoglycans (GAGs) are major components of the extracellular matrix in mammals and widely used for in vitro cell culture matrices. While composition, network microstructure and mechanics of these matrices sensitively determine cell fate, they are hard to adjust independently during matrix reconstitution. We report on a sequential preparation procedure of collagen I matrices, which allows a defined adjustment of network topology and mechanics in combination with GAG functionalization. Collagen I solution concentrations of 1.5 to 7 mg ml−1 allowed to vary topology (pore size) and elasticity of resulting networks with Young's moduli of 5 to 220 Pa. Zero-length crosslinking using carbodiimide chemistry increased Young's modulus 3 to 5 times without changing network topology. An optional covalent binding of hyaluronan and synthetically sulfated hyaluronan to the preformed matrices led to topologically unaffected networks with a stable functionalization with ∼30 μg GAG per mg collagen. While sulfated GAGs were stably attached to collagen I networks via physisorption or covalent binding at neutral and acidic conditions, non-sulfated hyaluronan required acidic conditions and covalent binding for stable attachment. In conclusion, this approach provides options to independently adjust biophysical and biochemical parameters of collagen I networks for in vitro studies.

Graphical abstract: Glycosaminoglycan functionalization of mechanically and topologically defined collagen I matrices

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Article information


Submitted
24 ágú. 2015
Accepted
19 okt. 2015
First published
20 okt. 2015

This article is Open Access

J. Mater. Chem. B, 2015,3, 8902-8910
Article type
Paper
Author version available

Glycosaminoglycan functionalization of mechanically and topologically defined collagen I matrices

L. Kalbitzer, K. Franke, S. Möller, M. Schnabelrauch and T. Pompe, J. Mater. Chem. B, 2015, 3, 8902
DOI: 10.1039/C5TB01737H

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