Collagen oligomers modulate physical and biological properties of three-dimensional self-assembled matrices.

Abstract:

:Elucidation of mechanisms underlying collagen fibril assembly and matrix-induced guidance of cell fate will contribute to the design and expanded use of this biopolymer for research and clinical applications. Here, we define how Type I collagen oligomers affect in-vitro polymerization kinetics as well as fibril microstructure and mechanical properties of formed matrices. Monomers and oligomers were fractionated from acid-solubilized pig skin collagen and used to generate formulations varying in monomer/oligomer content or average polymer molecular weight (AMW). Polymerization half-times decreased with increasing collagen AMW and closely paralleled lag times, indicating that oligomers effectively served as nucleation sites. Furthermore, increasing AMW yielded matrices with increased interfibril branching and had no correlative effect on fibril density or diameter. These microstructure changes increased the stiffness of matrices as evidenced by increases in both shear storage and compressive moduli. Finally, the biological relevance of modulating collagen AMW was evidenced by the ability of cultured endothelial colony forming cells to sense associated changes in matrix physical properties and alter vacuole and capillary-like network formation. This work documents the importance of oligomers as another physiologically-relevant design parameter for development and standardization of polymerizable collagen formulations to be used for cell culture, regenerative medicine, and engineered tissue applications.

journal_name

Biopolymers

journal_title

Biopolymers

authors

Bailey JL,Critser PJ,Whittington C,Kuske JL,Yoder MC,Voytik-Harbin SL

doi

10.1002/bip.21537

subject

Has Abstract

pub_date

2011-02-01 00:00:00

pages

77-93

issue

2

eissn

0006-3525

issn

1097-0282

journal_volume

95

pub_type

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