Methacrylation induces rapid, temperature-dependent, reversible self-assembly of type-I collagen.

ABSTRACT: Type-I collagen self-assembles into a fibrillar gel at physiological temperature and pH to provide a cell-adhesive, supportive, structural network. As such, it is an attractive, popular scaffold for in vitro evaluations of cellular behavior and for tissue engineering applications. In this study, type-I collagen is modified to introduce methacrylate groups on the free amines of the lysine residues to create collagen methacrylamide (CMA). CMA retains the properties of collagen such as self-assembly, biodegradability, and natural bioactivity but is also photoactive and can be rapidly cross-linked or functionalized with acrylated molecules when irradiated with ultraviolet light in the presence of a photoinitiator. CMA also demonstrates unique temperature-dependent behavior. For natural type-I

SUBMITTER: Drzewiecki KE 

PROVIDER: S-EPMC4172302 | biostudies-literature | 2014 Sep

REPOSITORIES: biostudies-literature