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Title: Development and utilization of a bovine type I collagen microfibril model

item Brown, Eleanor - Ellie

Submitted to: International Journal of Biological Macromolecules
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 10/26/2012
Publication Date: 1/1/2013
Citation: Brown, E.M. 2013. Development and utilization of a bovine type I collagen microfibril model. International Journal of Biological Macromolecules. 53:20-25.

Interpretive Summary: Collagen, the primary protein of connective tissue, plays an important role in technology, serving as a basis for industrial biopolymers including leather, medical devices, food and adhesives. A major challenge to the use of collagen in manufactured biomaterials is the identification of ways to stabilize its structure, which are acceptable and practical for the proposed end use. Computer-assisted molecular modeling is a useful tool for visualizing structure-function relationships in proteins, and for predicting the effects of proposed modifications to protein structure. The bovine type I collagen microfibril model was developed as a tool for exploring mechanisms for interactions of tanning chemicals with collagen, and has proved useful in the analysis of crosslinking reactions. It is anticipated that the designers of collagen based biomaterials including new tannages for leather may find it useful.

Technical Abstract: The structure of fibrous collagen, a long triple helix that self-associates in a staggered array to form a matrix of fibrils, fibers and fiber bundles, makes it uniquely suitable as a scaffold for biomaterial engineering. A major challenge for this application is to stabilize collagen structure by means that are acceptable for the end use. The bovine type I collagen microfibril model, built by computer assisted modeling, comprised of five right-handed triple helices in a left-handed super coil containing gap and overlap regions as well as the nonhelical telopeptides is a tool for predicting or visualizing chemistry to stabilize the matrix, insert an active agent, or otherwise modify collagen.