Submitted to: Proceedings of American Chemical Society National Meeting
Publication Type: Proceedings
Publication Acceptance Date: 5/30/2012
Publication Date: 8/19/2012
Citation: Brown, E.M., Liu, C. 2012. The collagen microfibril model, a tool for biomaterials scientists. Proceedings of American Chemical Society National Meeting, August 19-23, 2012, Philadelphia, PA. 1:1.
Technical Abstract: Animal hides, a major byproduct of the meat industry, are a rich source of collagen, a structural protein of the extracellular matrix that gives strength and form to the skin, tendons and bones of mammals. 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 medical materials is the stabilization of the collagen structure by means that are acceptable for the proposed end use. Our bovine type I collagen microfibril model comprises five right-handed triple helices in a left-handed super coil containing gap and overlap regions as well as the nonhelical telopeptides. This model can serve as a tool for predicting or visualizing the results of reactions intended to stabilize the matrix, insert an active agent, or otherwise modify collagen.