Submitted to: American Chemical Society Symposium Series
Publication Type: Proceedings
Publication Acceptance Date: November 17, 2005
Publication Date: N/A
Technical Abstract: The major fibrous collagens (types I, II, and III) perform a variety of structural functions in the skin, tendons, bones and cornea of animals. The basic structure of these molecules is the collagen triple helix, consisting of three chains with multiple repeats of the Gly-Xxx-Yyy tripeptide. In nature, these helices further associate into fibers, the length and supramolecular aggregate forms of which vary with the functional requirements. Enzyme catalyzed crosslinks involving the short, nonhelical telopeptides at the N- and C- termini of the triple helix contribute to fiber stability. As a basis for manufactured goods including biomedical devices and leather, the collagen network is further stabilized by the addition of synthetic crosslinks formed by the action of transglutaminase, dialdehydes, tannins or mineral tannages. These crosslinks contribute to high hydrothermal stability and resistance to microbial attack for collagen-based materials. Nature's network, with a little additional stabilization, finds many commercial applications.