Submitted to: International Union of Leather Technologists and Chemists Societies
Publication Type: Proceedings
Publication Acceptance Date: July 13, 2009
Publication Date: November 1, 2009
Citation: Brown, E.M. 2009. The collagen microfibil model as a tool for leather scientists. International Union of Leather Technologists and Chemists Societies. Technical Abstract: Collagen, a structural protein of the extracellular matrix, gives strength and form to the skin, tendons, bones, cornea and teeth of mammals. The discovery by early humans that the skin of an animal, slaughtered for meat, could be preserved by exposing it to smoke or rubbing with fat, led to the production of leather. Through empirical methods, a number of tanning agents with a variety of properties were identified. The methods for production of leather evolved over several centuries as art and engineering with little understanding of the underlying science. Scientific advances of the twentieth century, including increasing use of collagen in medical device research, began to provide a basis for understanding the relationship between collagen structure and function in both biology and technology. The unique structure of fibrous collagens, a Gly-X-Y repeating sequence that results in a long triple helix that further associates into fibers, makes solution-based studies of protein interactions challenging. Nearly twenty years ago, leather researchers at the Eastern Regional Research Center of the United States Department of Agriculture (ERRC) began the construction of a type I collagen microfibril model for the simulation of interactions of tanning chemistries with and between collagen triple helices. Insights gained, and possible new directions for research and development will be discussed.