50th John Arthur Wilson Memorial Lecture - Abstract: Collagen - A Natural Scaffold for Bilolgy and Engineering

摘要

Collagen, the most abundant protein in mammals, constitutes a quarter of the animal's total weight. The unique structure of fibrous collagens, a long triple helix that further associates into fibers, provides an insoluble scaffold that gives strength and form to the skin, tendons, bones, cornea and teeth. The ready availability, to meat eaters, of animal skins that would putrefy, if left untreated, led to man's earliest venture into biomaterials engineering and resulted in 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.rnDuring the past 20 years, leather researchers at ERRC have used experimental and theoretical approaches to investigate several methods for stabilizing collagen structure. This research, which includes studies of mineral and vegetable tannages, enzyme catalyzed and aldehyde based covalent crosslinks, electrostatic and hydrophobic interactions, will be reviewed. Insight gained from these studies and those of other leather and biomaterials scientists will be evaluated as steps toward a still elusive, comprehensive mechanism for stabilization of collagen in leather and other biomaterials.