Search

Collagen fibers form the structural units of connective tissue throughout the body, transmitting force, maintaining shape, and providing a scaffold for cells. Our laboratory has studied collagen self-assembly since the 1970s. In this study, collagen fibers were self-assembled from molecular collagen solutions and then stretched to enhance alignment. Fibers were tested in uniaxial tension to study the mechanical properties and failure mechanisms. Results reported suggest that axial orientation of collagen fibrils can be achieved by stretching uncrosslinked collagen fibers. Stretching by about 30% not only results in decreased diameter and increased tensile strength but also leads to unusual failure mechanisms that inhibit crack propagation across the fiber. It is proposed that stretching serves to generate oriented fibrillar substructure in self-assembled collagen fibers. © 1997 John Wiley & Sons, Inc. J Appl Polym Sci 63: 1429–1440, 1997

Collagen fibers self-assembled from solutions of molecular type I collagen were mineralized at pH 9.5, by exposure to super-saturated solutions of calcium and phosphate for a one week period in a double diffusion chamber. Uniaxial tensile mechanical properties increased with mineralization and electron microscopy of the mineral formed within the fiber was morphologically similar to the mineral phase of calcified tissues. Selected area electron diffraction confirms the presence of hydroxyapatite crystal. Further, the aligned fibrillar substructure serves as a template for the orientation of the c-axis diffraction maxima of the hydroxyapatite. These results indicate that an aligned system composed exclusively of selfassembled type I collagen fibrils serves as a scaffold for oriented growth of mineral analogous to calcification in vertebrate bone.