Production of a Novel, Self-Assembled, Collagenous Matrix Mimicking the Hierarchical Structure of Native Aligned Connect
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G. D. PINS, D. L. CHRISTIANSEN, R. PATEL AND F. H. SILVER, University of Medicine and Dentistry of New Jersey - Robert Wood Johnson Medical School, Department of Pathology/Division of Biomaterials, 675 Hoes Lane, Piscataway, New Jersey 08854, pins @rwja.umdnj.edu ABSTRACT
The primary goal of the biomaterials scientist and tissue engineer is to create a biocompatible implant which mimics the mechanical and morphological properties of the tissue being replaced. In vitro experimentation has documented the propensity of soluble type I collagen to self-assemble and form microscopic collagen fibrils with periodic banding analogous to native collagen fiber. Our laboratory has further investigated in vitro self-assembly by incorporating several of the "natural" processes into a multi-step fiber formation procedure which generates macroscopic collagen fiber from its molecular constituents. Results of uniaxial tensile tests and ultrastructural analyses indicate that these coextruded and stretched collagen fibers have mechanical properties and fibrillar substructure comparable to that observed in native collagen fiber. INTRODUCTION Fibrillar type I collagen is a primary structural element in vertebrate and invertebrate tissues 1. Over a period of several million years, natural selection and evolution have optimized the mechanical properties and morphological structures of the various tissues containing fibrillar type I collagen. The mechanisms involved in formation of mineralized and non-mineralized connective tissue have been studied in great detail by scientists interested in learning about tissue development, disease processes and possible means of treating pathological conditions. The biomaterials scientist and tissue engineer can make use of these "natural" design processes to create biocompatible implants which mimic the mechanical and morphological properties of the tissue being replaced. Over the past 20 years, extensive research has uncovered many of the intra- and extracellular mechanisms involved in the synthesis of oriented fibrillar connective tissue, the biosynthesis and self-assembly of individual collagen molecules and the linear and lateral packing of oligomeric fibril segments into hierarchically ordered tissue constructs such as tendon and ligament 2. In vitro experimentation has documented the propensity of acid soluble type I collagen to self-assemble and form microscopic collagen fibrils with periodic banding analogous to native fibril segments 3, 4. Our laboratory has extended in vitro self-assembly to the formation of oriented macroscopic collagen scaffolds by incorporating many of the "natural" design processes into our fiber production procedure 5. The purpose of this paper is to report the results of studies on the production of a novel, self-assembled collagenous matrix with mechanical properties and morphological characteristics comparable to native, aligned connective tissue. The results of our mechanical and ultrastructural studies show the collagen fibers coextruded from acid-soluble type I co
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