Student research award in the hospital intern, resident or clinical fellow category, 15th annual meeting of the society for biomaterials, Lake Buena Vista, Florida, April 28–May 2, 1989. An evaluation of purified reconstituted type 1 collagen fibers

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Abstract
Collagen fibers composed of type I collagen molecules were studied for biocompatibility and mechanical properties. These fibers were crosslinked using two different processes: (1) glutaraldehyde, (2) dehydration followed by exposure to cyanamide (DHT/C); the latter method produces only urea as a by-product of the crosslinking process and is postulated to be more biocompatible. An in vitro model using rat tendon fibroblasts growing on individual fibers was used to evaluate outgrowth rates, cell/fiber interactions, and cell morphology. These studies showed an advantage with DHT/C crosslinking, relative to glutaraldehyde crosslinking, in promoting fibroblast growth. In vivo intramuscular implantation in rats showed excellent biocompatibility for both kinds of collagen implants. In addition, aligned ingrowth into the implant from the medial collateral ligament when applied in that location was demonstrated. Mechanical testing demonstrated the higher strength of dry fibers; however, upon hydration, there was a marked decrease in stress to failure. This reduction in strength was due principally to an increase in cross section due to swelling. These collagen fibers appear to be very biocompatible even in the presence of low concentrations of glutaraldehyde. They promote fibrous aligned ingrowth in a setting of ligament healing. Thus, they represent a strong candidate as a scaffold ligament or tendon prosthesis if crosslink density can be increased.