Artificial Organs 14(6):443448,Raven Press, Ltd., New York 0 1990 International Society for Artificial Organs
Collagen Cross-Linking and Resorption: Effect of Glutaraldehyde Concentration Simon C. Roe, Bruce K. Milthorpe, and Klaus Schindhelm Centre f o r Biomedical Engineering, University of New South Wales, Kensington, Australia
Abstract: Cross-linked collagen bioprostheses usually are designed to be inert and nonresorbable, resulting in fatigue and wear failure in high-stress environments. Eventual replacement of the implant, although minimizing strength loss during resorption, would result in a graft with reparative ability. Kangaroo tail tendon (KTT) partially cross-linked with glutaraldehyde (GA) was evaluated in vitro for resistance to bacterial collagenase digestion and in vivo for biocompatibility and resorbability in
an intramuscular implant assay. Cross-linking was quantified by thermal denaturation studies. Incomplete crosslinking was achieved with concentrations of GA 0.05% GA were resistant to 240 h of collagenase digestion. Slight separation of peripheral fascicles was observed in some samples, but most remained unaltered. Tendons cross-linked in 0.025% GA began splitting after 48 h, and digestion was virtually complete after 216 h. Splitting of 0.01% cross-linked tendons was evident after 24 h, and digestion was complete in 120 h. Tendons not exposed to GA were digested completely within 36 h. The relationship between thermal denaturation temperature and GA concentration (Fig. 1) became asymptotic as the concentration of GA increased above 0.1%. A rapid increase in Td occurs from non-cross-linked tendon (Td = 47.1 O S T ) to tendon cross-linked in GA at a concentration of 0.05% (Td = 65.6 ? 0.7"C).The coefficient of variation for all Td was
Collagen cross-linking and resorption: effect of glutaraldehyde concentration.
Cross-linked collagen bioprostheses usually are designed to be inert and nonresorbable, resulting in fatigue and wear failure in high-stress environme...