The goal of this study is to characterize a collagenase produced by the periodontal pathogen, Tannerella forsythia. Data presented in this poster provides researchers with more information about the enzyme, hence furthering the development of a treatment for the disease. In this work, SDS-PAGE assays were used to show cleavage of native collagen by the T. forsythia collagenase. Collagenase activity was further studied by monitoring relief of fluorescent quenching of highly fluorescein-labeled collagen using a LS50 Luminescence Spectrophotometer. Enzyme activity was measured using collagen I and collagen IV as the substrate. The isolated collagenase cleaved type I, but not type IV, collagen. Therefore further enzyme characterization assays were performed using type I collagen. A wide array of enzyme inhibitors were tested to determine their effect on the collagenase. Serine protease inhibitors antipain and phenylmethanesulfonyl fluoride were found to inhibit the collagenase activity in a dose-dependent manner. Inhibition by these compounds gives insight into the functioning of this collagenase and could have potential medicinal applications in the treatment of periodontal disease.

Characterization of a Tannerella forsythia collagenase by SDS-PAGE and fluorescent spectroscopy

249th National Meeting (2015)

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