Biomedical Engineering and Bioengineering Commons^™

Β-Aminopropionitrile-Induced Reduction In Enzymatic Crosslinking Causes In Vitro Changes In Collagen Morphology And Molecular Composition, Silvia P. Canelón, Joseph M. Wallace

Weldon School of Biomedical Engineering Graduate Student Publications

Type I collagen morphology can be characterized using fibril D-spacing, a metric which describes the periodicity of repeating bands of gap and overlap regions of collagen molecules arranged into collagen fibrils. This fibrillar structure is stabilized by enzymatic crosslinks initiated by lysyl oxidase (LOX), a step which can be disrupted using β-aminopropionitrile (BAPN). Murine in vivo studies have confirmed effects of BAPN on collagen nanostructure and the objective of this study was to evaluate the mechanism of these effects in vitro by measuring D-spacing, evaluating the ratio of mature to immature crosslinks, and quantifying gene expression of type I collagen …