Abstract
Osteogenesis Imperfecta is a disease characterized by too little collagen in the body, causing brittle bones, permanent disfigurement, and often death. To provide fundamental understanding of the molecular basis of these diseases, extensive molecular dynamics simulations were conducted using the AMBER 10.0 suite. A Glycine-Proline-Hydroxyproline tropocollagen molecule was used as a building block for a fibril. The central tropocollagen molecule was later modified to corresponding mutations. Electrostatic measurements, hydration and ion patterns were determined, garnering an observation of a hydrophobic dipole. Our simulations indicate that the mutations significantly affect binding and mechanical properties of the collagen fibrils. Moreover, we predict that the high death rate related to lysine mutation can be explained by the increase in diameter and significant loss of mechanical properties in collagen fibril.
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