(269f) Modeling Statherin Structure Binding to Hydroxyapatite [001] Crystal Surface
AIChE Annual Meeting
2006
2006 Annual Meeting
Engineering Sciences and Fundamentals
Biomolecules at Interfaces V - Controlling and Observing Interfacial Protein Behavior
Tuesday, November 14, 2006 - 4:35pm to 4:51pm
Hydroxyapatite (HAP) is the major component of normal bone and teeth. The 43-residue protein statherin inhibits both the growth dynamics and nucleation of HAP in the environment of saliva. Despite their importance in hard-tissue formation and in pathological processes, there is little known of the statherin structure-function relationship and the molecular structure of the statherin-HAP interaction. In this work, we model statherin on HAP crystals with a multiscale Monte Carlo minimization structure prediction method. The protein structure is modeled according to solid state NMR constraints and includes two modified phosphoserine amino acids near the N-terminus. The HAP was modeled as a monoclinic crystal surface P21/b and an appropriate apatite forcefield was chosen. In the predicted model structure, residue Lys6 is close to the surface and has hydrogen bonds with HAP, and statherin is strongly bound in the acidic alpha-helical N-terminus in agreement with solid state NMR experiments.