The conformation and chemistry of proteins binding to hydroxyapatite (HAP) are critical to control the biomineralization of mammalian hard tissues such as bone and teeth. The mechanistic details of how amelogenin controls HAP crystal growth is not well understood. Protein structure (secondary, tertiary, and quaternary) is assumed to play a key role in the function of amelogenin in enamel formation, and the goal of these studies is to understand the structures of the wildtype protein, to allow correlating structure and function in enamel development. We have used solid/solution state NMR, TEM and in-situ AFM to develop a molecular level understanding of the protein-surface interface as well as the effect of protein on HAP crystal growth, with broader implications to hard-soft tissue interfaces in tissue repair and replacement. Recently these techniques have been extended to single site mutant amelogenin known to exist in malformed enamel found in patients with <i>amelogenesis imperfecta</i>. The advancement of study protein-protein, protein-mineral interactions and protein digestion by enzyme on surfaces in real time using <i>in-situ</i> AFM combined with NMR analysis, we can identify the cleavage sites, structural flexibility of mutant amelogenin on HAP (100) face, which has strong correlation with protein-mineral interaction. The protocol here should have general meaning to be applied to other protein-mineral interactions to further elucidate the role of proteins in biomineral formation processes.

Structure flexibility controls the adsorption and digestion kinetics of point mutant amelogenin on hydroxyapatite (100)

255th National Meeting (2018)

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