Biomineralization proteins act as nature's crystal engineers and adsorb onto crystal surfaces with precision. The human salivary protein statherin regulates the growth of hydroxyapatite (HAP) in bone and tooth enamel. We have used sum frequency generation (SFG) spectroscopy to probe the orientation and secondary structure of the binding domain of statherin, SN15, on HAP surfaces in situ. The data showed an a-helical secondary structure of SN15 on HAP with the helix axis parallel to the surface. Site selective isotope labeling allows the analysis of specific protein regions with atomic resolution (1) and we have used this method to determine the orientation of all hydrophobic side chains of SN15 on HAP (leucine, isoleucine, phenylalanine). We have also combined SFG with near edge X-ray absorption fine structure (NEXAFS) analysis of site-selectively fluorinated SN15 to complement our structural analysis.1.         Weidner et al. (2010) Proc. Natl. Acad. Sci. U. S. A. 107:13288.

Probing the structure of statherin on hydroxyapatite surfaces with SFG and NEXAFS spectroscopy

243rd National Meeting (2012)

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