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Title: Structure and Dynamics of Hydrated Statherin on Hydroxyapatite As Determined by Solid-State NMR

Journal Article · · Biochemistry, 40(51):15451-15455
DOI:https://doi.org/10.1021/bi010864c· OSTI ID:15003868

Proteins directly conrol the nucleation and growth of biominerals, but the details of molecular recognition at the protein-biomineral interface reamain poorly understood. The elucidation of recognition mechanisms at this interface may provide design principles for advanced materials development in medical and ceramic composite technologies. Here, we have used solid-state NMR techniques to provide the first high-resolution structural and dynamic characterization of a hydrated biomineralization protein, salivary statherin, adsorbed to its biologically relevant hydroxypapatite (HAP) surface. Backbone secondary structure for the N-terminal dodecyl region was determined using a combination of homonuclear and heteronuclear dipolar recoupling techniques. Both sets of experiments indicate the N-terminus is a-helical in character with the residues directly binding to the HAP being stabilized in the a-helical conformation by the presecne of water. Dynamic NMR studies demonstrate that the highly anionic N-terminus is strongly adsorbed and immobilized on the HAP surface, while the middle and C-terminal regions of this domain are mobile and thus weakly interacting with the mineral surface. The direct binding footprint of staterin is thus localized to the negatively charged N-terminal pentapeptide sequence. Study of a site-directed mutant demonstrated that alteration of the only anionic side chain ouside of this domain did not affect the dynamics of statherin on the HAP surface, suggesting that it does not play an important role in HAP binding.

Research Organization:
Pacific Northwest National Lab. (PNNL), Richland, WA (United States)
Sponsoring Organization:
USDOE
DOE Contract Number:
AC06-76RL01830
OSTI ID:
15003868
Report Number(s):
PNWD-SA-5638; TRN: US201015%%165
Journal Information:
Biochemistry, 40(51):15451-15455, Vol. 40, Issue 51
Country of Publication:
United States
Language:
English

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