Study of the Binding of SN-15 to Hydroxyapatite using 15N{31P} REDOR
EMSL Project ID
7803
Abstract
Proteins found in mineralized tissues act as nature's crystal engineers. They regulate biological mineralization by promoting or inhibiting the growth of minerals such as hydroxyapatite (HAP), the main mineral component of bone and teeth. Despite their importance to dentistry, there is remarkably little known of the protein structure-function relationships governing hard tissue engineering. Among these acidic proteins found in the saliva is statherin, a 43 amino-acid tyrosine rich peptide that is an inhibitor of both HAP crystal growth and nucleation. Earlier studies have proved that the N-terminal fragment of statherin (SN-15) binds strongly to hydroxyapatite. We would perform 15N{31P} REDOR NMR to analyze the binding mechanism of a 15 amino acid fragment of statherin (SN-15) to the HAP surface in biologically relevant hydrated conditions at low temperature.
Project Details
Project type
Capability Research
Start Date
2004-05-13
End Date
2005-09-30
Status
Closed
Released Data Link
Team
Principal Investigator
Team Members
Related Publications
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Gibson JM, V Raghunathan, JM Popham, P Stayton, and GP Drobny. 2005. "A REDOR NMR Study of a Phosphorylated Statherin Fragment Bound to Hydroxyapatite Crystals." Journal of the American Chemical Society 127(26):9350-9351.
Gibson JM, V Raghunathan, JM Popham, P Stayton, and GP Drobny. 2005. "A REDOR NMR Study of a Phosphorylated Statherin Fragment Bound to Hydroxyapatite Crystals." Journal of the American Chemical Society 127(26):9350-9351.
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