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Study of the binding mechanism of mutant SN-15 to hydroxyapatite using 15N{31P}REDOR


EMSL Project ID
10493

Abstract

Proteins are used in nature to control biomineralization processes in mineralized tissues. Acidic macromolecules functioning at the biological, inorganic interface regulate crystal formation and growth of minerals such as hydroxyapatite (HAP), the main mineral component of teeth. A salivary peptide, statherin is a 43-residue proline, and tyrosine-rich acidic phosphopeptide that has a dual function of preventing hydroxyapatite crystal formation as well as growth. Little is known about the binding mechanism nor of the protein structure-function relationships governing hard tissue engineering. From previous studies, it was shown that the N-terminal region of statherin binds strongly to HAP. We would perform 15N{31P} REDOR distance measurements between 15 amino acid N-terminal mutant fragments of statherin (SN-15) and HAP under biologically relevant hydrated conditions at low temperature. Results would provide insight into the function of statherin as well as provide information about binding mechanisms.

Project Details

Project type
Capability Research
Start Date
2004-10-05
End Date
2005-10-03
Status
Closed

Team

Principal Investigator

Jennifer Popham
Institution
University of Washington

Team Members

James Gibson
Institution
University of Washington

Vinodhkumar Raghunathan
Institution
University of Washington

Patrick Stayton
Institution
University of Washington

Gary Drobny
Institution
University of Washington

Related Publications

Raghunathan V, JM Gibson, G Goobes, JM Popham, E Louie, P Stayton, and GP Drobny. 2006. "Homonuclear and Heteronuclear NMR Studies of a Statherin Fragment Bound to Hydroxyapatite Crystals." Journal of Physical Chemistry B 110(18):9324-9332.