A (13)C{(31)P} REDOR NMR investigation of the role of glutamic acid residues in statherin- hydroxyapatite recognition
The side chain carboxyl groups of acidic proteins found in the extra-cellular matrix (ECM) of mineralized tissues play a key role in promoting or inhibiting the growth of minerals such as hydroxyapatite (HAP), the principal mineral component of bone and teeth. Among the acidic proteins found in the...
| Veröffentlicht in: | Langmuir : the ACS journal of surfaces and colloids. - 1992. - 25(2009), 20 vom: 20. Okt., Seite 12136-43 |
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| 1. Verfasser: | |
| Weitere Verfasser: | , , , , |
| Format: | Online-Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2009
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| Zugriff auf das übergeordnete Werk: | Langmuir : the ACS journal of surfaces and colloids |
| Schlagworte: | Journal Article Research Support, N.I.H., Extramural STATH protein, human Salivary Proteins and Peptides Solvents Glutamic Acid 3KX376GY7L Durapatite 91D9GV0Z28 |
| Zusammenfassung: | The side chain carboxyl groups of acidic proteins found in the extra-cellular matrix (ECM) of mineralized tissues play a key role in promoting or inhibiting the growth of minerals such as hydroxyapatite (HAP), the principal mineral component of bone and teeth. Among the acidic proteins found in the saliva is statherin, a 43-residue tyrosine-rich peptide that is a potent lubricant in the salivary pellicle and an inhibitor of both HAP crystal nucleation and growth. Three acidic amino acids-D1, E4, and E5-are located in the N-terminal 15 amino acid segment, with a fourth amino acid, E26, located outside the N-terminus. We have utilized (13)C{(31)P} REDOR NMR to analyze the role played by acidic amino acids in the binding mechanism of statherin to the HAP surface by measuring the distance between the delta-carboxyl (13)C spins of the three glutamic acid side chains of statherin (residues E4, E5, E26) and (31)P spins of the phosphate groups at the HAP surface. (13)C{(31)P} REDOR studies of glutamic-5-(13)C acid incorporated at positions E4 and E26 indicate a (13)C-(31)P distance of more than 6.5 A between the side chain carboxyl (13)C spin of E4 and the closest (31)P in the HAP surface. In contrast, the carboxyl (13)C spin at E5 has a much shorter (13)C-(31)P internuclear distance of 4.25 +/- 0.09 A, indicating that the carboxyl group of this side chain interacts directly with the surface. (13)C T(1rho) and slow-spinning MAS studies indicate that the motions of the side chains of E4 and E5 are more restricted than that of E26. Together, these results provide further insight into the molecular interactions of statherin with HAP surfaces |
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| Beschreibung: | Date Completed 25.01.2010 Date Revised 22.03.2024 published: Print Citation Status MEDLINE |
| ISSN: | 1520-5827 |
| DOI: | 10.1021/la901647n |