Hydroxyapatite growth inhibition by osteopontin hexapeptide sequences

The effects of three acidic hexapeptides on in vitro hydroxyapatite growth were characterized by pH-stat kinetic studies, adsorption isotherms, and molecular modeling. The three peptides, pSDEpSDE, SDESDE, and DDDDDD, are equal-length model compounds for the acidic sequences in osteopontin, a protei...

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Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1985. - 26(2010), 12 vom: 15. Juni, Seite 9899-904
1. Verfasser: Silverman, L D (VerfasserIn)
Weitere Verfasser: Saadia, M, Ishal, J S, Tishbi, N, Leiderman, E, Kuyunov, I, Recca, B, Reitblat, C, Viswanathan, R
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2010
Zugriff auf das übergeordnete Werk:Langmuir : the ACS journal of surfaces and colloids
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Peptide Fragments Osteopontin 106441-73-0 Durapatite 91D9GV0Z28
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520 |a The effects of three acidic hexapeptides on in vitro hydroxyapatite growth were characterized by pH-stat kinetic studies, adsorption isotherms, and molecular modeling. The three peptides, pSDEpSDE, SDESDE, and DDDDDD, are equal-length model compounds for the acidic sequences in osteopontin, a protein that inhibits mineral formation in both calcified and noncalcified tissues. Growth rates from 1.67 mM calcium and 1.00 mM phosphate solution were measured at pH 7.4 and 37 degrees C in 150 mM NaCl. pSDEpSDE was a strong growth inhibitor when preadsorbed onto hydroxyapatite (HA) seeds from > or = 0.67 mM solutions, concentrations where adsorption isotherms showed relatively complete surface coverage. The nonphosphorylated SDESDE control showed no growth inhibition. Although it adsorbed to almost the same extent as pSDEpSDE, it rapidly desorbed under the pH-stat growth conditions while pSDEpSDE did not. DDDDDD exhibited weak inhibition as its concentration was increased and similar adsorption/desorption behavior to pSDEpSDE. Molecular modeling yielded binding energy trends based on simple adsorption of peptides on the [100] surface that were consistent with observed inhibition, but not for the [001] surface. The relatively unfavorable binding energies for peptides on the [001] surface suggest that their absorption will be primarily on the [100] face. The kinetic and adsorption data are consistent with phosphorylation of osteopontin acting to control mineral formation 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
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650 7 |a Osteopontin  |2 NLM 
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650 7 |a Durapatite  |2 NLM 
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700 1 |a Saadia, M  |e verfasserin  |4 aut 
700 1 |a Ishal, J S  |e verfasserin  |4 aut 
700 1 |a Tishbi, N  |e verfasserin  |4 aut 
700 1 |a Leiderman, E  |e verfasserin  |4 aut 
700 1 |a Kuyunov, I  |e verfasserin  |4 aut 
700 1 |a Recca, B  |e verfasserin  |4 aut 
700 1 |a Reitblat, C  |e verfasserin  |4 aut 
700 1 |a Viswanathan, R  |e verfasserin  |4 aut 
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