Hydroxyapatite mineralization and demineralization in the presence of synthetic phosphorylated pentapeptides.
A constant composition (CC) method was used to compare the influence of statherin-like N-terminal 5-residue fragments having different amino acids in the terminal position on hydroxyapatite (HAP) growth and dissolution. The CC experiments were done in solutions containing 4.00 x 10(-4) mol/l calcium and 2.40 x 10(-4) mol/l phosphate. The solutions used in the crystallization studies were supersaturated only with respect to HAP (pH = 7.40, sigma HAP = 3.60). The CC dissolution studies were done in solutions undersaturated with respect to HAP (pH = 6.00; sigma HAP = -0.39). The HAP mineralization and demineralization processes were markedly inhibited by the negatively charged pentapeptides. Those containing a phosphorylated terminal residue inhibited dissolution to a greater extent than the native statherin fragment having aspartate as the N-terminal residue. Strong dependencies of the degree of inhibition of growth and dissolution reaction rates on the extents of reaction were noted. As the reactions proceeded, the rate inhibition decreased in the case of crystal growth and increased for dissolution.
Department of Chemistry, State University of New York at Buffalo.
K
K
Wikiel
E M
EM
Burke
J W
JW
Perich
E C
EC
Reynolds
G H
GH
Nancollas
D000327:Adsorption; D000595:Amino Acid Sequence; D002118:Calcium / Q000737:chemistry; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D003460:Crystallization; D017886:Durapatite / Q000737:chemistry*; D007700:Kinetics; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry; D010748:Phosphopeptides / Q000737:chemistry; D010766:Phosphorylation; D012471:Salivary Proteins and Peptides / Q000737:chemistry*; D013499:Surface Properties
D010446:Peptide Fragments; D010748:Phosphopeptides; C018149:STATH protein, human; D012471:Salivary Proteins and Peptides; D017886:Durapatite; D002118:Calcium