Specific Binding and Mineralization of Calcified Surfaces by Small Peptides

• Published in: Calcified tissue international Vol. 86; no. 1; pp. 58 - 66
• Main Authors: Yarbrough, Daniel K., Hagerman, Elizabeth, Eckert, Randal, He, Jian, Choi, Hyewon, Cao, Nga, Le, Karen, Hedger, Jennifer, Qi, Fengxia, Anderson, Maxwell, Rutherford, Bruce, Wu, Ben, Tetradis, Sotiris, Shi, Wenyuan
• Format: Journal Article
• Language: English
• Published: New York Springer-Verlag 01.01.2010; Springer Nature B.V
• Subjects: Amino Acid Sequence - physiology; Animals; Binding sites; Binding Sites - drug effects; Binding Sites - physiology; Biochemistry; Biomedical and Life Sciences; Cell Biology; Cells, Cultured; Cellular biology; Dental Caries - diagnosis; Dental Caries - metabolism; Dental Caries - physiopathology; Dentin - drug effects; Dentin - growth & development; Dentin - metabolism; Durapatite - chemistry; Durapatite - metabolism; Endocrinology; Extracellular Matrix Proteins - chemistry; Extracellular Matrix Proteins - metabolism; Life Sciences; Mice; Orthopedics; Peptides; Peptides - metabolism; Peptides - pharmacology; Peptides - therapeutic use; Phosphoproteins - chemistry; Phosphoproteins - metabolism; Phosphorylation; Protein Binding - drug effects; Protein Binding - physiology; Proteins; Sialoglycoproteins - chemistry; Sialoglycoproteins - metabolism; Teeth; Tooth - drug effects; Tooth - growth & development; Tooth - metabolism; Tooth Calcification - drug effects; Tooth Calcification - physiology; Dentin phosphoprotein; Mineralization; Peptide
• ISSN: 0171-967X; 1432-0827
• DOI: 10.1007/s00223-009-9312-0

Several small (<25aa) peptides have been designed based on the sequence of the dentin phosphoprotein, one of the major noncollagenous proteins thought to be involved in the mineralization of the dentin extracellular matrix during tooth development. These peptides, consisting of multiple repeats of the tripeptide aspartate-serine-serine (DSS), bind with high affinity to calcium phosphate compounds and, when immobilized, can recruit calcium phosphate to peptide-derivatized polystyrene beads or to demineralized human dentin surfaces. The affinity of binding to hydroxyapatite surfaces increases with the number of (DSS) n repeats, and though similar repeated sequences—(NTT) n , (DTT) n , (ETT) n , (NSS) n , (ESS) n , (DAA) n , (ASS) n , and (NAA) n —also showed HA binding activity, it was generally not at the same level as the natural sequence. Binding of the (DSS) n peptides to sectioned human teeth was shown to be tissue-specific, with high levels of binding to the mantle dentin, lower levels of binding to the circumpulpal dentin, and little or no binding to healthy enamel. Phosphorylation of the serines of these peptides was found to affect the avidity, but not the affinity, of binding. The potential utility of these peptides in the detection of carious lesions, the delivery of therapeutic compounds to mineralized tissues, and the modulation of remineralization is discussed.