Premium
Conformation of dentin phosphophoryn adsorbed on hydroxyapatite crystals
Author(s) -
Fujisawa Ryuichi,
Kuboki Yoshinori
Publication year - 1998
Publication title -
european journal of oral sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.802
H-Index - 93
eISSN - 1600-0722
pISSN - 0909-8836
DOI - 10.1111/j.1600-0722.1998.tb02183.x
Subject(s) - chemistry , magic angle spinning , adsorption , crystallography , molecule , aspartic acid , crystal structure , peptide , nuclear magnetic resonance spectroscopy , crystal (programming language) , amino acid , stereochemistry , organic chemistry , biochemistry , computer science , programming language
Phosphophoryn, the major noncollagenous protein of dentin, was adsorbed on synthetic hydroxyapatite crystals and analyzed by high‐resolution solid‐state nuclear magnetic resonance (NMR) spectroscopy. Binding of the protein was inhibited by acidic polypeptides, especially by a phosphorylated peptide. After phosphophoryn was incubated with the crystals, the crystals were collected and analyzed by 13 C‐cross‐polarization magic‐angle‐spinning NMR. Several signals could be assigned to carbons of aspartic acids, taking advantage of the unique amino acid composition of this protein. Chemical shifts of signals of aspartic acids are known to reflect secondary structure of the polypeptide. The chemical shifts obtained from the phosphophoryn indicate that the secondary structure of this protein on the crystal was near to a β‐sheet structure. This result is consistent with the result for poly(Asp) adsorbed on the crystals. The β‐sheet‐like structure enables phosphophoryn to extend on the crystal surface and to cover the surface with only a small number of the molecules, resulting in the high inhibitory effect of this protein on crystal growth.