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Amelogenin–enamelin association in phosphate‐buffered saline
Author(s) -
Yang Xiudong,
Fan Daming,
Mattew Shibi,
MoradianOldak Janet
Publication year - 2011
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.1600-0722.2011.00916.x
Subject(s) - amelogenin , enamel paint , chemistry , crystallography , dynamic light scattering , fluorescence spectroscopy , macromolecule , circular dichroism , phosphate , nucleation , biophysics , transmission electron microscopy , phosphate buffered saline , fluorescence , biochemistry , materials science , chromatography , biology , nanotechnology , optics , physics , organic chemistry , nanoparticle , composite material , gene
Yang X, Fan D, Mattew S, Moradian‐Oldak J. Amelogenin–enamelin association in phosphate‐buffered saline.
Eur J Oral Sci 2011; 119 (Supp. 1): 351–356. © 2011 Eur J Oral Sci The structures and interactions among macromolecules in the enamel extracellular matrix play vital roles in regulating hydroxyapatite crystal nucleation, growth, and maturation. We used dynamic light scattering (DLS), circular dichroism (CD), fluorescence spectroscopy, and transmission electron microscopy (TEM) to investigate the association of amelogenin and the 32‐kDa enamelin, at physiological pH 7.4, in phosphate‐buffered saline (PBS). The self‐assembly behavior of amelogenin (rP148) was altered following addition of the 32‐kDa enamelin. Dynamic light scattering revealed a trend for a decrease in aggregate size in the solution following the addition of enamelin to amelogenin. A blue‐shift and intensity increase of the ellipticity minima of rP148 in the CD spectra upon the addition of the 32‐kDa enamelin, suggest a direct interaction between the two proteins. In the fluorescence spectra, the maximum emission of rP148 was red‐shifted from 335 to 341 nm with a marked intensity increase in the presence of enamelin as a result of complexation of the two proteins. In agreement with DLS data, TEM imaging showed that the 32‐kDa enamelin dispersed the amelogenin aggregates into oligomeric particles and stabilized them. Our study provides novel insights into understanding the possible cooperation between enamelin and amelogenin in macromolecular co‐assembly and in controlling enamel mineral formation.