Journal Article
Proceedings of the National Academy of Sciences, vol. 116, iss. 28, pp. 13867-13872, 2019
Authors
Jinhui Tao, Yongsoon Shin, Rajith Jayasinha, Garry W. Buchko, Sarah D. Burton, Alice C. Dohnalkova, Zheming Wang, Wendy J. Shaw, Barbara J. Tarasevich
Abstract
Significance
Protein binding is important to many biological processes such as biomineralization, cell signaling, and enzyme interactions. We found that protein binding is key in explaining how single amino acid changes in amelogenin can lead to adverse effects on the biomineralization of hydroxyapatite (HAP) in tooth enamel. A normal amount of protein adsorption resulted in HAP formation and the enzymatic removal of protein from HAP surfaces by MMP20 for the wild-type amelogenin, rpM179. Excessive protein binding, however, inhibited HAP formation and slowed the removal of protein by MMP20 for T21I, P41T, and P71T single amino acid variants. Excessive protein binding may be an important factor in explaining how single amino acid variants cause the
amelogenesis imperfecta
phenotype in vivo.
