Dynamic interactions of amelogenin with hydroxyapatite surfaces are dependent on protein phosphorylation and solution pH.

ABSTRACT: Amelogenin, the predominant extracellular matrix protein secreted by ameloblasts, has been shown to be essential for proper tooth enamel formation. In this study, amelogenin adsorption to hydroxyapatite (HAP) surfaces, a prototype for enamel mineral, has been studied using a quartz crystal microbalance (QCM) to interrogate effects of protein phosphorylation and solution pH. Dynamic flow-based experiments were conducted at pH 7.4 and 8.0 using native phosphorylated porcine amelogenin (P173) and recombinant non-phosphorylated porcine amelogenin (rP172). Loading capacities (μmol/m²) on HAP surfaces were calculated under all conditions and adsorption affinities (K_ad) were calculated when Langmuir isotherm conditions appeared to be met. At pH 8.0, binding characteristics w

SUBMITTER: Connelly C 

PROVIDER: S-EPMC5096982 | biostudies-literature | 2016 Dec

REPOSITORIES: biostudies-literature