Protein scaffolds direct the organization of amorphous precursors that transform into
mineralized tissues, but the templating mechanism remains elusive. Motivated by models for …

Mechanisms of protein-guided mineralization in enamel, leading to organized fibrillar apatite
nanocrystals, remain elusive. In vitro studies reveal recombinant human amelogenin …

Amelogenin (Amel) accelerates the nucleation of hydroxyapatite (HAP) in supersaturated
solutions of calcium phosphate (Ca− P), shortening the induction time (delay period), under …

As the hardest tissue formed by vertebrates, enamel represents nature's engineering
masterpiece with complex organizations of fibrous apatite crystals at the nanometer scale …

The organic matrix in forming enamel consists largely of the amelogenin protein self-
assembled into nanospheres that play a pivotal role in controlling the oriented and …

Under near-physiological pH, temperature, and ionic strength, amelogenin (Amel)
accelerates hydroxyapatite (HAP) nucleation kinetics, decreasing the induction time in a …

Amelogenin proteins play a critical role in controlling crystal growth and orientation into
highly organized calcium phosphate (Ca–P) minerals during tooth enamel formation …

Enamel matrix self-assembly has long been suggested as the driving force behind aligned
nanofibrous hydroxyapatite formation. We tested if amelogenin, the main enamel matrix …

Enamel, the outermost layer of teeth, is an acellular mineralized tissue that cannot
regenerate; the mature tissue is composed of high aspect ratio apatite nanocrystals …

Enamel is a highly organized hierarchical nanocomposite, which consists of parallel arrays
of elongated apatitic crystallites forming an intricate three-dimensional microstructure …