PNNL

Abstract

Although amelogenin comprises the vast majority of the matrix that templates calcium phosphate nucleation during enamel formation, other proteins, particularly enamelin, are also known to play an important role in the formation of enamel’s intricate architecture. However, there is little understanding of the interplay between amelogenin and enamelin in controlling processes of mineral nucleation and growth. Here we used an in vitro model to investigate the impact of enamelin co-assembly with amelogenin on calcium phosphate nucleation for a range of enamelin-to-amelogenin ratios. We found that amelogenin alone is a weak promoter of nucleation, but addition of enamelin enhanced nucleation rates in a highly non-linear, non-monotonic manner reaching a sharp maximum at a ratio of 1:50. We provide a phenomenological model to explain this effect that assumes only isolated enamelin proteins can act as sites of enhanced nucleation, while enamelin oligomers cannot. Even when co-assembly is random, the model reproduces the observed behavior, suggesting a simple means to tightly control the timing and extent of nucleation and phase transformation by amelogenin and enamelin.