The importance of whole protein extracts from different types of human teeth in modulating the process of teeth biomineralization is reported. There are two crucial features in protein molecules that result in efficient teeth biomineralization. Firstly, the unique secondary structure characteristics within these proteins i.e. the exclusive presence of a large amount of intrinsic disorder and secondly, the presence of post-translational modifications (PTM) like phosphorylation and glycosylation within these protein molecules. The present study accesses the structural implications of PTMs in the tooth proteins through scanning electron microscopy and transmission electron microscopy. The deglycosylated/dephosphorylated protein extracts failed to form higher-order mineralization assemblies. Furthermore, through nanoparticle tracking analysis (NTA) we have shown that dephosphorylation and deglycosylation significantly impact the biomineralization abilities of the protein extract and resulted in smaller sized clusters. Hence, we propose these post-translational modifications are indispensable for the process of teeth biomineralization. In addition to basic science, this study would be worth consideration while designing of biomimetics architecture for an efficient peptide-based teeth remineralization strategy.
Keywords: biomineralization; human teeth; intrinsically disordered proteins; post-translational modifications; scanning electron microscopy; transmission electron microscopy.