The self-assembly of the tooth enamel protein, amelogenin
Teeth consist of highly organized columns and sheets of nanocrystals of hydroxyapatite that can grow up to millimetres in length, but with a limited width and breadth of around 50nm. The growth of these crystals utilizes a self-assembled extracellular amelogenin matrix for organization and direction. As well as forming a macroscale matrix, amelogenin can also self-assemble into smaller structures called nanospheres, which have a hydrodynamic radius of about 15-20nm and are made up of 50-100 protein monomers. In this talk, I will discuss recent biophysical research on the substructure of nanospheres and how this might affect how they function. In addition, I will discuss the destabilization of amelogenin via two missense mutations (T21I and P40T) that are known to cause amelogenesis imperfecta, a hereditary disease.
This is a weekly series of informal talks given primarily by members of the soft condensed matter and statistical mechanics groups, but is also open to members of other groups and external visitors. The aim of the series is to promote discussion and learning of various topics at a level suitable to the broad background of the group. Everyone is welcome to attend..