Abstract
AbstractAmelogenins are hydrophobic proteins that constitute more than 90% of the secretory stage enamel matrix. The assembly of amelogenin into nanospheres has been postulated to be a key factor in controlling the structural organization of the enamel extracellular matrix framework, which provides the scaffolding for the elongated and oriented growth of enamel apatite crystals. To get insight into the structure and function of amelogenin in controlling the process of crystal growth we have utilized two different approaches to investigate adsorption of amelogenin nanospheres onto charged surfaces: A) analysis of adsorption of amelogenin onto hydroxyapatite crystals by means of Langmuir Model for protein adsorption. B) analysis of amelogenin mono or multi-layer formation by sequential adsorption process onto auto-assembled polyelctrolytes films. Our data indicate that amelogenin nanospheres adsorb onto the surface of apatite crystals as binding units with defined adsorption sites. We found that amelogenin nanospheres are negatively charged and a monolayer of these nanospheres adsorbed in an irreversible way on positively ending polyelectrolyte multilayers most likely through electrostatic interactions.
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