Department of Biomaterials, Max Planck Institute of Colloids and Interfaces, Potsdam, Germany.
Biomacromolecules. 2010 Feb 8;11(2):369-76. doi: 10.1021/bm900983b.
It is well-known that amelogenin self-assembles to form nanoparticles, usually referred to as amelogenin nanospheres, despite the fact that not much is known about their actual shape in solution. In the current paper, we combine SAXS and DLS to study the three-dimensional shape of the recombinant amelogenins rP172 and rM179. Our results show for the first time that amelogenins build oblate nanoparticles in suspension using experimental approaches that do not require the proteins to be in contact with a support material surface. The SAXS studies give evidence for the existence of isolated amelogenin nano-oblates with aspect ratios in the range of 0.45-0.5 at pH values higher than pH 7.2 and show an aggregation of these nano-oblates at lower pH values. The role of the observed oblate shape in the formation of chain-like structures at physiological conditions is discussed as a key factor in the biomineralization of dental enamel.
众所周知,釉原蛋白会自组装形成纳米颗粒,通常称为釉原蛋白纳米球,尽管人们对其在溶液中的实际形状知之甚少。在本论文中,我们结合 SAXS 和 DLS 研究了重组釉原蛋白 rP172 和 rM179 的三维形状。我们的结果首次表明,釉原蛋白在悬浮液中使用不需要蛋白质与支撑材料表面接触的实验方法构建扁长形纳米颗粒。SAXS 研究证明了在 pH 值高于 7.2 的情况下,存在具有 0.45-0.5 纵横比的孤立釉原蛋白纳米扁球体,并在较低的 pH 值下显示出这些纳米扁球体的聚集。讨论了所观察到的扁形形状在生理条件下形成链状结构中的作用,这是牙釉质生物矿化的关键因素。