Department of Chemistry, University of Washington, Seattle, WA 98195, USA.
Magn Reson Chem. 2007 Dec;45 Suppl 1:S32-47. doi: 10.1002/mrc.2123.
Proteins are found to be involved in interaction with solid surfaces in numerous natural events. Acidic proteins that adsorb to crystal faces of a biomineral to control the growth and morphology of hard tissue are only one example. Deducing the mechanisms of surface recognition exercised by proteins has implications to osteogenesis, pathological calcification and other proteins functions at their adsorbed state. Statherin is an enamel pellicle protein that inhibits hydroxyapatite nucleation and growth, lubricates the enamel surface, and is recognized by oral bacteria in periodontal diseases. Here, we highlight some of the insights we obtained recently using both thermodynamic and solid state NMR measurements to the adsorption process of statherin to hydroxyapatite. We combine macroscopic energy characterization with microscopic structural findings to present our views of protein adsorption mechanisms and the structural changes accompanying it and discuss the implications of these studies to understanding the functions of the protein adsorbed to the enamel surfaces.
在许多自然事件中，人们发现蛋白质与固体表面相互作用。吸附到生物矿物晶体表面以控制硬组织生长和形态的酸性蛋白质就是一个例子。推断蛋白质表面识别的机制对成骨、病理性钙化和其他蛋白质在吸附状态下的功能具有重要意义。牙釉蛋白是一种牙釉质蛋白，能抑制羟基磷灰石成核和生长、润滑牙釉质表面，并被牙周病中的口腔细菌识别。在这里，我们强调了我们最近使用热力学和固态 NMR 测量方法对牙釉蛋白吸附到羟基磷灰石的吸附过程的一些见解。我们将宏观能量特性与微观结构发现相结合，提出了我们对蛋白质吸附机制及其伴随结构变化的看法，并讨论了这些研究对理解吸附到牙釉质表面的蛋白质功能的意义。
