Molecular analysis of chemically modified tau from pathological view points : fibrous aggregation and environmental interactions

为了阐明磷酸化作用对tau蛋白淀粉样蛋白形成的分子机制，我们对它们的聚集特性和淀粉样蛋白结构进行了详细的分析。本文建立了淀粉样蛋白临界浓度的精确测定方法、X射线纤维衍射与计算机模拟相结合的方法。分析发现磷酸残基上的电荷、磷酸在肽上的位置以及聚集体内的特异性分子内和分子间相互作用的关键作用。

In order to elucidate molecualr mechanisms of phosphorylation effects on tau amyloidgenesis, their aggregation properties and amyloid stuctures were analyzed in detail. A varity of methods used for the analaysis such as a precise determination method of critical concentration of amyloidgenesis and a combination of X-ray fiber diffraction and computer simulation methods were established here. The analysis found critical roles of charges on phosphate residues, position of phosphate on the peptides, and specipic intra-and inter-molecular interaction within the aggregate.