硫黄素-T 与淀粉样纤维相互作用形成的原纤维。

Thioflavin-T excimer formation upon interaction with amyloid fibers.

机构信息

Institut de Nanociència i nanotecnologia, Departament Fisicoquímica, Universitat de Barcelona, Joan XXIII s/n, E-08028-Barcelona, Spain.

出版信息

Chem Commun (Camb). 2013 Jun 28;49(51):5745-7. doi: 10.1039/c3cc42040j.

DOI:10.1039/c3cc42040j

PMID:23687656

Abstract

The molecular mechanism of the Thioflavin-T (Th-T) binding to amyloids remains unknown. By combining experimental analysis of Th-T excitation and emission spectra with theoretical calculations we suggest that Th-T fluorescence changes upon interaction with amyloids may arise from the formation of an excimer with an oblique angle of ~120 degrees.

摘要

噻唑黄素（Th-T）与淀粉样蛋白结合的分子机制尚不清楚。通过结合噻唑黄素激发和发射光谱的实验分析和理论计算，我们提出噻唑黄素与淀粉样蛋白相互作用时荧光强度的变化可能是由于形成了一个倾斜角度约为 120 度的斜交二聚体。