ИСТИНА

Formation of ordered aggregates - amyloid fibrils - is associated with the occurrence of many serious diseases such as Alzheimer's, Parkinson's, prion disease, type II diabetes, etc. Despite the great interest in this issue, the processes underlying the abnormal protein aggregation and its pathological manifestations in the disease are poorly understood. The successful solution of these problems depends on the fundamental knowledge of the structure and properties of amyloid fibrils. The aim of this work is the investigation of alpha-synuclein amyloid fibrils depositions of which accompanies Parkinson's disease. The main tool for the comparative study of the structure of amyloid fibrils used in our work is the fluorescent dye thioflavin T (ThT). To study the interaction of this dye with amyloid fibrils, we developed a special approach based on the absorption and fluorescence spectroscopy of solutions obtained by equilibrium microdialysis [1,2]. With the use of this approach it was defined ThT-amyloid fibrils binding parameters and the characteristics of the bound dye. The estimated parameters were analyzed in comparison with the existing information about ThT binding to insulin, lysozyme, Abeta-petptid, and beta-microglobulin amyloid fibrils [3]. Obtained results confirm the notion that the fibrils on the basis of different proteins are distinct and that proposed approach can be used to compare and study of their structure.