ИСТИНА

Misfolding of some proteins, including plasma proteins, can lead to loss of their functional activity and to aggregation to the filiform nanostructure - fibrils. Fibril formation is a consequence of pathological processes in the body and can lead to several diseases such as Alzheimer's disease and Parkinson's and type II diabetes. In recent works it was shown that in some special cases of external influences, that simulating the pathological processes in the body (glycation, oxidative stress, and others.) albumin may form fibrils. This fact is quite interesting, since in the native state albumin comprises 67% alpha-helical structures whereas the fibrils is mainly composed of beta-list. Thus, fibril formation of albumin involve several processes leading to restructuring of polypeptide chain, in particular, the protein passes through intermediate disordered state "molten globule". In the literature, there is no complete models of the processes involved in the formation of fibrils albumin. Thus, this project aims to study the initial stage of the processes involved in the formation of fibrils from serum albumin. Studing was performed in vitro under the various external factors by small angle Xray scattering technique.The measurements were done for BSAsolution pH 3.0 and 7.4 on synchrotron station DICSY. For evaluation of protein conformational properties two parameters have been chosen - gyration radius and value of integral under “molten globule” peak at Kratky plot. The vector decomposition on native and final state was done for the dynamic evaluation of the processe.