Xxiv международная медико-биологическая конференция молодых исследователей Фундаментальная наука и клиническая

POSSIBLE PATHWAYS OF AMYLOID FIBRIL 
FORMATION ON THE EXAMPLE OF INSULIN PROTEIN
Соколович О.А., студ., Дорошевич А.К., студ., 
Саган В.В., студ. 
Международный государственный экологический институт 
имени А. Д. Сахарова, филиал БГУ,
Минск, Республика Беларусь
Научный руководитель: Богданова Н.В., ст. преп.
Research of the structure of ordered protein aggregates — amyloid 
fibrils, the influence of the native protein structure and external conditions 
on the process of fibrillation a very important topic for research nowadays. 
The formation of various structures by the prion mechanism is convincing 
proof. This show how one protein can form various structures, including 
amyloids and amyloid-like fibrils, due to changes in conformation. 
Especially it became relevant when it turned out that improper folding 
of some proteins can cause pathological aggregations and lead to the 
development of many neurodegenerative diseases, such as Alzheimer's 
disease and Parkinson's disease, T2DM etc. But it should be noted that 
not all amyloids and various amyloid-like fibrils are associated with 
neurodegenerative diseases, and this property is inherent in many proteins. 
Although, despite such a variety of proteins, the amyloid fibrils, that formed 
are similar to each other at first blush and represent stacked antiparallel 
β-structures directed perpendicular to the fibril axis. Amyloid fibrils can 
be straight or twisted, it can contain many protofilaments that line up 
parallel to the fibril axis or twist relatively to each other. It can be imagined 
that amyloid fibrils are antiparallel β-sheets twisted into a spiral; a cavity is 
formed inside the spiral, like a cylinder.
An important difference between protein folding into a native structure 
and the formation of amyloid fibrils is that when folding into a native 
structure, a correspondence between the amino acid sequence and 
the uniqueness of the folded state is assumed, whereas during amyloid 
formation, the same polypeptide sequence can form fibrils of different 
morphologies. Currently we can distinguish three ways of the formation 
of amyloid fibrils depending on the nucleus size. The first suggests that 

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fibrillogenesis can occur through assembly of insulin monomers. The 
second assumed that precursors of fibrils are dimers. The third suggests 
that precursors of fibrils are oligomers.
Research of the identities of the formation of amyloid fibrils based on 
insulin may be of significant importance for the improvement of insulin 
therapy in patients with diabetes mellitus.

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