The Peculiarities of Oligomerization of Smooth Muscle Titin and Skeletal Muscle Myosin-Binding Protein C.

Autor: Bobyleva, L. G., Timchenko, M. A., Yakupova, E. I., Vikhlyantsev, I. M., Bobylev, A. G.
Zdroj: Biophysics; Jun2023, Vol. 68 Issue 3, p365-368, 4p
Abstrakt: Protein oligomers are important intermediates in the formation of amyloid fibrils. In amyloidosis, for example, Alzheimer's disease, oligomers can have a toxic effect on cells. This paper describes the distinctive features of oligomerization of multidomain muscle proteins, smooth muscle titin, and myosin-binding protein C (C-protein) of skeletal muscles consisting of FnIII-like and IgC2-like domains and capable of forming amyloid amorphous aggregates in vitro. Under conditions of low ionic strength (below physiological values), the C-protein formed stable oligomers that were not involved in further aggregation. Smooth muscle titin formed oligomers under conditions of high ionic strength (μ ~ 0.6), which were precursors of amyloid amorphous aggregates of this protein.The results we obtained expand the understanding of the process of protein aggregation. [ABSTRACT FROM AUTHOR]
Databáze: Complementary Index
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