About the pathway of amyloid aggregation of titin

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Abstract

The process of amyloid aggregation is quite complex and poorly understood. In this work, having summarized previously obtained results on the aggregation of the multidomain smooth muscle protein titin, an attempt has been made to expand understanding of this process, and a new possible mechanism by which amyloid aggregation of titin may occur is delineated. Our main conclusion is that the ability of titin to form amorphous aggregates seems to be the only possible way of aggregation of this protein. Most likely, only separate parts of the molecules, but not the whole protein, are involved in the formation of the amyloid structure in amorphous aggregates of smooth muscle titin. This feature, given the large size of the protein molecule, distinguishes titin from other amyloid or amyloid-like proteins. The paper discusses the potential energy landscape underlying the formation of titin amyloid aggregates.

About the authors

L. G Bobyleva

Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences

Pushchino, Moscow Region, Russia

T. A Uryupina

Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences

Pushchino, Moscow Region, Russia

M. A Timchenko

Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences

Pushchino, Moscow Region, Russia

S. N Udaltsov

Institute of Physicochemical and Biological Problems of Soil Science, Russian Academy of Sciences

Pushchino, Moscow Region, Russia

I. M Vikhlyantsev

Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences;Institute of Fundamental Medicine and Biology, Kazan Federal University

Pushchino, Moscow Region, Russia;Kazan, Russia

A. G Bobylev

Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences

Email: bobylev1982@gmail.com
Pushchino, Moscow Region, Russia

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