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The Pathway of Amyloid Aggregation of Titin

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Abstract

The process of amyloid aggregation is quite complex and poorly studied. In this paper, summarizing the previously obtained results on the aggregation of the multidomain smooth muscle protein titin, we tried to complement the idea of its amyloid aggregation by presenting a new, in our opinion, possible mechanism. The main conclusion is that the ability of titin to form amorphous aggregates seems to be the only possible means of aggregation of this protein. Apparently, only individual sections of the molecules, and not the entire protein, are involved in the formation of the amyloid structure in amorphous aggregates of smooth muscle titin. This feature distinguishes titin from other amyloid or amyloid-like proteins due to the large size of the molecule. The possible energy landscape underlying the formation of amyloid aggregates of titin is discussed.

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Funding

The work was supported by the Russian Science Foundation, project no. 22-24-00805.

Author information

Authors and Affiliations

  1. Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, 142290, Pushchino, Moscow oblast, Russia

    L. G. Bobyleva, T. A. Uryupina, M. A. Timchenko, I. M. Vikhlyantsev & A. G. Bobylev

  2. Institute of Physicochemical and Biological Problems of Soil Science, Russian Academy of Sciences, 142290, Pushchino, Moscow oblast, Russia

    S. N. Udaltsov

  3. Institute of Fundamental Medicine and Biology, Kazan Federal University, 420012, Kazan, Russia

    I. M. Vikhlyantsev

Authors
  1. L. G. Bobyleva
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  2. T. A. Uryupina
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  3. M. A. Timchenko
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  4. S. N. Udaltsov
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  5. I. M. Vikhlyantsev
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Correspondence to A. G. Bobylev.

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Translated by E. Puchkov

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Bobyleva, L.G., Uryupina, T.A., Timchenko, M.A. et al. The Pathway of Amyloid Aggregation of Titin. BIOPHYSICS 68, 1085–1091 (2023). https://doi.org/10.1134/S0006350923060039

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