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Article

Trypsin Induced Degradation of Amyloid Fibrils

1
Laboratory of Structural Dynamics, Stability and Folding of Proteins, Institute of Cytology, Russian Academy of Sciences, 4 Tikhoretsky Avenue, 194064 St. Petersburg, Russia
2
Laboratory of Cell Morphology, Institute of Cytology, Russian Academy of Sciences, 4 Tikhoretsky Avenue, 194064 St. Petersburg, Russia
3
Institute of Physics, Nanotechnology and Telecommunications, Peter the Great St. Petersburg Polytechnic University, Polytechnicheskaya 29, 195251 St. Petersburg, Russia
*
Author to whom correspondence should be addressed.
Academic Editor: Ludmilla A. Morozova-Roche
Int. J. Mol. Sci. 2021, 22(9), 4828; https://doi.org/10.3390/ijms22094828
Received: 1 April 2021 / Revised: 26 April 2021 / Accepted: 30 April 2021 / Published: 2 May 2021
(This article belongs to the Special Issue Pathological and Functional Amyloid Fibrils)
Proteolytic enzymes are known to be involved in the formation and degradation of various monomeric proteins, but the effect of proteases on the ordered protein aggregates, amyloid fibrils, which are considered to be extremely stable, remains poorly understood. In this work we study resistance to proteolytic degradation of lysozyme amyloid fibrils with two different types of morphology and beta-2-microglobulun amyloids. We showed that the proteolytic enzyme of the pancreas, trypsin, induced degradation of amyloid fibrils, and the mechanism of this process was qualitatively the same for all investigated amyloids. At the same time, we found a dependence of efficiency and rate of fibril degradation on the structure of the amyloid-forming protein as well as on the morphology and clustering of amyloid fibrils. It was assumed that the discovered relationship between fibrils structure and the efficiency of their degradation by trypsin can become the basis of a new express method for the analysis of amyloids polymorphism. Unexpectedly lower resistance of both types of lysozyme amyloids to trypsin exposure compared to the native monomeric protein (which is not susceptible to hydrolysis) was attributed to the higher availability of cleavage sites in studied fibrils. Another intriguing result of the work is that the cytotoxicity of amyloids treated with trypsin was not only failing to decline, but even increasing in the case of beta-2-microglobulin fibrils. View Full-Text
Keywords: amyloid fibrils; proteolytic degradation; trypsin; stability; fragmentation; cytotoxicity; florescent probes; thioflavin T (ThT); 1-anilinonaphthalene-8-sulphonate (ANS) amyloid fibrils; proteolytic degradation; trypsin; stability; fragmentation; cytotoxicity; florescent probes; thioflavin T (ThT); 1-anilinonaphthalene-8-sulphonate (ANS)
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MDPI and ACS Style

Stepanenko, O.V.; Sulatsky, M.I.; Mikhailova, E.V.; Stepanenko, O.V.; Kuznetsova, I.M.; Turoverov, K.K.; Sulatskaya, A.I. Trypsin Induced Degradation of Amyloid Fibrils. Int. J. Mol. Sci. 2021, 22, 4828. https://doi.org/10.3390/ijms22094828

AMA Style

Stepanenko OV, Sulatsky MI, Mikhailova EV, Stepanenko OV, Kuznetsova IM, Turoverov KK, Sulatskaya AI. Trypsin Induced Degradation of Amyloid Fibrils. International Journal of Molecular Sciences. 2021; 22(9):4828. https://doi.org/10.3390/ijms22094828

Chicago/Turabian Style

Stepanenko, Olga V., Maksim I. Sulatsky, Ekaterina V. Mikhailova, Olesya V. Stepanenko, Irina M. Kuznetsova, Konstantin K. Turoverov, and Anna I. Sulatskaya. 2021. "Trypsin Induced Degradation of Amyloid Fibrils" International Journal of Molecular Sciences 22, no. 9: 4828. https://doi.org/10.3390/ijms22094828

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