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Lysozyme Fibrils Alter the Mechanism of Insulin Amyloid Aggregation

Published version
Peer-reviewed

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Authors

Ziaunys, Mantas 
Sakalauskas, Andrius 
Smirnovas, Vytautas  ORCID logo  https://orcid.org/0000-0002-1829-5455

Abstract

Protein aggregation into amyloid fibrils is linked to multiple disorders. The understanding of how natively non-harmful proteins convert to these highly cytotoxic amyloid aggregates is still not sufficient, with new ideas and hypotheses being presented each year. Recently it has been shown that more than one type of protein aggregates may co-exist in the affected tissue of patients suffering from amyloid-related disorders, sparking the idea that amyloid aggregates formed by one protein may induce another protein’s fibrillization. In this work, we examine the effect that lysozyme fibrils have on insulin amyloid aggregation. We show that not only do lysozyme fibrils affect insulin nucleation, but they also alter the mechanism of its aggregation.

Description

Keywords

insulin fibrils, lysozyme fibrils, amyloid aggregation, aggregation mechanism

Journal Title

International Journal of Molecular Sciences

Conference Name

Journal ISSN

1422-0067

Volume Title

22

Publisher

MDPI
Sponsorship
Lietuvos Mokslo Taryba (S-SEN-20-3)