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Lysozyme Fibrils Alter the Mechanism of Insulin Amyloid Aggregation
| Content Provider | MDPI |
|---|---|
| Author | Ziaunys, Mantas Sakalauskas, Andrius Sneideris, Tomas Smirnovas, Vytautas |
| Copyright Year | 2021 |
| Description | 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. |
| Starting Page | 1775 |
| e-ISSN | 14220067 |
| DOI | 10.3390/ijms22041775 |
| Journal | International Journal of Molecular Sciences |
| Issue Number | 4 |
| Volume Number | 22 |
| Language | English |
| Publisher | MDPI |
| Publisher Date | 2021-02-10 |
| Access Restriction | Open |
| Subject Keyword | International Journal of Molecular Sciences Biophysics Insulin Fibrils Lysozyme Fibrils Amyloid Aggregation Aggregation Mechanism |
| Content Type | Text |
| Resource Type | Article |
