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.
Highlights
The event of protein or peptide aggregation into amyloid fibrils is considered to be the cause of multiple disorders [1,2,3]
We show that do lysozyme fibrils increase the rate of insulin nucleation, but they have a peculiar effect on the actual mechanism of its aggregation
Considering that previously reported cases analyzed the interaction of amyloid proteins that had the ability of coming into contact in vivo [24,28,29,30,31,32], it was interesting to examine if such amyloid crossinteractions can occur between proteins that do not share a localization
Summary
The event of protein or peptide aggregation into amyloid fibrils is considered to be the cause of multiple disorders [1,2,3]. The conformational change of a protein’s structure, leading to the formation of a stable primary aggregation center (nucleus) [11] This is both the critical step in launching a cascade of protein aggregation, as well as the slowest step [12], which requires a plethora of events and factors to proceed in just the right way to achieve a stable nucleus [11]. Afterward, these primary nuclei elongate [13] by templating their structure [14] onto nearby homologous protein molecules and incorporating them into the aggregate’s structure. Additional secondary events have been proposed, which take place during aggregation, such as fibril ends of one type of amyloid serving as templates for partial misfolding of other proteins [17]
Sign-in/Register to view highlights & summary Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
