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The Kinetics of Amyloid Fibrillar Aggregation of Uperin 3.5 Is Directed by the Peptide's Secondary Structure

John, Torsten; Dealey, Tiara J A; Gray, Nicholas P.; Patil, Nitin A; Hossain, Mohammed A.; Abel, Bernd; Carver, John; Hong, Yuning; Martin, Lisandra

Description

Many peptides aggregate into insoluble β-sheet rich amyloid fibrils. Some of these aggregation processes are linked to age-related diseases, such as Alzheimer’s disease and type 2 diabetes. Here, we show that the secondary structure of the peptide uperin 3.5 directs the kinetics and mechanism of amyloid fibrillar aggregation. Uperin 3.5 variants were investigated using thioflavin T fluorescence assays, circular dichroism spectroscopy, and structure prediction methods. Our results suggest that...[Show more]

CollectionsANU Research Publications
Date published: 2019
Type: Journal article
URI: http://hdl.handle.net/1885/203844
Source: Biochemistry
DOI: 10.1021/acs.biochem.9b00536

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