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