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Amyloid aggregation and membrane activity of the antimicrobial peptide uperin 3.5

Martin, Lisandra; Kubeil, Clemens; Piantavigna, Stefania; Tikkoo, Tarun; Gray, Nicholas P.; John, Torsten; Calabrese, Antonio N.; Liu, Yanqin; Hong, Yuning; Hossain, Mohammed A.; Carver, John

Description

Amyloid fibrils are highly ordered, β‐sheet rich forms of aggregated peptides and proteins that are associated with a variety of pathological human disorders, including Alzheimer's and Parkinson's diseases. Amyloid fibril‐forming peptides may be functionally related to antimicrobial peptides, despite differing significantly in sequence and structure. Specifically, their interaction with lipid membranes has mechanistic similarities. The 17‐amino acid peptide uperin 3.5 (U3.5) from an Australian...[Show more]

CollectionsANU Research Publications
Date published: 2018
Type: Journal article
URI: http://hdl.handle.net/1885/164253
Source: Peptide Science
DOI: 10.1002/pep2.24052

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