Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/79036
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Type: Journal article
Title: A radish seed antifungal peptide with a high amyloid fibril-forming propensity
Author: Garvey, M.
Meehan, S.
Gras, S.
Schirra, H.
Craik, D.
Van der Weerden, N.
Anderson, M.
Gerrard, J.
Carver, J.
Citation: BBA - Proteins and Proteomics, 2013; 1834(8):1615-1623
Publisher: Elsevier Science BV
Issue Date: 2013
ISSN: 1570-9639
1878-1454
Organisation: Institute for Photonics & Advanced Sensing (IPAS)
Statement of
Responsibility: 
Megan Garvey, Sarah Meehan, Sally L. Gras, Horst J. Schirra, David J. Craik, Nicole L. Van der Weerden, Marilyn A. Anderson, Juliet A. Gerrard, John A. Carver
Abstract: The amyloid fibril-forming ability of two closely related antifungal and antimicrobial peptides derived from plant defensin proteins has been investigated. As assessed by sequence analysis, thioflavin T binding, transmission electron microscopy, atomic force microscopy and X-ray fiber diffraction, a 19 amino acid fragment from the C-terminal region of Raphanus sativus antifungal protein, known as RsAFP-19, is highly amyloidogenic. Further, its fibrillar morphology can be altered by externally controlled conditions. Freezing and thawing led to amyloid fibril formation which was accompanied by loss of RsAFP-19 antifungal activity. A second, closely related antifungal peptide displayed no fibril-forming capacity. It is concluded that while fibril formation is not associated with the antifungal properties of these peptides, the peptide RsAFP-19 is of potential use as a controllable, highly amyloidogenic small peptide for investigating the structure of amyloid fibrils and their mechanism of formation.
Keywords: Amyloid fibril; Antifungal peptide; Antimicrobial peptide; Protein misfolding; Protein aggregation
RMID: 0020130752
DOI: 10.1016/j.bbapap.2013.04.030
Appears in Collections:IPAS publications

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