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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
Organisation: Institute for Photonics & Advanced Sensing (IPAS)
Statement of
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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