A radish seed antifungal peptide with a high amyloid fibril-forming propensity
Date
2013
Authors
Garvey, Megan
Meehan, Sarah
Gras, Sally L.
Schirra, Horst J.
Craik, David J
Van der Weerden, Nicole L.
Anderson, Marilyn
Gerrard, Juliet A.
Carver, John
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Volume Title
Publisher
Elsevier
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.
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Keywords
Keywords: alanine; amyloid; cysteine; Raphanus sativus antifungal protein 19; unclassified drug; amyloid; antifungal agent; defensin; peptide fragment; thiazole derivative; thioflavine; antifungal activity; article; atomic force microscopy; controlled study; freezi Amyloid fibril; Antifungal peptide; Antimicrobial peptide; Protein aggregation; Protein misfolding
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Source
Biochimica et Biophysica Acta: Proteins & Proteomics
Type
Journal article
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2037-12-31
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