A radish seed antifungal peptide with a high amyloid fibril-forming propensity

Garvey, Megan, Meehan, Sarah, Gras, Sally L., Schirra, Horst, Craik, David J., Van der Weerden, Nicole L., Anderson, Marilyn A., Gerrard, Juliet A. and Carver, John A. (2013) A radish seed antifungal peptide with a high amyloid fibril-forming propensity. Biochimica et Biophysica Acta: Proteins and Proteomics, 1834 8: 1615-1623. doi:10.1016/j.bbapap.2013.04.030

Author Garvey, Megan
Meehan, Sarah
Gras, Sally L.
Schirra, Horst
Craik, David J.
Van der Weerden, Nicole L.
Anderson, Marilyn A.
Gerrard, Juliet A.
Carver, John A.
Title A radish seed antifungal peptide with a high amyloid fibril-forming propensity
Journal name Biochimica et Biophysica Acta: Proteins and Proteomics   Check publisher's open access policy
ISSN 1570-9639
Publication date 2013-08-01
Year available 2013
Sub-type Article (original research)
DOI 10.1016/j.bbapap.2013.04.030
Volume 1834
Issue 8
Start page 1615
End page 1623
Total pages 9
Place of publication Amsterdam: Netherlands
Publisher Elsevier
Language eng
Formatted 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.
Keyword Amyloid fibril
Antifungal peptide
Antimicrobial peptide
Protein aggregation
Protein misfolding
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ
Additional Notes Available online: 9 May 2013.

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2014 Collection
Institute for Molecular Bioscience - Publications
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Created: Thu, 06 Jun 2013, 01:28:22 EST by Susan Allen on behalf of Institute for Molecular Bioscience