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

dc.contributor.authorGarvey, Megan
dc.contributor.authorMeehan, Sarah
dc.contributor.authorGras, Sally L.
dc.contributor.authorSchirra, Horst J.
dc.contributor.authorCraik, David J
dc.contributor.authorVan der Weerden, Nicole L.
dc.contributor.authorAnderson, Marilyn
dc.contributor.authorGerrard, Juliet A.
dc.contributor.authorCarver, John
dc.date.accessioned2015-12-10T23:04:03Z
dc.date.issued2013
dc.date.updated2016-02-24T10:25:44Z
dc.description.abstractThe 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.
dc.identifier.issn1570-9639
dc.identifier.urihttp://hdl.handle.net/1885/62212
dc.publisherElsevier
dc.sourceBiochimica et Biophysica Acta: Proteins & Proteomics
dc.subjectKeywords: 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
dc.titleA radish seed antifungal peptide with a high amyloid fibril-forming propensity
dc.typeJournal article
local.bibliographicCitation.issue8
local.bibliographicCitation.lastpage1623
local.bibliographicCitation.startpage1615
local.contributor.affiliationGarvey, Megan, University of Adelaide
local.contributor.affiliationMeehan, Sarah, University of Cambridge
local.contributor.affiliationGras, Sally L., University of Melbourne
local.contributor.affiliationSchirra, Horst J., University of Queensland
local.contributor.affiliationCraik, David J, University of Queensland
local.contributor.affiliationVan der Weerden, Nicole L., La Trobe University
local.contributor.affiliationAnderson , Marilyn , La Trobe University
local.contributor.affiliationGerrard, Juliet A., University of Canterbury
local.contributor.affiliationCarver, John, College of Physical and Mathematical Sciences, ANU
local.contributor.authoremailu1571001@anu.edu.au
local.contributor.authoruidCarver, John, u1571001
local.description.embargo2037-12-31
local.description.notesImported from ARIES
local.identifier.absfor030406 - Proteins and Peptides
local.identifier.absseo970103 - Expanding Knowledge in the Chemical Sciences
local.identifier.ariespublicationu4005981xPUB677
local.identifier.citationvolume1834
local.identifier.doi10.1016/j.bbapap.2013.04.030
local.identifier.scopusID2-s2.0-84879040264
local.identifier.thomsonID000321802200019
local.identifier.uidSubmittedByu4005981
local.type.statusPublished Version

Downloads

Original bundle

Now showing 1 - 1 of 1
No Thumbnail Available
Name:
01_Garvey_A_radish_seed_antifungal_2013.pdf
Size:
1.98 MB
Format:
Adobe Portable Document Format