A radish seed antifungal peptide with a high amyloid fibril-forming propensity
dc.contributor.author | Garvey, Megan | |
dc.contributor.author | Meehan, Sarah | |
dc.contributor.author | Gras, Sally L. | |
dc.contributor.author | Schirra, Horst J. | |
dc.contributor.author | Craik, David J | |
dc.contributor.author | Van der Weerden, Nicole L. | |
dc.contributor.author | Anderson, Marilyn | |
dc.contributor.author | Gerrard, Juliet A. | |
dc.contributor.author | Carver, John | |
dc.date.accessioned | 2015-12-10T23:04:03Z | |
dc.date.issued | 2013 | |
dc.date.updated | 2016-02-24T10:25:44Z | |
dc.description.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. | |
dc.identifier.issn | 1570-9639 | |
dc.identifier.uri | http://hdl.handle.net/1885/62212 | |
dc.publisher | Elsevier | |
dc.source | Biochimica et Biophysica Acta: Proteins & Proteomics | |
dc.subject | 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 | |
dc.title | A radish seed antifungal peptide with a high amyloid fibril-forming propensity | |
dc.type | Journal article | |
local.bibliographicCitation.issue | 8 | |
local.bibliographicCitation.lastpage | 1623 | |
local.bibliographicCitation.startpage | 1615 | |
local.contributor.affiliation | Garvey, Megan, University of Adelaide | |
local.contributor.affiliation | Meehan, Sarah, University of Cambridge | |
local.contributor.affiliation | Gras, Sally L., University of Melbourne | |
local.contributor.affiliation | Schirra, Horst J., University of Queensland | |
local.contributor.affiliation | Craik, David J, University of Queensland | |
local.contributor.affiliation | Van der Weerden, Nicole L., La Trobe University | |
local.contributor.affiliation | Anderson , Marilyn , La Trobe University | |
local.contributor.affiliation | Gerrard, Juliet A., University of Canterbury | |
local.contributor.affiliation | Carver, John, College of Physical and Mathematical Sciences, ANU | |
local.contributor.authoremail | u1571001@anu.edu.au | |
local.contributor.authoruid | Carver, John, u1571001 | |
local.description.embargo | 2037-12-31 | |
local.description.notes | Imported from ARIES | |
local.identifier.absfor | 030406 - Proteins and Peptides | |
local.identifier.absseo | 970103 - Expanding Knowledge in the Chemical Sciences | |
local.identifier.ariespublication | u4005981xPUB677 | |
local.identifier.citationvolume | 1834 | |
local.identifier.doi | 10.1016/j.bbapap.2013.04.030 | |
local.identifier.scopusID | 2-s2.0-84879040264 | |
local.identifier.thomsonID | 000321802200019 | |
local.identifier.uidSubmittedBy | u4005981 | |
local.type.status | Published Version |
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