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|Title:||A radish seed antifungal peptide with a high amyloid fibril-forming propensity|
Van der Weerden, N.
|Citation:||BBA - Proteins and Proteomics, 2013; 1834(8):1615-1623|
|Publisher:||Elsevier Science BV|
|Organisation:||Institute for Photonics & Advanced Sensing (IPAS)|
|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|
|Appears in Collections:||IPAS publications|
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