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- W2044285722 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." @default.
- W2044285722 created "2016-06-24" @default.
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- W2044285722 date "2013-08-01" @default.
- W2044285722 modified "2023-09-27" @default.
- W2044285722 title "A radish seed antifungal peptide with a high amyloid fibril-forming propensity" @default.
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- W2044285722 doi "https://doi.org/10.1016/j.bbapap.2013.04.030" @default.
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