A radish seed antifungal peptide with a high amyloid fibril-forming propensity
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...[Show more]
|Collections||ANU Research Publications|
|Source:||Biochimica et Biophysica Acta: Proteins & Proteomics|
|01_Garvey_A_radish_seed_antifungal_2013.pdf||2.03 MB||Adobe PDF||Request a copy|
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