| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10835988 | Peptides | 2011 | 7 Pages |
Abstract
⺠Tn-AFP1, a small peptide of 1230 Da was purified from the fruits of Trapa natans, showed antifungal activity against human pathogen, Candida tropicalis. ⺠The MIC and IC50 values were 32 μg/ml and 16 μg/ml against C. tropicalis. ⺠Sequence of the peptide was determined by tandem mass spectrometry and found to contain eleven amino acid residues, showed a single coil structure attached by a unique disulphide bond anticipated by in silico analysis. ⺠Tn-AFP1 downregulated MDR1 and ERG11 gene expression level and disrupted bioflim formation of C. tropicalis. ⺠In summary, this peptide could be used as a promising candidate for the development of more effective antimycotic compounds.
Keywords
TFARPMI-1640Candida tropicalisMDR1MICTrapa natansERG11LC–MS/MSCHCATrifluoroacetic acidα-cyano-4-hydroxycinnamic acidAFPMinimum inhibitory concentrationMatrix assisted laser desorption ionization time of flight mass spectrometryMALDI ToF MSFruitsAntifungal peptideAntifungal peptidesliquid chromatography tandem mass spectrometryhigh performance liquid chromatographyHPLC
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Authors
Santi M. Mandal, Ludovico Migliolo, Octavio L. Franco, Ananta K. Ghosh,