Abstract:
:Due to recent emergence of fungal pathogens resistant to current antifungal therapies, several studies have been focused on screening of plant peptides to find novel compounds having antifungal activities. Here, a novel antifungal plant peptide, with molecular mass of 1230 Da was purified from fruits of Trapa natans by reverse phase high performance liquid chromatography using 300SB-C18 column and named as Tn-AFP1. Determination of complete amino acid sequences of this peptide by tandem mass spectrometry showed to contain following eleven amino acid residues: LMCTHPLDCSN. Purified Tn-AFP1 showed the inhibition of Candida tropicalis growth in vitro and disrupted the biofilm formation in a concentration dependent manner. It also showed downregulation of MDR1 and ERG11 gene expression in real time-PCR analysis. In silico molecular modeling predicted the structure of Tn-AFP1 as a single coil attached by a unique disulfide bond. Characterization of Tn-AFP1 could contribute in designing novel derivative(s) of this peptide for the development of more effective antimycotic compounds.
journal_name
Peptidesjournal_title
Peptidesauthors
Mandal SM,Migliolo L,Franco OL,Ghosh AKdoi
10.1016/j.peptides.2011.06.020subject
Has Abstractpub_date
2011-08-01 00:00:00pages
1741-7issue
8eissn
0196-9781issn
1873-5169pii
S0196-9781(11)00245-2journal_volume
32pub_type
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