Premium
Direct cell penetration of the antifungal peptide, MMGP1, in Candida albicans
Author(s) -
Pushpanathan Muthuirulan,
Rajendhran Jeyaprakash,
Jayashree Sathyanarayanan,
Sundarakrishnan Balakrishnan,
Jayachandran Seetharaman,
Gunasekaran Paramasamy
Publication year - 2012
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.2445
Subject(s) - internalization , candida albicans , peptide , cell penetrating peptide , endocytosis , cytotoxicity , flow cytometry , chemistry , biochemistry , endocytic cycle , fluorescence microscope , biology , microbiology and biotechnology , cell , fluorescence , in vitro , physics , quantum mechanics
An antifungal peptide, MMGP1, was recently identified from marine metagenome. The mechanism of cellular internalization of this peptide in Candida albicans was studied using fluorescein 5–isothiocynate (Sigma, California, USA) labeling followed by fluorescence microscopy and flow cytometry analyses. The peptide could enter C . albicans cells even at 4 °C, where all energy‐dependent transport mechanisms are blocked. In addition, the peptide internalization was not affected by the endocytic inhibitor, sodium azide. The kinetic study has shown that the peptide was initially localized on cell membrane and subsequently internalized into cytosol. The MMGP1 treatment exhibited time‐dependent cytotoxicity in C . albicans as evidenced by SYTOX Green (Molecular Probes Inc., Eugene, Oreg) uptake. Copyright © 2012 European Peptide Society and John Wiley & Sons, Ltd.