Journal of Peptide Science · 2012 · 22 citations · 11 references
Life SciencesCell BiologyMicrobiologyEndocytosisMicrobial PhysiologyMycologyAntifungal AgentsAntimicrobial PeptidesCell-penetrating PeptidesFungal Cell BiologyFungal PathogenesisFungal PhysiologyAntifungal PeptidesAntimicrobial Peptide ActivityCandida Albicans InfectionCell Penetration MechanismsCellular Internalization PathwaysCytotoxicity AssaysTransport Mechanisms
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.
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Effects of histatin 5 and derived peptides on Candida albicans
A.L.A Ruissen, Jasper Groenink, Eva J. Helmerhorst et al. · Biochemical Journal · 2001 · 96 citations · Full text