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Antifungal properties of a peptide derived from the signal peptide of the HIV‐1 regulatory protein, Rev
Author(s) -
Lee Juneyoung,
Lee Dong Gun
Publication year - 2009
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.03.063
Subject(s) - calcein , peptide , vesicle , antifungal , chemistry , in vitro , in vivo , liposome , biochemistry , membrane , biophysics , microbiology and biotechnology , biology
Antifungal effects of nuclear entry inhibitory signal peptide of HIV‐1 Rev protein (Rev‐NIS) were investigated. Rev‐NIS contained potent antifungal activities without hemolytic effects. To understand the antifungal mechanism(s), in vivo and in vitro fluorescent studies were conducted. Flow cytometric analysis with bis‐(1,3‐dibutylbarbituric acid) trimethine oxonol [DiBAC 4 (3)] and calcein‐leakage measurement from large unilamellar vesicles (LUVs) indicated that Rev‐NIS depolarized and disrupted the fungal membranes. These results were further confirmed by using giant unilamellar vesicles (GUVs). The current study suggests that Rev‐NIS exerts its antifungal activity with membrane‐active mechanism(s).