Oroidin inhibits the activity of the multidrug resistance target Pdr5p from yeast plasma membranes

Fernanda R da Silva; Ana Claudia Tessis; Patricia F Ferreira; Luciana P Rangel; Aline S Garcia-Gomes; Fabio R Pereira; Roberto G S Berlinck; Guilherme Muricy; Antonio Ferreira-Pereira

doi:10.1021/np1006247

Oroidin inhibits the activity of the multidrug resistance target Pdr5p from yeast plasma membranes

J Nat Prod. 2011 Feb 25;74(2):279-82. doi: 10.1021/np1006247. Epub 2011 Jan 5.

Authors

Fernanda R da Silva¹, Ana Claudia Tessis, Patricia F Ferreira, Luciana P Rangel, Aline S Garcia-Gomes, Fabio R Pereira, Roberto G S Berlinck, Guilherme Muricy, Antonio Ferreira-Pereira

Affiliation

¹ Laboratório de Bioquímica Microbiana, Departamento de Microbiologia Geral, IMPPG, Universidade Federal do Rio de Janeiro, CEP 21941-590, Rio de Janeiro, RJ, Brazil.

PMID: 21207971
DOI: 10.1021/np1006247

Abstract

Oroidin was isolated from the marine sponge Agelassventres and inhibited the activity and function of Pdr5p, an enzyme responsible for the multidrug resistance phenotype in Saccharomyces cerevisiae. This compound may help in the development of new drugs that reverse this dangerous phenotype of pathogenic yeast and fungi.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

ATP-Binding Cassette Transporters / drug effects*
Animals
Cell Membrane / chemistry
Cell Membrane / metabolism
Drug Resistance, Multiple / genetics
Marine Biology
Molecular Structure
Porifera / chemistry
Pyrroles / chemistry
Pyrroles / isolation & purification
Pyrroles / pharmacology*
Saccharomyces cerevisiae / enzymology*
Saccharomyces cerevisiae / metabolism
Saccharomyces cerevisiae Proteins / drug effects*

Substances

ATP-Binding Cassette Transporters
PDR5 protein, S cerevisiae
Pyrroles
Saccharomyces cerevisiae Proteins
oroidin