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Download fileGlutathione Transferases: Surrogate Targets for Discovering Biologically Active Compounds
journal contribution
posted on 2020-10-01, 17:14 authored by Muriel Barbier, Thomas Perrot, Guillaume Salzet, Nadine Amusant, Stéphane Dumarçay, Philippe Gérardin, Mélanie Morel-Rouhier, Rodnay Sormani, Eric GelhayeGlutathione transferases comprise
a large class of multifunctional
enzymes, some involved in detoxification pathways. Since these enzymes
are able to interact with potentially toxic molecules, they could
be used as targets to screen for compounds with biological activity.
To test this hypothesis, glutathione transferases (GSTs) from the
white-rot fungus Trametes versicolor have been used
to screen for antifungal molecules from a library of tropical wood
extracts. The interactions between a set of six GSTs from the omega
class and 116 extracts from 21 tropical species were quantified using
a high-throughput thermal shift assay. A correlation between these
interactions and the antifungal properties of the tested extracts
was demonstrated. This approach has been extended to the fractionation
of an Andira coriacea extract and led to the detection
of maackiain and lapachol in this wood. Altogether, the present results
supported the hypothesis that such detoxification enzymes could be
used to detect biologically active molecules.
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GSTglutathione transferasesantifungal propertiesantifungal moleculesAndira coriaceaCompounds Glutathione transferaseswood extractsdetoxification enzymesdetoxification pathwaysGlutathione Transferaseswhite-rot fungus Trametes versicoloromega classinteractionhypothesisshift assay116 extractsmultifunctional enzymes