Inhibition of Leishmania infantum Trypanothione Reductase by New Aminopropanone Derivatives Interacting with the NADPH Binding Site.

ABSTRACT:

Background

As a result of the paucity of treatment, Leishmaniasis continues to provoke about 60,000 deaths every year worldwide. New molecules are needed, and drug discovery research is oriented toward targeting proteins crucial for parasite survival. Among them, trypanothione reductase (TR) is of remarkable interest owing to its vital role in Leishmania species protozoan parasite life. Our previously identified compound 1 is a novel chemotype endowed with a unique mode of TR inhibition thanks to its binding to a formerly unknown but druggable site at the entrance of the NADPH binding cavity, absent in human glutathione reductase (hGR).

Methods

We designed and synthesized new 3-amino-1-arylpropan-1-one derivatives structurally related to compound 1 and e

SUBMITTER: Madia VN 

PROVIDER: S-EPMC9823735 | biostudies-literature | 2023 Jan

REPOSITORIES: biostudies-literature