<i>In Vitro</i> and <i>In Vivo</i> Characterization of Potent Antileishmanial Methionine Aminopeptidase 1 Inhibitors
Felipe Rodriguez, Sarah Finney John, Eva Iniguez, Sebastian Montalvo, Karina Michael, Lyndsey White, Dong Liang, Omonike A. Olaleye, Rosa A. Maldonado
Abstract
Leishmania major is the causative agent of cutaneous leishmaniasis (CL). No human vaccine is available for CL, and current drug regimens present several drawbacks, such as emerging resistance, severe toxicity, medium effectiveness, and/or high cost. Thus, the need for better treatment options against CL is a priority. In the present study, we validate the enzyme methionine aminopeptidase 1 of L. major (MetAP1 Lm ), a metalloprotease that catalyzes the removal of N-terminal methionine from peptides and proteins, as a chemotherapeutic target against CL infection.
Topics & Concepts
MethionineAminopeptidaseIn vivoIn vitroLeishmaniasisPharmacologyEnzymeLeishmaniaToxicityLeishmania majorChemistryBiologyBiochemistryMicrobiologyAmino acidImmunologyLeucineBiotechnologyParasite hostingWorld Wide WebOrganic chemistryComputer sciencePeptidase Inhibition and AnalysisResearch on Leishmaniasis StudiesSynthesis and Biological Evaluation