Document Type

Article

Publication Date

2018

Publication Title

Frontiers in Chemistry

Keywords

oxovanadium, decavanadate, phosphatase inhibition, Leishmania, acid phosphatase, enzyme studies

Abstract

Leishmaniasis is an endemic disease affecting a diverse spectra of populations, with 1.6 million new cases reported each year. Current treatment options are costly and have harsh side effects. New therapeutic options that have been previously identified, but still underappreciated as potential pharmaceutical targets, are Leishmania secreted acid phosphatases (SAP). These acid phosphatases, which are reported to play a role in the survival of the parasite in the sand fly vector, and in homing to the host macrophage, are inhibited by orthovanadate and decavanadate. Here, we use L. tarentolae to further evaluate these inhibitors. Using enzyme assays, and UV-visible spectroscopy, we investigate which oxovanadium starting material (orthovanadate or decavanadate) is a better inhibitor of L. tarentolae secreted acid phosphatase activity in vitro at the same total moles of vanadium. Considering speciation and total vanadium concentration, decavanadate is a consistently better inhibitor of SAP in our conditions, especially at low substrate:inhibitor ratios.

Funding Source

We would like to thank the Chemistry Department at Illinois State University, and the Kurz Fellowship (to BD) for partial funding of this research.

DOI

10.3389/fchem.2018.00109

Comments

First published in Frontiers in Chemistry April 2018, volume 6. https://doi.org/10.3389/fchem.2018.00109

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner are credited and that the original publication in this journal is cited, in accordance with accepted academic practice.

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