Development of Small Molecule Inhibitors of Entamoeba histolytica MTA Nucleosidases (MTNs)

Merlin Bope Miongolo, Boise State University
Lacey Wayment, College of Idaho
John Thurston, College of Idaho
Danny Xu, Idaho State University
Ken Cornell (Mentor), Boise State University

W18

Abstract

Entamoeba histolytica is a parasitic protozoan that causes 50,000-100,000 deaths annually, and untold millions of cases of severe dysentery, mostly in developing countries. The incidence and severity has increased due to the recent emergence of chronic infections and drug-resistant parasite strains. This underscores the need to develop new anti-parasitic drugs with novel targets within the parasite. The Entamoeba enzyme 5’ Methylthioadenosine Nucleosidase (EH MTN) is a potential target since it is required to salvage essential adenine and methionine required for parasite survival. In this study, we examined a series of non-nucleoside small molecule inhibitors (SMIs) of EH MTN that were initially identified by in silico screening against the known E. coli MTN enzyme structure. The results of our work show that a number of the inhibitors exert low micromolar inhibition constants, and are potential lead compounds for further drug development.

 

Development of Small Molecule Inhibitors of Entamoeba histolytica MTA Nucleosidases (MTNs)

Entamoeba histolytica is a parasitic protozoan that causes 50,000-100,000 deaths annually, and untold millions of cases of severe dysentery, mostly in developing countries. The incidence and severity has increased due to the recent emergence of chronic infections and drug-resistant parasite strains. This underscores the need to develop new anti-parasitic drugs with novel targets within the parasite. The Entamoeba enzyme 5’ Methylthioadenosine Nucleosidase (EH MTN) is a potential target since it is required to salvage essential adenine and methionine required for parasite survival. In this study, we examined a series of non-nucleoside small molecule inhibitors (SMIs) of EH MTN that were initially identified by in silico screening against the known E. coli MTN enzyme structure. The results of our work show that a number of the inhibitors exert low micromolar inhibition constants, and are potential lead compounds for further drug development.