Discovery of novel inhibitors targeting enoyl-acyl carrier protein reductase in Plasmodium falciparum by structure-based virtual screening. Academic Article

abstract

• There is a dire need for novel therapeutics to treat the virulent malarial parasite, Plasmodium falciparum. Recently, the X-ray crystal structure of enoyl-acyl carrier protein reductase (ENR) in complex with triclosan has been determined and provides an opportunity for the rational design of novel inhibitors targeting the active site of ENR. Here, we report the discovery of several compounds by virtual screening and their experimental validation as high potency PfENR inhibitors.

authors

• Sacchettini, James

published proceedings

• Biochem Biophys Res Commun

altmetric score

• 6

author list (cited authors)

• Nicola, G., Smith, C. A., Lucumi, E., Kuo, M. R., Karagyozov, L., Fidock, D. A., Sacchettini, J. C., & Abagyan, R.

citation count

• 30

complete list of authors

• Nicola, George||Smith, Colin A||Lucumi, Edinson||Kuo, Mack R||Karagyozov, Luchezar||Fidock, David A||Sacchettini, James C||Abagyan, Ruben

publication date

• July 2007

publisher

• Elsevier  Publisher

published in

• Biochemical and Biophysical Research Communications  Journal

keywords

• Animals
• Antimalarials
• Binding Sites
• Caco-2 Cells
• Crystallography, X-Ray
• Drug Design
• Drug Evaluation, Preclinical
• Enoyl-(acyl-carrier-protein) Reductase (nadh)
• Humans
• Hydrogen Bonding
• Kinetics
• Malaria
• Models, Molecular
• Plasmodium Falciparum
• Triclosan

PubMed Central ID

• 17509532

Digital Object Identifier (DOI)

• 10.1016/j.bbrc.2007.04.113

start page

• 686

end page

• 691

volume

• 358

issue

• 3

URL

• http://dx.doi.org/10.1016/j.bbrc.2007.04.113