MAIN


©1996-2013 All Rights Reserved. Online Journal of Bioinformatics . You may not store these pages in any form except for your own personal use. All other usage or distribution is illegal under international copyright treaties. Permission to use any of these pages in any other way besides the before mentioned must be gained in writing from the publisher. This article is exclusively copyrighted in its entirety to OJB publications. This article may be copied once but may not be, reproduced or re-transmitted without the express permission of the editors. This journal satisfies the refereeing requirements (DEST) for the Higher Education Research Data Collection (Australia). Linking:To link to this page or any pages linking to this page you must link directly to this page only here rather than put up your own page.


OJBTM

Online Journal of Bioinformatics ©

Volume 14 (2): 146-159, 2013


In Silico inhibitors for Plasmodium falciparum lactate dehydrogenase

 

Madhu Sudhana Saddala, K. Kranthi Kumar and A. Usha Rani*

 

 

Division of Environmental Biology, Department of Zoology, DBT Bioinformatics Center, Sri Venkateswara University, Tirupati  A.P., India.

 

ABSTRACT

 

Madhu Sudhana Saddala, K. Kranthi Kumar and A. Usha Rani, In Silico Inhibitors for Plasmodium falciparum lactate dehydrogenase, Onl J Bioinform., 14 (2): 146-159, 2013  Dysruption of receptor sites on Plasmodium falciparum lactate dehydrogenase (PfLDH) could inhibit the malarial parasite. We describe Virtual gossypol-like compounds that might inhibit PfLDH by interacting with amino acids on its receptors. Multiple sequence alignment of PfLDH with Plasmodium spp was performed with Clustal W1.83. A phylogenetic tree was constructed with Tree Viewer 3.0.   Protein structure was refined by 2ns molecular simulation and energy minimization. Compounds (1997) were then screened Virtually (Autodoc Vina) for similarity with gossypol from The Zinc database for binding capacity. Docking showed that sequentially ZINC27313038, ZINC13759138, ZINC13759183, ZINC13759202, ZINC59648667 and ZINC11159075 k.cal/mol had most binding capacity with PfLDH compared with gossipol. These compounds bind by hydrogen bonds and hydrophobic interactions and may  inhibit PfLDH mediated glycolysis The cavity surrounded by Ile31, Gly99, Asn140, Gly32, Thr101, Gly29 Thr97, Asp53, Met30, Phe52 and Glu122 may possibly be manipulated to inhibit the parasite.

 

Keywords: PfLDH, NAMD, MDSimulation, Virtual screening, Docking, Zinc database


MAIN

 

FULL-TEXT(SUBSCRIPTION)