<?xml version="1.0" encoding="utf-8"?>
<Journal>
<Journal-Info>
<name>International Journal of Pharma and Bio Sciences</name>
<website>ijpbs.net</website>
<email>editorijpbs@rediffmail.com (or) editorofijpbs@yahoo.com (or) prasmol@rediffmail.com</email>
</Journal-Info>
<article>
<article-id pub-id-type='other'>10.22376/ijpbs.2019.10.1.p1-12</article-id>
<issue_number>Volume 3 Issue 3</issue_number>
<issue_period>2012 (July - September)</issue_period>
<title>Structural Insights On Brugia Malayi Transglutaminase With Cinnamoyl Derivatives - A Molecular Docking Approach </title>
<abstract>The parasite lessThan i greaterThan  Brugia malayi,  lessThan /i greaterThan one of the causative agents for human lymphatic filariasis, found endemic in tropical and sub tropical countries like India, Indonesia, Malaysia and Thailand. The enzyme transglutaminase (TGase) is involved in the growth and development stages of parasite. Transglutaminase has been found to be a better target for the anti filarial agents due to its critical role in the parasite's growth and development. In our study, we reported cinnamoyl derivatives as potent inhibitors for  lessThan i greaterThan Brugia malayi  lessThan /i greaterThan transglutaminase. The computational molecular docking approach was used to confirm the inhibition of cinnamoyl derivatives with the enzyme transglutaminase to block the growth and development of parasite  lessThan i greaterThan Brugia malayi lessThan /i greaterThan  and acts as a novel anti filarial agent. </abstract>
<authors>Srikumar P S And Rohini K</authors>
<keywords>Filariasis, Brugia malayi, Transglutaminase, Ramachandran plot, Molecular docking and Binding energy.</keywords>
<pages>998-1006</pages>
</article>
</Journal>
