<?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 6 Issue 1</issue_number>
<issue_period>2015 (January - March)</issue_period>
<title>PROTEIN MODELING AND DRUG DOCKING STUDIES ON ROTEIN TARGET OF EAE IUNTIMIN (E COLI)) BY BIOACTIVE ONSTITUENTS OF PHYLLANTHUS EMBLICA </title>
<abstract>The background of the present  lessThan i greaterThan Insilico lessThan /i greaterThan  studies, was to find out the potential protein target in Eae  lessThan i greaterThan iuntimin (E coli)  lessThan /i greaterThan and deliver the 3 D structure and to find out the best inhibitors of the virulence protein. Alkaloids from medicinally important plant  lessThan i greaterThan Phyllanthus emblica lessThan /i greaterThan  ( lessThan i greaterThan Phyllantidine and Phyllanthine lessThan /i greaterThan ) were used for the above purpose using molecular drug docking techniques. The lessThan i greaterThan  Phyllanthine lessThan /i greaterThan ,  lessThan i greaterThan Phyllantidine lessThan /i greaterThan  and the commercial antibiotic gentamicine potentially inhibited the target protein Eae  lessThan i greaterThan iuntimin (E coli)  lessThan /i greaterThan  . Based on the molecular drug docking and binding affinities of the target protein Eae  lessThan i greaterThan iuntimin (E coli)  lessThan /i greaterThan  it was found that the Amla alkaloid lessThan i greaterThan  Phyllanthine lessThan /i greaterThan  showed high binding values than  lessThan i greaterThan Phyllantidine lessThan /i greaterThan  and the existing drug  lessThan i greaterThan Gentamicine. lessThan /i greaterThan </abstract>
<authors>S.K.SUNDAR AND S.U.ANUSHA</authors>
<keywords>Drug docking, Virulence factor, Alkaloids</keywords>
<pages>297-304</pages>
</article>
</Journal>
