Drug Invention Today
ISSN NO: 0975-7619
Drug Invention Today (DIT) was first published in 2009 by JPR Solutions. It is a journal, which publishes reviews, research papers and short communications . 
• Novel Drug Delivery Systems • Nanotechnology & Nanomedicine • Biotechnology related pharmaceutical technology • Polymeric bio-conjugates • Biological macromolecules • Biomaterials • Drug Information • Drug discovery/development • Screening of drugs from natural & synthetic origins • Novel therapeutic strategies • Combinatorial chemistry and parallel synthesis • Clinical trials • Case Reports
 Impact FactorTM ( India ) = 0.897 as on date (08.05.2017)
  Scopus Indexed ( link http://www.scimagojr.com/journalsearch.php?q=21100202909&tip=sid&clean=0)
Journal Metrics for this   Drug Invention Today (Source ID: 21100202909): 2014 (SNIP) Source Normalized Impact Per Paper : 0.402; SCImago Journal Rank (SJR):0.301; Impact Per Publication : 0.517 (Top level : Life Science)
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Manuscripts Published

Journal: Drug Invention Today , Volume: 3, Issue: July
Article Id: JPRS-BSN-00001084
Title: In- silico analysis of pyrazinamide resistance of Mycobacterium sp.
Category: Biomaterials ( Synthetic and Natural )
Section: Research Article
Country: India
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Pyrazinamide (PZA), a prodrug used for the treatment of tuberculosis, requires conversion into its active form, pyrazinoic acid (POA), by the bacterial enzyme pyrazinamidase (PZase), which is encoded by the 561- nucleotide pncA gene. The present study was aimed at predicting the active site and drug binding characteristics of mycobacterial PZase by constructing homology models and docking with PZA. Despite 99% identity in the amino acid sequences of PZases from M. tuberculosis and M. bovis, significant variations in their three dimensional structure was observed. PZase of M. kansasii also differed from all other PZases. Active sites of PZases were identified by docking studies and were found to be partially conserved in the PZases. These results suggest that PZA resistance of these organisms is not necessarily due to a non-functional PZase but by alternate mechanism. On comparing with reported mutations responsible for PZA resistance in M. tuberculosis, the mutations His51Gln, Trp68Arg, His71Glu, Tyr103His and Cys138Tyr might have direct role in the enzyme activity as these occur in the active site whereas the other mutations cause resistance by bringing structural changes in the functional PZase.