By a News Reporter-Staff News Editor at Life Science Weekly -- Investigators publish new report on Proteobacteria. According to news reporting from Chandigarh, India, by NewsRx journalists, research stated, "Emergence of the multidrug-resistant pathogens has rendered the current therapies ineffective thereby, resulting in the need for new drugs and drug targets. The accumulating protein sequence data has initiated a drift from classical drug discovery protocols to structure-based drug designing."
The news correspondents obtained a quote from the research from Panjab University, "In the present study, in silico subtractive genomics approach was implemented to find a set of potential drug targets present in an opportunist bacterial pathogen, Acinetobacter baumannii (A. baumannii). Out of the 43 targets identified, further studies for protein model building and lead-inhibitor identification were carried out on two cell-essential targets, MurA and MurB enzymes (of A. baumannii designated as MurA(Ab) and MurB(Ab)) involved in the peptidoglycan biosynthesis pathway of bacteria. The homology model built for each of them was further refined and validated using various available programs like PROCHECK, Errat, ProSA energy plots, etc. Compounds showing activity against MurA and MurB enzymes of other organisms were collected from the literature and were docked into the active site of MurA(Ab) and MurB(Ab) enzymes. Three inhibitors namely, T6361, carbidopa, and aesculin, showed maximum Glide score, hydrogen bonding interactions with the key amino acid residues of both the enzymes and acceptable ADME properties. Furthermore, molecular dynamics simulation studies on MurA(Ab)-T6361 and MurB(Ab)-T6361 complexes suggested that the ligand has a high binding affinity with both the enzymes and the hydrogen bonding with the key residues were stable in the dynamic condition also."
According to the news reporters, the research concluded: "Therefore, these ligands have been propsed as dual inhibitors and promising lead compounds for the drug design against MurA(Ab) and MurB(Ab) enzymes."
For more information on this research see: Identification of Druggable Targets for Acinetobacter baumannii Via Subtractive Genomics and Plausible Inhibitors for MurA and MurB. Applied Biochemistry and Biotechnology, 2013;171(2):417-436. Applied Biochemistry and Biotechnology can be contacted at: Humana Press Inc, 999 Riverview Drive Suite 208, Totowa, NJ 07512, USA. (Springer - www.springer.com; Applied Biochemistry and Biotechnology - www.springerlink.com/content/0273-2289/)
Our news journalists report that additional information may be obtained by contacting N. Kaur, Panjab University, Sect 14, Dept. of Biochem, Chandigarh 160014, India. Additional authors for this research include M. Khokhar, V. Jain, P.V. Bharatam, R. Sandhir and R. Tewari (see also Proteobacteria).
Keywords for this news article include: Asia, India, Chandigarh, Moraxellaceae, Proteobacteria, Enzymes and Coenzymes, Gram-Negative Bacteria, Acinetobacter baumannii, Gram-Negative Aerobic Bacteria, Gram-Negative Aerobic Rods and Cocci
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