Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/84863
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dc.contributor.authorJayaraman, Premkumaren
dc.contributor.authorDaniel, Lim Chu Siangen
dc.contributor.authorSiddiqi, Mohammad Imranen
dc.contributor.authorDhillon, Sarinder Kauren
dc.contributor.authorSakharkar, Kishore R.en
dc.contributor.authorSakharkar, Meena K.en
dc.date.accessioned2014-10-17T07:06:45Zen
dc.date.accessioned2019-12-06T15:52:33Z-
dc.date.available2014-10-17T07:06:45Zen
dc.date.available2019-12-06T15:52:33Z-
dc.date.copyright2013en
dc.date.issued2013en
dc.identifier.citationJayaraman, P., Sakharkar, K. R., Daniel, L. C. S., Siddiqi, M. I., Dhillon, S. K., et al. (2013). Hybrid-drug design targeting pseudomonas aeruginosa DHPS and DHFR. Frontiers in bioscience, 5, 864-882.en
dc.identifier.urihttps://hdl.handle.net/10356/84863-
dc.identifier.urihttp://hdl.handle.net/10220/24068en
dc.description.abstractIn this study, we successfully present the dual-target design hypothesis to inhibit both dihydropteroate synthase (DHPS) and dihydrofolate reductase (DHFR) enzymes using a novel scheme that integrates our previous antibiotic-phytochemical interaction data, fragment combination and knowledge-based methods. Both the enzymes are well established antibacterial targets from folate biosynthesis pathway and their synergistic modulation by a single hybrid entity may have profound therapeutic benefits. Evaluation of the designed hybrid compounds based on their physico-chemical properties has indicated them as promising drug candidates with drug-like pharmacotherapeutic profiles. In addition, the stereo-electronic properties such as HOMO, LUMO and MEP maps calculated by quantum chemical methods gave a good correlation with the common pharmacophoric features required for dual-site interactions. Furthermore, docking and dynamics simulation studies reveal that the designed hybrid compounds have favorable binding affinity and stability in both pterin-binding site of DHPS and folate-binding site of DHFR by forming strong hydrogen bonds and hydrophobic interactions with key active-site residues. Looking forward this study could serve as a prospective lead in the process of new natural-product based hybrid-drugs development.en
dc.language.isoenen
dc.relation.ispartofseriesFrontiers in bioscienceen
dc.rights© 2013 Frontiers in Bioscience.en
dc.subjectDRNTU::Science::Biological sciencesen
dc.titleHybrid-drug design targeting pseudomonas aeruginosa DHPS and DHFRen
dc.typeJournal Articleen
dc.contributor.researchBioMedical Engineering Research Centreen
dc.identifier.doihttp://dx.doi.org/10.2741/E666en
dc.identifier.urlhttps://www.bioscience.org/2013/v5e/af/666/fulltext.htmen
item.grantfulltextnone-
item.fulltextNo Fulltext-
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