Please use this identifier to cite or link to this item: http://hdl.handle.net/10321/3016
Title: Design, synthesis, anticancer, antimicrobial activities and molecular docking studies of novel quinoline bearing dihydropyridines
Authors: Nkosi, S'busiso Mfan'vele 
Anand, Krishnan 
Anandakumar, S. 
Singh, Sanil 
Chuturgoon, Anil A. 
Gengan, Robert Moonsamy 
Keywords: 2-Chloro-3-formylquinoline;Dihydropyridines;Molecular docking;Anti-cancer;Human mdm2
Issue Date: 2016
Publisher: Elsevier
Source: Nkosi. S M. 2016. Design, synthesis, anticancer, antimicrobial activities and molecular docking studies of novel quinoline bearing dihydropyridines. Journal of Photochemistry & Photobiology, B: Biology. 165: 266–276.
Abstract: A new series of eight quinoline bearing dihydropyridine derivatives (A1–A8) were synthesized in high yield and in short reaction time by a four component reaction of 2-chloro-3-fomyl quinoline, malononitrile, arylamines and dimethyl acetylenedicarboxylate in the presence of a catalytic amount of triethylamine. The compounds were fully characterized by IR, NMR and GC–MS. These compounds were screened for potential biological activity in an A549 lung cancer cell line and were also evaluated for their antibacterial activities against Pseudomonas aeruginosa ATCC 27853, Escherichia coli ATCC 25922 and Staphylococcus aureus ATCC 29213 whilst their molecular docking properties in an enzymatic system were also determined. Compounds A2, A3, A4 and A8 showed anti-proliferative activity; with A4 having the highest toxicity at 250 μg/mL and A8 has high toxicity at 125, 250 and 500 μg/mL, respectively. Antibacterial results indicated that A4 have significant activity against tested microorganisms at the minimum inhibitory concentration (MIC) values of 32 μg/mL against Pseudomonas aeruginosa and Escherichia coli,and 16μg/mL against Staphylococcus aureus. Docking of A1 with human mdm2 indicated the lowest binding energy (−6.111 Kcal/mol) thereby showing strong affinity of the ligand molecule with the receptor which has been stabilized by strong hydrogen bond interactions in the binding pocket. This confirms that A1 is a better inhibitor for E3 ubiquitin-protein ligase mdm2.
URI: http://hdl.handle.net/10321/3016
ISSN: 1011-1344 (print)
1873-2682 (online)
Appears in Collections:Research Publications (Applied Sciences)

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