Molecular docking analysis of curcumin analogues as human neutrophil elastase inhibitors
In the present study, we aimed to dock 17 different ligands of curcumin analogues with that of human neutrophil elastase. Molecular descriptors analysis using Molinspiration online tool was carried out including investigation on human neutrophil elastase putative binding sites using Discovery Studio. The molecular physicochemical analysis revealed that all of the curcumin analogues complied well with the five rules of thumb. With regard to bioactivity score, compound 17 has exhibited least score towards nuclear receptor ligand (0.05) and enzyme inhibitor (0.10) compared to all other ligands. Compounds 2, 4 and 13 exhibited the maximum interaction energy (-40 kcal/mol). Interestingly, seven compounds namely 3, 11-14, 16 and 17 interacted well with Arg147 amino acid residue. The present study outcomes, therefore, might provide new insight in understanding these 17 curcumin analogues as potential candidates for human neutrophil elastase inhibitory agents.
Anonymous. Chemspider ( http://www.chemspider.com).
Anonymous. ACD, ChemSketch Version 12, Advanced Chemistry Development Inc., Toronto, ON, Canada, 2009 (http://www.acdlabs.com/download/chemsk.html).
Anonymous. Research collaborator for structural bioinformatics Protein data bank (RCSB PDB) (http://www.rcsb.org).
Anonymous, Molinspiration Database (http://www.molinspiration.com).
Bode W, Meyer EJr, Powers JC. Human leukocyte and porcine pancreatic elastase: X-ray crystal structures, mechanism, substrate specificity, and mechanism-based inhibitors. Biochemistry 1989; 28: 1951-63.
Bustanji Y, Taha MO, Almasri IM, Al-Ghussein MA, Mohammad MK, Alkhatib HS. Inhibition of glycogen synthase kinase by curcumin: Investigation by simulated molecular docking and subsequent in vitro/in vivo evaluation. J Enzyme Inhib Med Chem. 2009; 24: 771-78.
Crocetti L, Schepetkin IA, Cilibrizzi A, Graziano A, Vergelli C, Giomi D, Khlebnikov AI, Quinn MT, Giovannoni MP. Optimization of N-benzoylindazole derivatives as inhibitors of human neutrophil elastase. J Med Chem. 2013; 56: 6259-72.
Furness MS, Robinson TP, Ehlers T, Hubbard RB, Arbiser JL, Goldsmith DJ, Bowen JP. Antiangioge-nic agents: studies on fumagillin and curcumin analogs. Curr Pharm Des. 2005; 11: 357-73.
Girija CR, Karunakar P, Poojari CS, Begum NS, Syed AA. Molecular docking studies of curcumin derivatives with multiple protein targets for procarcinogen activating enzyme inhibition. J Proteomics Bioinform. 2010; 3: 200-03.
Gupta SC, Prasad S, Kim JH, Patchva S, Webb LJ, Priyadarsini IK, Aggarwal BB. Multi-targeting by curcumin as revealed by molecular interaction studies. Nat Prod Rep. 2011; 28: 1937-55.
Hosoya T, Nakata A, Yamasaki F, Abas F, Shaari K, Lajis NH, Morita H. Curcumin-like diarylpentanoid analogues as melanogenesis inhibitors. J Nat Med. 2012; 66: 166-76.
Istyastono EP. Docking studies of curcumin as a potential lead compound to develop novel dipeptydyl peptidase-4 inhibitors. Indo J Chem. 2009; 9: 132-36.
Jankun J, Aleem AM, Malgorzewicz S, Szkudlarek M, Zavodszky MI, Dewitt DL, Feig M, Selman SH, Skrzypczak-Jankun E. Synthetic curcuminoids modulate the arachidonic acid metabolism of human platelet 12-lipoxygenase and reduce sprout formation of human endothelial cells. Mol Cancer Ther. 2006; 5: 1371-82.
Jantan I, Bukhari SN, Lajis NH, Abas F, Wai LK, Jasamai M. Effects of diarylpentanoid analogues of curcumin on chemiluminescence and chemotactic activities of phagocytes. J Pharm Pharmacol. 2012; 64: 404-12.
Lam KW, Tham CL, Liew CY, Israf DA, Syahida A, Mohd Abdul Rahman B, Lajis NH. Synthesis and evaluation of DPPH and anti-inflammatory activities of 2, 6 bis benzylidenecyclohexanone and pyrazoline derivatives. Med Chem Res. 2012; 21: 333-44.
Lee KH, Ab Aziz FH, Syahida A, Abas F, Shaari K, Israf DA, Lajis NH. Synthesis and biological evaluation of curcumin-like diarylpentanoid analogues for anti-inflammatory, antioxidant and anti-tyrosinase activities. Eur J Med Chem. 2009; 44: 3195-3200.
Lipinski CA, Lombardo F, Dominy BW, Feeney PJ. Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings. Adv Drug Deliv Rev. 2001; 46: 3-26.
Liu M, Yuan M, Luo M, Bu X, Luo HB, Hu X. Binding of curcumin with glyoxalase I: Molecular docking, molecular dynamics simulations, and kinetics analysis. Biophys Chem. 2010; 147: 28-34.
Liu Z, Xie Z, Jones W, Pavlovicz RE, Liu S, Yu J, Li PK, Lin J, Fuchs JR, Marcucci G, Li C, Chan KK. Curcumin is a potent DNA hypomethylation agent. Bioorg Med Chem Lett. 2009; 19: 706-09.
Lucas SD, Costa E, Guedes RC, Moreira R. Structure based virtual screening for discovery of novel human neutrophil elastase inhibitors. Med Res Rev. 2013; 33: E73-101.
Majhi A, Rahman GM, Panchal S, Das J. Binding of curcumin and its long chain derivatives to the activator binding domain of novel protein kinase C. Bioorg Med Chem. 2010; 18: 1591-98.
Mukhopadhyay A, Basu N, Ghatak N, Gujral PK. Anti-inflammatory and irritant activities of curcumin analogues in rats. Agents Actions. 1982; 12: 508-15.
Nirmal N, Praba GO, Velmurugan D. Modeling studies on phospholipase A2-inhibitor complexes. Indian J Biochem Biophys. 2008; 45: 256-62.
Padhye S, Banerjee S, Chavan D, Pandye S, Swamy KV, Ali S, Li J, Dou QP, Sarkar FH. Fluorocurcumins as cyclooxygenase-2 inhibitor: Molecular docking, pharmacokinetics and tissue distribution in mice. Pharm Res. 2009; 26: 2438-45.
Pham CT. Neutrophil serine proteases: specific regulators of inflammation. Nat Rev Immunol. 2006; 6: 541-50.
Radhakrishnan N, Lam KW, Intan SI. Molecular docking analysis of natural compounds as Human neutrophil elastase (HNE) inhibitors. J Chem Pharm Res. 2013; 5: 337-41.
Sangeetha S, Ranjitha S, Murugan K, Ramesh kumar G. Breast cancer specific histone deacetylase inhibitors and lead discovery using molecular docking and descriptor study. Trends in Bioinform. 2013; 6: 25-44.
Sahoo BK, Gosh KS, Dasgupta S. An investigation of the molecular interactions of diacetylcurcumin with ribonuclease A. Protein Pept Lett. 2009; 16: 1485-95.
Selvam C, Jachak SM, Thilagavathi R, Chakraborti AK. Design, synthesis, biological evaluation and molecular docking of curcumin analogues as antioxidant, cyclooxygenase inhibitory and anti-inflammatory agents. Bioorg Med Chem Lett. 2005; 15: 1793-97.
Siedle B, Cisielski S, Murillo R, Loser B, Castro V, Klaas CA, Hucke O, Labahn A, Melzig MF, Merfort I. Sesquiterpene lactones as inhibitors of human neutrophil elastase. Bioorg Med Chem. 2002; 10: 2855-61.
Sivamani P, Singaravelu G, Thiagarajan V, Jayalakshmi T, Rameshkumar G. Comparative molecular docking analysis of essential oil constituents as elastase inhibitors. Bioinform. 2012; 8: 457-60.
Singh A, Mishra A, Gautam MK, Verma S, Goel RK. Regulation of wound strength by Curcuma longa: In silico and in vivo evidences. J Pharm Res. 2012; 5: 4734-38.
Shen L, Ji HF. Insights into the inhibition of xanthine oxidase by curcumin. Bioorg Med Chem Lett. 2009; 19: 5990-93.
Sui Z, Salto R, Li J, Craik C, Ortiz de Montellano PR. Inhibition of the HIV-1 and HIV-2 proteases by curcumin and curmumin boron complexes. Bioorg Med Chem. 1993; 1: 415-22.
Takeuchi T, Ishidoh T, Iijima H, Kuriyama I, Shimazaki N, Koiwai O, Kuramochi K, Kobayashi S, Sugawara F, Sakaguchi K, Yoshida H, Mizushina Y. Structural relationship of curcumin derivatives binding to the BRCT domain of human DNA polymerase lambda. Genes Cells. 2006; 11: 223-35.
Wang YJ, Pan MH, Cheng AL, Lin LI, Ho YS, Hsieh CY, Lin JK. Stability of curcumin in buffer solutions and characterization of its degradation products. J Pharm Biomed Anal. 1997; 15: 1867-76.
Wu G, Robertson DH, Brooks CL, Vieth M. Detailed analysis of grid-based molecular docking: A case study of Cdocker-A CHARMm-based MD docking algorithm. J Comput Chem. 2003; 24: 1549-62.
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