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Binding studies of trans-resveratrol with superoxide dismutase (SOD1): Docking assessment and Thermoanalysis

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Submitted   Dec 31, 2018
Published   Feb 22, 2019
Issue    Vol 1 No 1 (2019)
DOI   10.25082/JPBR.2019.01.003

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Janhvi Dureja
University Institute of Pharmaceutical Sciences, Panjab University, Chandigarh 160014, India
Renu Chadha corresponding author
University Institute of Pharmaceutical Sciences, Panjab University, Chandigarh 160014, India
Maninder Karan
University Institute of Pharmaceutical Sciences, Panjab University, Chandigarh 160014, India
Akshita Jindal
University Institute of Pharmaceutical Sciences, Panjab University, Chandigarh 160014, India
Kunal Chadha
University Institute of Pharmaceutical Sciences, Panjab University, Chandigarh 160014, India

Abstract

The binding pursuits of trans-resveratrol (t-RSV), an amazing health supplement are investigated with an antioxidant enzyme, superoxide dismutase (SOD1). The aim of the study is to dock t-RSV on the adrenaline binding site on SOD1 in order to explore its potential to act as a safety net against amyotrophic lateral sclerosis (ALS), a fatal neurodegenerative disorder that affects motor neurons. In silico GLIDE docking methodology and in vitro microcalorimetry technique is utilized for the investigation of binding parameters of t-RSV with SOD1. The study provides useful and distinct information about the amino acids involved in the interactions at molecular level along with the nature of forces involved in binding of t-RSV with SOD1.  The docking analysis using the scoring functions of Schrodinger's Glide package depicts that GLU100, PRO28, LYS23, TRP32 residues of the peptide backbone on SOD 1 interact with phenolic groups of t-RSV. The information on thermodynamic parameters, i.e. binding constant (Kb), free energy (ΔG) and enthalpy (ΔH) generated through calorimetric titrations suggests that the reaction between t-RSV and SOD 1 is spontaneous and exothermic. Both the studies are found to be in close agreement with each other based as far as the magnitude of binding constant (Kb =9.9 x10 4) is concerned.

Keywords
trans-Resveratrol, superoxide dismutase, docking, microcalorimetry, binding constant, free energy

Article Details

How to Cite
Dureja, J., Chadha, R., Karan, M., Jindal, A., & Chadha, K. (2019). Binding studies of trans-resveratrol with superoxide dismutase (SOD1): Docking assessment and Thermoanalysis. Journal of Pharmaceutical and Biopharmaceutical Research, 1(1), 21-27. https://doi.org/10.25082/JPBR.2019.01.003
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This work is licensed under a Creative Commons Attribution-NonCommercial 4.0 International License.

References

  1. Harikumar KB and Aggarwal BB. Resveratrol: a multitargeted agent for age-associated chronic diseases. Cell cycle, 2008, 7(8): 1020-1035. https://doi.org/10.4161/cc.7.8.5740
  2. Valenzano DR, Terzibasi E, Genade T, et al. Resveratrol prolongs lifespan and retards the onset of age-related markers in a short-lived vertebrate. Current Biology, 2006, 16(3): 296-300. https://doi.org/10.1016/j.cub.2005.12.038
  3. Baur JA, Pearson KJ, Price NL, et al. Resveratrol improves health and survival of mice on a high-calorie diet. Nature, 2006, 44(7117): 337. https://doi.org/10.1038/nature05354
  4. Berrougui H, Grenier G, Loued S, et al. A new insight into resveratrol as an atheroprotective compound: inhibition of lipid peroxidation and enhancement of cholesterol efflux. Atherosclerosis, 2009, 207(2): 420-427. https://doi.org/10.1016/j.atherosclerosis.2009.05.017
  5. Frankel EN, German JB, Kinsella JE, et al. Inhibition of oxidation of human low-density lipoprotein by phenolic substances in red wine. The Lancet, 1993, 341(8843): 454-457. https://doi.org/10.1016/0140-6736(93)90206-V
  6. Kaindl U, Eyberg I, Rohr-Udilova N, et al. The dietary antioxidants resveratrol and quercetin protect cells from exogenous pro-oxidative damage. Food and chemical toxicology, 2008, 46(4): 1320-1326. https://doi.org/10.1016/j.fct.2007.09.002
  7. Ndiaye M, Philippe C, Mukhtar H, et al. The grape antioxidant resveratrol for skin disorders: promise, prospects, and challenges. Archives of biochemistry and biophysics, 2011, 508(2): 164-170. https://doi.org/10.1016/j.abb.2010.12.030
  8. Udenigwe CC, Ramprasath VR, Aluko RE, et al. Potential of resveratrol in anticancer and anti-inflammatory therapy. Nutrition reviews, 2008, 66(8): 445-454. https://doi.org/10.1111/j.1753-4887.2008.00076.x
  9. Robb EL, Winkelmolen L, Visanji N, et al. Dietary resveratrol administration increases MnSOD expression and activity in mouse brain. Biochemical and biophysical research communications, 2008, 372(1): 254-259. https://doi.org/10.1016/j.bbrc.2008.05.028
  10. Flanagan SW, Anderson RD, Ross MA, et al. Overexpression of manganese superoxide dismutase attenuates neuronal death in human cells expressing mutant (G37R) Cu/Zn-superoxide dismutase. Journal of neurochemistry, 2002, 81(1): 170-177. https://doi.org/10.1046/j.1471-4159.2002.00812.x
  11. Alscher RG, Erturk N and Heath LS. Role of superoxide dismutases (SODs) in controlling oxidative stress in plants. Journal of experimental botany, 2002, 53(372): 1331-1341. https://doi.org/10.1093/jxb/53.372.1331
  12. Raychaudhuri SS and Deng XW. The role of superoxide dismutase in combating oxidative stress in higher plants. The Botanical Review, 2000, 66(1): 89-98. https://doi.org/10.1007/BF02857783
  13. Simm A, Nass N, Bartling B, et al. Potential biomarkers of ageing. Biological chemistry, 2008, 389(3): 257-265. https://doi.org/10.1515/BC.2008.034
  14. Krishna Sree V and Das S. Oxidative Stress and Antioxidant-The Link to Cancer Celebrating 60 years of excellence, 2014: 38.
  15. Richardson J, Thomas KA, Rubin BH, et al. Crystal structure of bovine Cu, Zn superoxide dismutase at 3 A resolution: chain tracing and metal ligands. Proceedings of the National Academy of Sciences, 1975, 72(4): 1349-1353. https://doi.org/10.1073/pnas.72.4.1349
  16. Forbes RB, Colville S and Swingler RJ. The epidemiology of amyotrophic lateral sclerosis (ALS/MND) in people aged 80 or over. Age and ageing, 2004, 33(2): 131-134. https://doi.org/10.1093/ageing/afh013
  17. Wright GSA, Antonyuk SV, Kershaw NM, et al. Ligand binding and aggregation of pathogenic SOD1. Nature communications, 2013, 4: 1758. https://doi.org/10.1038/ncomms2750
  18. Mitchell JD and Borasio GD. Amyotrophic lateral sclerosis. The Lancet, 2007, 369(9578): 2031-2041. https://doi.org/10.1016/S0140-6736(07)60944-1
  19. Traynor BJ, Codd MB, Corr B, et al. Clinical features of amyotrophic lateral sclerosis according to the El Escorial and Airlie House diagnostic criteria: A population-based study. Archives of neurology, 2000, 57(8): 1171-1176. https://doi.org/10.1001/archneur.57.8.1171
  20. Rosen DR, Siddique T, Patterson D, et al. Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Nature, 1993, 362(6415): 59. https://doi.org/10.1038/362059a0
  21. Logroscino G, Tortelli R, Rizzo G, et al. Amyotrophic lateral sclerosis: an aging-related disease. Current Geriatrics Reports, 2015, 4(2): 142-153. https://doi.org/10.1007/s13670-015-0127-8
  22. Ganesalingam J and Bowser R. The application of biomarkers in clinical trials for motor neuron disease. Biomarkers in medicine, 2010, 4(2): 281-297. https://doi.org/10.2217/bmm.09.71
  23. Ray SS, Nowak RJ, Brown RH, et al. Small-molecule-mediated stabilization of familial amyotrophic lateral sclerosis-linked superoxide dismutase mutants against unfolding and aggregation. Proceedings of the National Academy of Sciences, 2005, 102(10): 3639-3644. https://doi.org/10.1073/pnas.0408277102
  24. Nowak RJ, Cuny GD, Choi S, et al. Improving binding specificity of pharmacological chaperones that target mutant superoxide dismutase-1 linked to familial amyotrophic lateral sclerosis using computational methods. Journal of medicinal chemistry, 2010, 53(7): 2709-2718. https://doi.org/10.1021/jm901062p
  25. Kelly GS. A review of the sirtuin system, its clinical implications, and the potential role of dietary activators like resveratrol: part 2. Alternative medicine review, 2010, 15(3): 245-264.
  26. Feoktistov IA, Baldenkov GN, Barannik IV, et al. Interaction of calcium agonists and antagonists with Ca-binding proteins and their effect on cyclic nucleotide phosphodiesterase. Biokhimiia (Moscow, Russia), 1990, 55(4): 754-759.
  27. Gertz M, Nguyen GTT, Fischer F, et al. A molecular mechanism for direct sirtuin activation by resveratrol. PloS one, 2012, 7(11): e49761. https://doi.org/10.1371/journal.pone.0049761
  28. Agarwal B and Baur JA. Resveratrol and life extension. Annals of the New York Academy of Sciences, 2012, 1215(1): 138-143. https://doi.org/10.1111/j.1749-6632.2010.05850.x
  29. Leavitt S and Freire E. Direct measurement of protein binding energetics by isothermal titration calorimetry. Current opinion in structural biology, 2001, 11(5): 560-566. https://doi.org/10.1016/S0959-440X(00)00248-7
  30. Ghai R, Falconer RJ and Collins BM. Applications of isothermal titration calorimetry in pure and applied research-survey of the literature from 2010. Journal of Molecular Recognition, 2012, 25(1): 32-52. https://doi.org/10.1002/jmr.1167
  31. Nunez S, Venhorst J and Kruse CG. Target-drug interactions: first principles and their application to drug discovery. Drug discovery today, 2012, 17(1-2): 10-22. https://doi.org/10.1016/j.drudis.2011.06.013
  32. Release, Schrdinger. “2: Maestro, version 9.8; Schrdinger, LLC: New York, NY, USA, 2014. 36. Lew, JM; Kapopoulou, A.; Jones, LM; Cole, ST TubercuList10 years after” Tuberculosis (Edinb), 2011, 91: 17.
  33. Yamali C, Gul HI, Ece A, et al. Synthesis, molecular modeling, and biological evaluation of 4-
  34. -aryl-3-(thiophen-2-yl)-4,5-dihydro-1H-pyrazol-1-yl] benzenesulfonamides toward acetylcholinesterase, carbonic anhydrase I and II enzymes. Chemical biology and drug design, 2017, 91(4): 854-866. https://doi.org/10.1111/cbdd.13149
  35. Friesner RA, Murphy RB, Repasky MP, et al. Extra precision glide: Docking and scoring incorporating a model of hydrophobic enclosure for protein ligand complexes. Journal of medicinal chemistry, 2006, 49(21): 6177-6196. https://doi.org/10.1021/jm051256o
  36. Halgren TA, Murphy RB, Friesner RA, et al. Glide: a new approach for rapid, accurate docking and scoring. 2. Enrichment factors in database screening. Journal of medicinal chemistry, 2004, 47(7): 1750-1759. https://doi.org/10.1021/jm030644s
  37. Friesner RA, Banks JL, Murphy RB, et al. Glide: a new approach for rapid, accurate docking and scoring. 1. Method and assessment of docking accuracy. Journal of medicinal chemistry, 2004, 47(7): 1739-1749. https://doi.org/10.1021/jm0306430
  38. Ahmad E, Rabbani G, Zaidi N, et al. Stereo-selectivity of human serum albumin to enantiomeric and isoelectronic pollutants dissected by spectroscopy, calorimetry and bioinformatics. PloS one, 2011, 6(11): e26186. https://doi.org/10.1371/journal.pone.0026186
  39. Neelam S, Gokara M, Sudhamalla B, et al. Interaction studies of coumaroyltyramine with human serum albumin and its biological importance. The Journal of Physical Chemistry B,2010, 114(8): 3005-3012. https://doi.org/10.1021/jp910156k