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(E)-2-Benzylidenecyclanones: Part XVI.† Study on the interaction of some (E)-2-benzylidenebenzosuberone derivatives with serum albumin by UV-Vis method, inhibitory effect on topoisomerase

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UV-Vis absorption spectra of HSA
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Submitted   Jul 13, 2020
Published   Aug 14, 2020
Issue    Vol 2 No 1 (2020)
DOI   10.25082/JPBR.2020.01.003

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Zsuzsanna Rozmer corresponding author
Department of Pharmaceutical Chemistry, University of Pécs, Rókus Str. 2, Pécs 7624, Hungary
Pál Perjési
Department of Pharmaceutical Chemistry, University of Pécs, Rókus Str. 2, Pécs 7624, Hungary

Abstract

Interaction of some cyclic chalcone analogs, (E)-2-(4-X-benzylidene)-1-benzosuberone derivatives with bovine serum albumin (BSA) and human serum albumin (HSA) has been investigated using UV-Vis spectroscopic methods. Recording the UV-Vis spectra of compounds in the presence of BSA or HSA indicated interaction of the molecules with the hydrophobic binding site(s) of the proteins. Investigated analogs have shown remarkable topo I and topo II inhibitory activity compared to camptothecin and etoposide, respectively, at 40 μM concentration. The observed interactions between the cyclic chalcone analogs and the cellular macromolecules might play a role in the previously detected cytotoxicity against several tumor cell lines.

Keywords
cyclic chalcone analogs, enones, bovine serum albumin, human serum albumin, UV-Vis spectroscopy, DNA topoisomerases I and II

Article Details

How to Cite
Rozmer, Z., & Perjési, P. (2020). (E)-2-Benzylidenecyclanones: Part XVI.† Study on the interaction of some (E)-2-benzylidenebenzosuberone derivatives with serum albumin by UV-Vis method, inhibitory effect on topoisomerase. Journal of Pharmaceutical and Biopharmaceutical Research, 2(1), 118-125. https://doi.org/10.25082/JPBR.2020.01.003
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References

  1. Rozmer Zs and Perj´esi P. Naturally occuring chalcones and their biological activities. Phytochemistry Reviews, 2016, 15: 87-120. https://doi.org/10.1007/s11101-014-9387-8
  2. Dimmock JR, Elias DW, Beazely MA, et al. Bioactivities of chalcones. Current Medicinal Chemistry, 1999, 6: 1125- 1149.
  3. Ni L, Meng CQ and Sikorski JA. Recent advances in therapeutic compounds. Expert Opinion on Therapeutic Patents, 2004, 14(12): 1669-1691. https://doi.org/10.1517/13543776.14.12.1669
  4. Go ML, Wu X and Liu XL. Chalcones: an update on cytotoxic and chemoprotective properties. Current Medicinal Chemistry, 2005, 12(4): 483-499. https://doi.org/10.2174/0929867053363153
  5. Nowakowska Z. A review of anti-infective and antiinflammatory chalcones. European Journal of Medicinal Chemistry, 2007, 42(2): 125-137. https://doi.org/10.1016/j.ejmech.2006.09.019
  6. Mahapatra DK, Bharti SK and Asati V. Anti-cancer chalcones: Structural and molecular target perspectives. European Journal of Medicinal Chemistry, 2015, 98: 69-114. https://doi.org/10.1016/j.ejmech.2015.05.004
  7. Mahapatra DK, Bharti SK and Asati V. Chalcone scaffolds as anti-infective agents: Structural and molecular target perspectives. European Journal of Medicinal Chemistry, 2015, 101: 496-524. https://doi.org/10.1016/j.ejmech.2015.06.052
  8. Dimmock JR, Kandepu NM, Nazarali AJ, et al. Conformational and quantitative structure-activity relationship study of cytotoxic 2-arylidenebenzocyclanones. Journal of Medicinal Chemistry, 1999, 42(8): 1358-1366. https://doi.org/10.1021/jm9806695
  9. Perj´esi P, Nusser T, Tarczay Gy, et al. E-2-benzylidenebenzocycloalkanones. Stereostructure and NMR spectroscopic investigation. Journal of Molecular Structure, 1999, 479: 13- 19. https://doi.org/10.1016/S0022-2860(98)00805-9
  10. Tarczay Gy, V´ekey K, Lud´anyi K, et al. E-2-benzylidenebenzocyclanones. II. IR and mass spectrometric investigations. Journal of Molecular Structure, 2000, 520: 97-102. https://doi.org/10.1016/S0022-2860(99)00330-0
  11. Perj´esi P, Perj´essy A, Kolehmainen E, et al. E-2-benzylidenebenzocycloalkanones III. Studies on transmission of substituent effect on IR carbonyl stretching frequencies and 13C NMR chemical shifts of E-2-(Xbenzylidene)- 1-indanones. Comparison with the IR date of E-2-(X-benzylidene)-1-indanones, -tetralones, and - benzosuberones. Journal of Molecular Structure, 2004, 697: 41-47. https://doi.org/10.1016/j.molstruc.2004.02.006
  12. Perj´esi P, Linnato J, Kolehmainen E, et al. E-2-Benzylidenebenzocycloalkanones. IV. Studies on transmission of substituent effects on 13C NMR chemical shifts of E-2- (X-benzylidene)-1-tetralones, and -benzosuberones. Comparison with the 13C NMR data of chalcones and E-2-(Xbenzylidene)- 1-indanones. Journal of Molecular Structure, 2005, 740: 81-89. https://doi.org/10.1016/j.molstruc.2004.10.013
  13. Dimmock JR, Zello GA, Oloo EO, et al. Correlations between cytotoxicity and topography of some 2- arylidenebenzocycloalkanones determined by X-ray crystallography. Journal of Medicinal Chemistry, 2002, 45: 3103- 3111. https://doi.org/10.1021/jm010559p
  14. Rozmer Zs, Berki T and Perj´esi P. Different effects of two cyclic chalcone analogues on cell cycle of Jurkat T cells. Toxicology in Vitro, 2006, 20: 1354-1362. https://doi.org/10.1016/j.tiv.2014.06.006
  15. Pilatova M, Varinska L, Perj´esi P, et al.In vitro antiproliferative and antiangiogenic effects of synthetic chalcone analogues. Toxicology in Vitro, 2010, 24(5): 1347-1355. https://doi.org/10.1016/j.tiv.2010.04.013
  16. Tomeckova V, Perj´esi P, Guzy J, et al. Comparison of effect of selected synthetic chalcone analogues on mitochondrial outer membrane determined by fluorescence spectroscopy. Journal of Biochemical and Biophysical Methods, 2004, 61: 135-141. https://doi.org/10.1016/j.jbbm.2004.04.010
  17. Tomeckova V, Stefanisinova M, Velika B, et al. investigation of interaction of some chalcones and cyclic chalcone analogues with outer mitochondrial membrane by UV-Vis and fluorescence spectroscopy. Spectral Analysis Review, 2013, 1: 1-9. https://doi.org/10.4236/sar.2013.11001
  18. Perj´esi P, Das U, De Clercq ED, et al. Design, synthesis and antiproliferative activity of some 3-benzylidene-2,3- dihydro-1-benzopyran-4-ones which display selective toxicity for malignant cells. European Journal of Medicinal Chemistry, 2008, 43: 839-845. https://doi.org/10.1016/j.ejmech.2007.06.017
  19. Perj´esi P, Kubalkova J, Chovanova Z, et al. Comparison of effects of some cyclic chalcone analogues on selected mitochondrial functions. Pharmazie, 2008, 63: 899-903. https://doi.org/10.1691/ph.2008.8629
  20. Rozmer Zs, Marton E and Perj´esi P. (E)-2-Benzylidenecyclanones: part XIV. Study on interaction of some (E)- 2-benzylidenebenzosuberone derivatives with calf thymus DNA by TLC and UV-Vis methods, a DNA cleavage study. Medicinal Chemistry Research, 2017, 26: 2172-2179. https://doi.org/10.1007/s00044-017-1924-8
  21. Jiang YL. Design, synthesis and spectroscopic studies of resveratrol aliphatic ligands of human serum albumin. Bioorganic Medicinal Chemistry, 2008, 16(12): 6406-6414. https://doi.org/10.1016/j.bmc.2008.05.002
  22. Da Silva JG, Despaigne AAR, Louro SRW, et al. Cytotoxic activity, albumin and DNA binding of new copper(II) complexes with chalcone-derived thiosemicarbazones. European Journal of Medicinal Chemistry, 2013, 65: 415-426. https://doi.org/10.1016/j.ejmech.2013.04.036
  23. Zhang X, Song Q, Cao Z, et al.Study on the binding of chloramphenicol with bovine serum albumin by fluorescence and UV-Vis spectroscopy. Spectrochimica Acta A, 2013, 105: 74-79. https://doi.org/10.1016/j.saa.2012.11.064
  24. Carter DC and Ho JX. Structure of serum albumin. Advances in Protein Chemistry, 1994, 45: 153-203. https://doi.org/10.1016/s0065-3233(08)60640-3
  25. Yin BT, Yan CY, Peng XM, et al.Synthesis and biological evaluation of -triazolyl chalcones as a new type of potential antimicrobial agents and their interaction with calf thymus DNA and human serum albumin. European Journal of Medicinal Chemistry, 2014, 71: 148-159. https://doi.org/10.1016/j.ejmech.2013.11.003
  26. Naik KM and Nandibewoor ST. Spectroscopic studies on the interaction between chalcone and bovine serum albumin. Journal of Luminescence, 2013, 143: 484-491. https://doi.org/10.1016/j.jlumin.2013.05.013
  27. Champoux JJ. DNA topoisomerases: structure, function and mechanism. Annual Review of Biochemistry, 2001, 70: 369- 413. https://doi.org/10.1146/annurev.biochem.70.1.369
  28. Heck MM and Ernshaw WC. Topoisomerase II: a specific marker for cell proliferation. Journal of Cell Biology, 1986, 103: 2569-2581. https://doi.org/10.1083/jcb.103.6.2569
  29. Larsen AK, Escargueil AE and Skladanowski A. Catalytic topoisomerase II inhibitors in cancer therapy. Pharmacology Therapeutics, 2003, 99: 167-181. https://doi.org/10.1016/S0163-7258(03)00058-5
  30. Hande KR. Topoisomerase II inhibitors. Update in Cancer Therapeutics, 2008, 3: 13-26. https://doi.org/10.1016/j.uct.2008.02.001
  31. Hevener KE, Verstak TA, Lutat KE, et al. Recent developments in topoisomerase-targeted cancer chemotherapy. Acta Pharmaceutica Sinica B, 2018, 8: 844-861. https://doi.org/10.1016/j.apsb.2018.07.008
  32. Stefanisinova M, Tomeckova V, Kozurkova M, et al. Study of DNA interactions with cyclic chalcone derivatives by spectroscopic techniques. Spectrochimica Acta A, 2011, 81: 666-671. https://doi.org/10.1016/j.saa.2011.06.071
  33. Velika B, Tomeckova V, Fodor K, et al. (E)-Benzyli- denecycloalkanones XII. Kinetic measurement of bovine and human serum albumin interaction with selected chalcones and their cyclic chalcone analogues by UV spectrophotometry. Spectral Analysis Review, 2015, 3: 1-8. https://doi.org/10.4236/sar.2015.31001
  34. Fodor K, Tomescova V, K˝oszegi T, et al. (E)-2-Benzylidenecyclanones: Part VI. Solvent effect on the UV and fluorescence properties of some chalcones and their cyclic analogues. Interaction of 4-dimethylaminochalcones with bovine and human serum albumin: a UV–Vis study. Monatshefte f¨ur Chemie, 2011, 142: 463-468. https://doi.org/10.1007/s00706-011-0463-0
  35. Perj´esi P. (E)-2-Benzylidenebenzocyclanones: part XIII. Light-induced in solution (E)/(Z) isomerization of some cyclic chalcone analogues. Effect of ring size on lipophilicity of geometric isomers. Monatshefte f¨ur Chemie, 2015, 146: 1275-1281. https://doi.org/10.1007/s00706-015-1463-2
  36. Fukuda M, Nishio K, Kanzawa F, et al.Synergism between cisplatin and topoisomerase I inhibitors, NB-506 and SN- 38, in human small cell lung cancer cells. Cancer Research, 1996, 56: 789-793.
  37. Jun KY, KwonH, Park SE, et al. Discovery of dihydroxylated 2,4-diphenyl-6-thiophen-2-yl-pyridine as a nonintercalative DNA-binding topoisomerase II-specific catalytic inhibitor. European Journal of Medicinal Chemistry, 2014, 80: 428-438. https://doi.org/10.1016/j.ejmech.2014.04.066
  38. Kang DH, Kim JS, Jung MJ, et al.New insight for fluoroquinophenoxazine derivatives as possibly new potent topoisomerase I inhibitor. Bioorganic Medicinal Chemistry Letters, 2008, 18: 1520-1524. https://doi.org/10.1016/j.bmcl.2007.12.053
  39. Ma J, Fan Y, Si Q, et al.Interactions of three chalcones with human serum albumin revealed by spectroscopic techniques. Analytical Sciences, 2017, 33: 493-498. https://doi.org/10.2116/analsci.33.493
  40. Mabry TJ, Markham KR and Thomas MB. The Ultraviolet spectra of flavones and flavonols. In: The systematic identification of flavonoids. Springer, Berlin, Heidelberg, 1970. https://doi.org/10.1007/978-3-642-88458-0_5
  41. He XM and Carter DC. Atomic structure and chemistry of human serum albumin. Nature, 1992, 358: 209-215. https://doi.org/10.1038/358209a0
  42. Sudlow G, Birkett DJ and Wade DN. The characterization of two specific drug binding sites on human serum albumin. Molecular Pharmacology, 1975, 11(6): 824-832.
  43. Moriyama Y and Takeda K. Re-formation of the helical structure of human serum albumin by the addition of small amounts of sodium dodecyl sulfate after the disruption of the structure by urea. A comparison with bovine serum albumin. Lamgmuir, 1999, 15: 2003-2008. https://doi.org/10.1021/la981442f
  44. Moriyama Y, Sato Y and Takeda K. Reformation of the helical structure of bovine serum albumin by the addition of small amounts of sodium dodecyl sulfate after the disruption of the structure by urea. Journal of Colloid Interface Sciences, 1993, 156: 420-424. https://doi.org/10.1006/jcis.1993.1132
  45. Trnkova L, Bousova I, Kubicek V, et al. Binding of naturally occuring hydroxycinnamic acids to bovine serum albumin. Natural Science, 2010, 2: 563-670. https://doi.org/10.4236/ns.2010.26071
  46. Chen X, Qian K and Chen Q. Comparison between loureirin A and cochinchinenin C on the interaction with human serum albumin. European Journal of Medicinal Chemistry, 2015, 93: 492-500. https://doi.org/10.1016/j.ejmech.2015.02.025
  47. Cho HJ, Jung MJ, Woo S, et al.New benzoxanthone derivatives as topoisomerase inhibitors and DNA cross-linkers. Bioorganic Medicinal Chemistry, 2010, 18: 1010-1017. https://doi.org/10.1016/j.bmc.2009.12.069
  48. Woessner RD, Mattern MR, Mirabelli CJ, et al. Proliferation- and cell cycle-dependent differences in expression of the 170 kilodalton and 180 kilodalton forms of topoisomerase II in NIH-3T3 cells. Cell Growth Differentation, 1992, 2: 209-214.