239
Views
1
CrossRef citations to date
0
Altmetric
Research Articles

Biomolecular interaction mechanism of an anticancer drug, pazopanib with human serum albumin: a multi-spectroscopic and computational approach

, , , &
Pages 8312-8323 | Received 06 Aug 2020, Accepted 26 Mar 2021, Published online: 19 Apr 2021

References

  • Abou-Zied, O. K., & Al-Shihi, O. I. (2008). Characterization of subdomain IIA binding site of human serum albumin in its native, unfolded, and refolded states using small molecular probes. Journal of the American Chemical Society, 130(32), 10793–10801. https://doi.org/10.1021/ja8031289
  • Abraham, M. J., Murtola, T., Schulz, R., Pall, S., Smith, J. C., Hess, B., & Lindahl, E. (2015). GROMACS: High performance molecular simulations through multi-level parallelism from laptops to supercomputers. SoftwareX, 1–2, 19–25. https://doi.org/10.1016/j.softx.2015.06.001
  • Balaei, F., & Ghobadi, S. (2019). Hydrochlorothiazide binding to human serum albumin induces some compactness in the molecular structure of the protein: A multi-spectroscopic and computational study. Journal of Pharmaceutical and Biomedical Analysis, 162, 1–8. https://doi.org/10.1016/j.jpba.2018.09.009
  • Best, R. B., Zhu, X., Shim, J., Lopes, P. E., Mittal, J., Feig, M., & Mackerell, A. D. Jr. (2012). Optimization of the additive CHARMM all-atom protein force field targeting improved sampling of the backbone φ, ψ and side-chain χ(1) and χ(2) dihedral angles. Journal of Chemical Theory and Computation, 8(9), 3257–3273. https://doi.org/10.1021/ct300400x
  • Bi, S., Ding, L., Tian, Y., Song, D., Zhou, X., Liu, X., & Zhang, H. (2004). Investigation of the interaction between flavonoids and human serum albumin. Journal of Molecular Structure, 703(1–3), 37–45. https://doi.org/10.1016/j.molstruc.2004.05.026
  • Bozoğlan, B. K., Tunç, S., & Duman, O. (2014). Investigation of neohesperidin dihydrochalcone binding to human serum albumin by spectroscopic methods. Journal of Luminescence, 155, 198–204. https://doi.org/10.1016/j.jlumin.2014.06.032
  • Bussi, G., Donadio, D., & Parrinello, M. (2007). Canonical sampling through velocity rescaling. The Journal of Chemical Physics, 126(1), 014101–014107. https://doi.org/10.1063/1.2408420
  • Castaneda, C. A., & Gomez, H. L. (2009). Pazopanib: An antiangiogenic drug in perspective. Future Oncology (London, England), 5(9), 1335–1348. https://doi.org/10.2217/fon.09.112
  • Darden, T., York, D., & Pedersen, L. (1993). Particle mesh Ewald: An N log (N) method for Ewald sums in large systems. The Journal of Chemical Physics, 98(12), 10089–10092. https://doi.org/10.1063/1.464397
  • Durrant, J. D., & McCammon, J. A. (2011). Molecular dynamics simulations and drug discovery. BMC Biology, 9, 71–79. https://doi.org/10.1186/1741-7007-9-71
  • Feroz, S. R., Mohamad, S. B., Lee, G. S., Malek, S. N. A., & Tayyab, S. (2015). Supramolecular interaction of 6-shogaol, a therapeutic agent of Zingiber officinale with human serum albumin as elucidated by spectroscopic, calorimetric and molecular docking methods. Phytomedicine, 22(6), 621–630. https://doi.org/10.1016/j.phymed.2015.03.016
  • García, A. E. (1992). Large-amplitude nonlinear motions in proteins. Physical Review Letters, 68(17), 2696–2699. https://doi.org/10.1103/PhysRevLett.68.2696
  • Guercia, E., Forzato, C., Navarini, L., & Berti, F. (2016). Interaction of coffee compounds with serum albumins. Part II: Diterpenes. Food Chemistry, 199, 502–508. https://doi.org/10.1016/j.foodchem.2015.12.051
  • Guglielmelli, A., Rizzuti, B., & Guzzi, R. (2018). Stereoselective and domain-specific effects of ibuprofen on the thermal stability of human serum albumin. European Journal of Pharmaceutical Sciences, 112, 122–131. https://doi.org/10.1016/j.ejps.2017.11.013
  • Halgren, T. A. (1996). Merck molecular force field. I. Basis, form, scope, parameterization, and performance of MMFF94. Journal of Computational Chemistry, 17(5–6), 490–519. https://doi.org/10.1002/(SICI)1096-987X(199604)17:5/6<490::AID-JCC1>3.0.CO;2-P
  • Hamberg, P., Verweij, J., & Sleijfer, S. (2010). (Pre-)Clinical pharmacology and activity of pazopanib, a novel multikinase angiogenesis Inhibitor. The Oncologist, 15(6), 539–547. https://doi.org/10.1634/theoncologist.2009-0274
  • Hanwell, M. D., Curtis, D. E., Lonie, D. C., Vandermeersch, T., Zurek, E., & Hutchison, G. R. (2012). Avogadro: An advanced semantic chemical editor, visualization, and analysis platform. Journal of Cheminformatics, 4(1), 17. https://doi.org/10.1186/1758-2946-4-17
  • Harris, P. A., Boloor, A., Cheung, M., Kumar, R., Crosby, R. M., Davis-Ward, R. G., Epperly, A. H., Hinkle, K. W., Hunter, R. N., Johnson, J. H., Knick, V. B., Laudeman, C. P., Luttrell, D. K., Mook, R. A., Nolte, R. T., Rudolph, S. K., Szewczyk, J. R., Truesdale, A. T., Veal, J. M., Wang, L., & Stafford, J. A. (2008). Discovery of 5-[[4-[(2,3-dimethyl-2H-indazol-6-yl)methylamino]-2-pyrimidinyl]amino]-2-methyl-benzenesulfonamide (Pazopanib), a novel and potent vascular endothelial growth factor receptor inhibitor. Journal of Medicinal Chemistry, 51(15), 4632–4640. https://doi.org/10.1021/jm800566m
  • Hasanzadeh, A., Dehghan, G., Shaghaghi, M., Panahi, Y., Jouyban, A., & Yekta, R. (2017). Multi-spectral and molecular docking studies on the interaction of human serum albumin with iohexol. Journal of Molecular Liquids, 248, 459–467. https://doi.org/10.1016/j.molliq.2017.10.096
  • Jorgensen, W. L., Chandrasekhar, J., Madura, J. D., Impey, R. W., & Klein, M. L. (1983). Comparison of simple potential functions for simulating liquid water. The Journal of Chemical Physics, 79(2), 926–935. https://doi.org/10.1063/1.445869
  • Kabir, M. Z., Ghani, H., Mohamad, S. B., Alias, Z., & Tayyab, S. (2018). Interactive association between RhoA transcriptional signaling inhibitor, CCG1423 and human serum albumin: Biophysical and in silico studies. Journal of Biomolecular Structure & Dynamics, 36(10), 2495–2507. https://doi.org/10.1080/07391102.2017.1360207
  • Kabir, M. Z., Roslan, A. A., Ridzwan, N. F. W., Mohamad, S. B., & Tayyab, S. (2020). Biomolecular interaction of a platelet aggregation inhibitor, 3,4-methylenedioxy-β-nitrostyrene with human serum albumin: Multi-spectral and computational characterization. Journal of Biomolecular Structure & Dynamics, 38(9), 2693–2703. https://doi.org/10.1080/07391102.2019.1640133
  • Kabir, M. Z., Tee, W. V., Mohamad, S. B., Alias, Z., & Tayyab, S. (2016). Interaction of an anticancer drug, gefitinib with human serum albumin: Insights from fluorescence spectroscopy and computational modeling analysis. RSC Advances, 6(94), 91756–91767. https://doi.org/10.1039/C6RA12019A
  • Kandandapani, S., Ridzwan, N. F. W., Mohamad, S. B., & Tayyab, S. (2020). Exploring the interaction between tyrphostin 9 and human serum albumin using biophysical and computational methods. Journal of Biomolecular Structure & Dynamics, 38(14), 4134–4142. https://doi.org/10.1080/07391102.2019.1673210
  • Kragh-Hansen, U., Chuang, V. T. G., & Otagiri, M. (2002). Practical aspects of the ligand-binding and enzymatic properties of human serum albumin. Biological & Pharmaceutical Bulletin, 25(6), 695–704. https://doi.org/10.1248/bpb.25.695
  • Kumar, R., Knick, V. B., Rudolph, S. K., Johnson, J. H., Crosby, R. M., Crouthamel, M.-C., Hopper, T. M., Miller, C. G., Harrington, L. E., Onori, J. A., Mullin, R. J., Gilmer, T. M., Truesdale, A. T., Epperly, A. H., Boloor, A., Stafford, J. A., Luttrell, D. K., & Cheung, M. (2007). Pharmacokinetic-pharmacodynamic correlation from mouse to human with pazopanib, a multikinase angiogenesis inhibitor with potent antitumor and antiangiogenic activity. Molecular Cancer Therapeutics, 6(7), 2012–2021. https://doi.org/10.1158/1535-7163.mct-07-0193
  • Lakowicz, J. R. (2006). Principles of fluorescence spectroscopy (3rd ed.). Springer.
  • Lee, A. T. J., Jones, R. L., & Huang, P. H. (2019). Pazopanib in advanced soft tissue sarcomas. Signal Transduction and Targeted Therapy, 4, 16. https://doi.org/10.1038/s41392-019-0049-6
  • Li, Y., Chen, C., Zhang, C., Duan, J., Yao, H., & Wei, Q. (2017). Probing the binding interaction of AKR with human serum albumin by multiple fluorescence spectroscopy and molecular modeling. Journal of Biomolecular Structure & Dynamics, 35(6), 1189–1199. https://doi.org/10.1080/07391102.2016.1174622
  • Lin, J., Liu, Y., Chen, M., Huang, H., & Song, L. (2014). Investigation on the binding activities of citalopram with human and bovine serum albumins. Journal of Luminescence, 146, 114–122. https://doi.org/10.1016/j.jlumin.2013.09.054
  • Martínez, L. (2015). Automatic identification of mobile and rigid substructures in molecular dynamics simulations and fractional structural fluctuation analysis. PLoS One, 10(3), e0119264. https://doi.org/10.1371/journal.pone.0119264
  • Morris, G. M., Huey, R., Lindstrom, W., Sanner, M. F., Belew, R. K., Goodsell, D. S., & Olson, A. J. (2009). AutoDock4 and AutoDockTools4: Automated docking with selective receptor flexibility. Journal of Computational Chemistry, 30(16), 2785–2791. https://doi.org/10.1002/jcc.21256
  • Painter, L., Harding, M. M., & Beeby, P. J. (1998). Synthesis and interaction with human serum albumin of the first 3,18-disubstituted derivative of bilirubin. Journal of the Chemical Society, Perkin Transactions 1, 18(18), 3041–3044. https://doi.org/10.1039/a803429j
  • Parrinello, M., & Rahman, A. (1981). Polymorphic transitions in single crystals: A new molecular dynamics method. Journal of Applied Physics, 52(12), 7182–7190. https://doi.org/10.1063/1.328693
  • Peters, T. (1996). All about albumin: Biochemistry, genetics, and medical applications. Academic Press.
  • Pettersen, E. F., Goddard, T. D., Huang, C. C., Couch, G. S., Greenblatt, D. M., Meng, E. C., & Ferrin, T. E. (2004). UCSF Chimera-a visualization system for exploratory research and analysis. Journal of Computational Chemistry, 25(13), 1605–1612. https://doi.org/10.1002/jcc.20084
  • Ross, P. D., & Subramanian, S. (1981). Thermodynamics of protein association reactions: Forces contributing to stability. Biochemistry, 20(11), 3096–3102. https://doi.org/10.1021/bi00514a017
  • Saito, M. (1999). Molecular dynamics model structures for the molten globule state of alpha-lactalbumin: Aromatic residue clusters I and II. Protein Engineering, 12(12), 1097–1104. https://doi.org/10.1093/protein/12.12.1097
  • Singh, S. K., & Kishore, N. (2008). Calorimetric and spectroscopic studies on the interaction of methimazole with bovine serum albumin. Journal of Pharmaceutical Sciences, 97(6), 2362–2372. https://doi.org/10.1002/jps.21140
  • Subramani, A., & Floudas, C. A. (2012). Structure prediction of loops with fixed and flexible stems. The Journal of Physical Chemistry B, 116(23), 6670–6682. https://doi.org/10.1021/jp2113957
  • Sudlow, G., Birkett, D. J., & Wade, D. N. (1975). The characterization of two specific drug binding sites on human serum albumin. Molecular Pharmacology, 11(6), 824–832.
  • Tayyab, S., Francis, J. A., Kabir, M. Z., Ghani, H., & Mohamad, S. B. (2019). Probing the interaction of 2,4-dichlorophenoxyacetic acid with human serum albumin as studied by experimental and computational approaches. Spectrochimica Acta, Part A: Molecular and Biomolecular Spectroscopy, 207, 284–293. https://doi.org/10.1016/j.saa.2018.09.033
  • Todo, M. A. K. I., Shirotake, S., Nishimoto, K., Yasumizu, Y. O. T. A., Kaneko, G. O. U., Kondo, H., Okabe, T., Makabe, H., & Oyama, M. (2019). Usefulness of implementing comprehensive pharmaceutical care for metastatic renal cell carcinoma outpatients treated with pazopanib. Anticancer Research, 39(2), 999–1004. https://doi.org/10.21873/anticanres.13205
  • Tunç, S., Duman, O., Soylu, İ., & Bozoğlan, B. K. (2014). Study on the bindings of dichlorprop and diquat dibromide herbicides to human serum albumin by spectroscopic methods. Journal of Hazardous Materials, 273, 36–43. https://doi.org/10.1016/j.jhazmat.2014.03.022
  • Vennila, K. N., & Elango, K. P. (2018). Understanding the binding of quinoline amines with human serum albumin by spectroscopic and induced fit docking methods. Journal of Biomolecular Structure and Dynamics, 37(4), 1–37.
  • Verlet, L. (1967). Computer experiments on classical fluids. I. Thermodynamical properties of Lennard-Jones molecules. Physical Review, 159(1), 98–103. https://doi.org/10.1103/PhysRev.159.98
  • Ward, J. E., & Stadler, W. M. (2010). Pazopanib in renal cell carcinoma. Clinical Cancer Research, 16(24), 5923–5927. https://doi.org/10.1158/1078-0432.CCR-10-0728
  • Xiong, X., Gan, R., Suo, Z., Tang, P., Zhang, S., Zhu, Y., Sun, Q., & Li, H. (2018). Interactions between the antiviral drug telaprevir and human serum albumin: A combined study with spectroscopic methods and molecular modeling. New Journal of Chemistry, 42(12), 9791–9800. https://doi.org/10.1039/C8NJ00655E
  • Yan, X., Yuan, D., & Pan, D. (2018). Interactions of bromocarbazoles with human serum albumin using spectroscopic methods. Molecules, 23(12), 3120. https://doi.org/10.3390/molecules23123120
  • Yeggoni, D. P., Rachamallu, A., Kallubai, M., & Subramanyam, R. (2015). Cytotoxicity and comparative binding mechanism of piperine with human serum albumin and α-1-acid glycoprotein. Journal of Biomolecular Structure & Dynamics, 33(6), 1336–1351. https://doi.org/10.1080/07391102.2014.947326
  • Zoete, V., Cuendet, M. A., Grosdidier, A., & Michielin, O. (2011). SwissParam: A fast force field generation tool for small organic molecules. Journal of Computational Chemistry, 32(11), 2359–2368. https://doi.org/10.1002/jcc.21816

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.