Spectrophotometric and molecular modelling studies on in vitro interaction of tyrosine kinase inhibitor Linifanib with bovine serum albumin

PLoS ONE

Volumn 12, Issue 4, 2017, Pages

  Wani, Tanveer A ^a   Bakheit, Ahmed H ^a,b   Zargar, Seema ^c   Hamidaddin, Mohammed A ^a   Darwish, Ibrahim A ^a  

^a KING SAUD UNIVERSITY   (Saudi Arabia)

^b AL NEELAIN UNIVERSITY   (Sudan)

^c KING SAUD UNIVERSITY   (Saudi Arabia)

Author keywords

[No Author keywords available]

Indexed keywords

BOVINE SERUM ALBUMIN; LINIFANIB; CARBANILAMIDE DERIVATIVE; INDAZOLE DERIVATIVE; N-(4-(3-AMINO-1H-INDAZOL-4-YL)PHENYL)-N1-(2-FLUORO-5-METHYLPHENYL)UREA; PROTEIN BINDING; PROTEIN KINASE INHIBITOR; PROTEIN TYROSINE KINASE;

ARTICLE; BINDING AFFINITY; BINDING ENERGY; BINDING SITE; CHEMICAL INTERACTION; COMPLEX FORMATION; CONFORMATION; ENERGY; FLUORESCENCE; FLUORESCENCE SPECTROSCOPY; FORCE; HYDROGEN BOND; IN VITRO STUDY; MOLECULAR DOCKING; SPECTROPHOTOMETRY; SPECTROSCOPY; THERMODYNAMICS; ULTRAVIOLET VISIBLE SPECTROPHOTOMETRY; VAN DER WAALS FORCE; ANIMAL; ANTAGONISTS AND INHIBITORS; BOVINE; CHEMISTRY; METABOLISM; SPECTROFLUOROMETRY; ULTRAVIOLET SPECTROPHOTOMETRY;

ANIMALS; BINDING SITES; CATTLE; INDAZOLES; MOLECULAR DOCKING SIMULATION; PHENYLUREA COMPOUNDS; PROTEIN BINDING; PROTEIN KINASE INHIBITORS; PROTEIN-TYROSINE KINASES; SERUM ALBUMIN, BOVINE; SPECTROMETRY, FLUORESCENCE; SPECTROPHOTOMETRY, ULTRAVIOLET; THERMODYNAMICS;

EID: 85017604576     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0176015     Document Type: Article

References (43)

1. Sugio S, Kashima A, Mochizuki S, Noda M, Kobayashi K. Crystal structure of human serum albumin at 2.5 Å resolution. Protein Eng. 1999;12:439-46. PMID: 10388840
2. Flarakos J, Morand KL, Vouros P. High-throughput solution-based medicinal library screening against human serum albumin. Anal Chem. 2005;77:1345-53. https://doi.org/10.1021/ac048685z PMID: 15732917
3. Bakkialakshmi S, Chandrakala D. A spectroscopic investigations of anticancer drugs binding to bovine serum albumin. Spectrochim Acta A Mol Biomol Spectrosc. 2012;88:2-9. https://doi.org/10.1016/j.saa. 2011.10.076 PMID: 22226896
4. Dhar S, Rana DK, Pal A, Bhattacharya SC. Photobehavior and docking simulations of drug within macromolecules: Binding of an antioxidative isoquinolindione to a serine protease and albumin proteins. J Photochem Photobiol B. 2013;129:69-77. https://doi.org/10.1016/j.jphotobiol.2013.09.007 PMID: 24177206
5. Sun H, Wu Y, Xia X, Liu X, Shi Z. Interaction between diethylstilbestrol and bovine serum albumin. Monatshefte fü r Chemie-Chemical. 2013;144:739-46.
6. Shi J-H, Zhu Y-Y, Wang J, Chen J, Shen Y-J. Intermolecular interaction of prednisolone with bovine serum albumin: spectroscopic and molecular docking methods. Spectrochim Acta A Mol Biomol Spectrosc. 2013;103:287-94. https://doi.org/10.1016/j.saa.2012.11.034 PMID: 23261625
7. Meti MD, Gunagi SD, Nandibewoor ST, Chimatadar SA. Investigation of the interaction of the new antiarrhythmic drug procainamide hydrochloride with bovine serum albumin and the effect of some metal ions on the binding: a fluorescence quenching study. Monatshefte fü r Chemie-Chemical. 2013;144(8):1253-9.
8. Shahabadi N, Fili SM. Molecular modeling and multispectroscopic studies of the interaction of mesalamine with bovine serum albumin. Spectrochim Acta A Mol Biomol Spectrosc. 2014;118:422-9. https://doi.org/10.1016/j.saa.2013.08.110 PMID: 24076458
9. Shi J-H, Wang J, Zhu Y-Y, Chen J. Characterization of interaction between isoliquiritigenin and bovine serum albumin: Spectroscopic and molecular docking methods. J Lumin. 2014;145:643-50.
10. Chamani J, Moosavi-Movahedi A. Effect of n-alkyl trimethylammonium bromides on folding and stability of alkaline and acid-denatured cytochrome c: A spectroscopic approach. J Colloid Interface Sci. 2006;297:561-9. https://doi.org/10.1016/j.jcis.2005.11.035 PMID: 16338232
11. Moosavi-Movahedi A, Gharanfoli M, Nazari K, Shamsipur M, Chamani J, Hemmateenejad B, et al. A distinct intermediate of RNase A is induced by sodium dodecyl sulfate at its pK a. Colloids Surf B Biointerfaces. 2005;43:150-7. https://doi.org/10.1016/j.colsurfb.2005.04.008 PMID: 15949923
12. Sharif-Barfeh Z, Beigoli S, Marouzi S, Rad AS, Asoodeh A, Chamani J. Multi-spectroscopic and HPLC Studies of the Interaction Between Estradiol and Cyclophosphamide With Human Serum Albumin: Binary and Ternary Systems. J Solution Chem. 2017;46:488-504.
13. Chamani J, Vahedian-Movahed H, Saberi MR. Lomefloxacin promotes the interaction between human serum albumin and transferrin: A mechanistic insight into the emergence of antibiotic's side effects. J Pharm Biomed Anal. 2011;55:114-24. https://doi.org/10.1016/j.jpba.2010.12.029 PMID: 21273024
14. Sattar Z, Saberi MR, Chamani J. Determination of LMF binding site on a HSA-PPIX complex in the presence of human holo transferrin from the viewpoint of drug loading on proteins. PloS one. 2014;9:e84045. https://doi.org/10.1371/journal.pone.0084045 PMID: 24392106
15. He XM, Carter DC. Atomic structure and chemistry of human serum albumin. Nature 1992;358:209-215. https://doi.org/10.1038/358209a0 PMID: 1630489
16. Moghaddam MM, Pirouzi M, Saberi MR, Chamani J. Comparison of the binding behavior of FCCP with HSA and HTF as determined by spectroscopic and molecular modeling techniques. Luminescence 2014;29:314-31. https://doi.org/10.1002/bio.2546 PMID: 23832656
17. Zolfagharzadeh M, Pirouzi M, Asoodeh A, Saberi MR, Chamani J. A comparison investigation of DNPbinding effects to HSA and HTF by spectroscopic and molecular modeling techniques. J Biomol Struct Dyn. 2014;32:1936-52. https://doi.org/10.1080/07391102.2013.843062 PMID: 24125112
18. Bergers G, Song S, Meyer-Morse N, Bergsland E, Hanahan D. Benefits of targeting both pericytes and endothelial cells in the tumor vasculature with kinase inhibitors. J Clin Invest. 2003;111:1287-95. https://doi.org/10.1172/JCI17929 PMID: 12727920
19. Erber R, Thurnher A, Katsen AD, Groth G, Kerger H, Hammes HP, Menger MD, Ullrich A, Vajkoczy P: Combined inhibition of VEGF and PDGF signaling enforces tumor vessel regression by interfering with pericyte-mediated endothelial cell survival mechanisms. FASEB J. 2004;18:338-340. https://doi.org/10.1096/fj.03-0271fje PMID: 14657001
20. Dai Y, Hartandi K, Ji Z, Ahmed AA, Albert DH, Bauch JL, Bouska JJ, Bousquet PF, Cunha GA, Glaser KB et al: Discovery of N-(4-(3-amino-1H-indazol-4-yl) phenyl)-N'-(2-fluoro-5-methylphenyl) urea (ABT-869), a 3-aminoindazole-based orally active multitargeted receptor tyrosine kinase inhibitor. J Med Chem. 2007;50:1584-1597. https://doi.org/10.1021/jm061280h PMID: 17343372
21. Albert DH, Tapang P, Magoc TJ, Pease LJ, Reuter DR, Wei RQ, Li J, Guo J, Bousquet PF, Ghoreishi-Haack NS et al: Preclinical activity of ABT-869, a multitargeted receptor tyrosine kinase inhibitor. Mol Cancer Ther. 2006, 5:995-1006. https://doi.org/10.1158/1535-7163. MCT-05-0410 PMID: 16648571
22. Guo J, Marcotte PA, McCall JO, Dai Y, Pease LJ, Michaelides MR, Davidsen SK, Glaser KB: Inhibition of phosphorylation of the colony-stimulating factor-1 receptor (c-Fms) tyrosine kinase in transfected cells by ABT-869 and other tyrosine kinase inhibitors. Mol Cancer Ther. 2006;5:1007-1013. https://doi.org/10.1158/1535-7163. MCT-05-0359 PMID: 16648572
23. Aversa C, Leone F, Zucchini G, Serini G, Geuna E, Milani A, et al. Linifanib: current status and future potential in cancer therapy. Expert Rev Anticancer Ther. 2015;15:677-87. https://doi.org/10.1586/14737140.2015.1042369 PMID: 25936222
24. Toh HC, Chen PJ, Carr BI, Knox JJ, Gill S, Ansell P, et al. Phase 2 trial of linifanib (ABT-869) in patients with unresectable or metastatic hepatocellular carcinoma. Cancer. 2013;119:380-7. https://doi.org/10. 1002/cncr.27758 PMID: 22833179
25. Tannir NM, Wong YN, Kollmannsberger CK, Ernstoff MS, Perry DJ, Appleman LJ, Posadas EM, Cho D, Choueiri TK, Coates A et al: Phase 2 trial of LNF (ABT-869) in patients with advanced renal cell cancer after sunitinib failure. Eur J Cancer. 2011;47:2706-2714. https://doi.org/10.1016/j.ejca.2011.09.002 PMID: 22078932
26. Chiu YL, Carlson DM, Pradhan RS, Ricker JL: Exposure-Response (Safety) Analysis to Identify LNF Dose for a Phase III Study in Patients With Hepatocellular Carcinoma. Clin Ther. 2013;35:1770-1777. https://doi.org/10.1016/j.clinthera.2013.09.002 PMID: 24094464
27. Wong CI, Koh TS, Soo R, Hartono S, Thng CH, McKeegan E, Yong WP, Chen CS, Lee SC, Wong J et al: Phase I and biomarker study of ABT-869, a multiple receptor tyrosine kinase inhibitor, in patients with refractory solid malignancies. J Clin Oncol. 2009;27:4718-4726. https://doi.org/10.1200/JCO. 2008.21.7125 PMID: 19720910
28. Iqbal M, Ezzeldin E, Wani TA, Khalil NY. Simple, sensitive and rapid determination of linifanib (ABT-869), a novel tyrosine kinase inhibitor in rat plasma by UHPLC-MS/MS. Chem Cent J. 2014;8:13. https://doi.org/10.1186/1752-153X-8-13 PMID: 24533632
29. Khorsand Ahmadi S, Mahmoodian Moghadam M, Mokaberi P, Reza Saberi M, Chamani J. A comparison study of the interaction between β-lactoglobulin and retinol at two different conditions: spectroscopic and molecular modeling approaches. J Biomol Struct Dyn. 2015;33(9):1880-98 https://doi.org/10.1080/07391102.2014.977351 PMID: 25402748
30. Marouzi S, Rad AS, Beigoli S, Baghaee PT, Darban RA, Chamani J. Study on effect of lomefloxacin on human holo-transferrin in the presence of essential and nonessential amino acids: Spectroscopic and molecular modeling approaches. Int J Biol Macromol. 2017;97:688-99. https://doi.org/10.1016/j. ijbiomac.2017.01.047 PMID: 28115228
31. Chamani J, Heshmati M. Mechanism for stabilization of the molten globule state of papain by sodium nalkyl sulfates: spectroscopic and calorimetric approaches. J Colloid Interface Sci. 2008;322:119-27. https://doi.org/10.1016/j.jcis.2008.03.001 PMID: 18405913
32. Mendonça A, Rocha AC, Duarte AC, Santos EB. The inner filter effects and their correction in fluorescence spectra of salt marsh humic matter. Anal Chim Acta. 2013;788:99-107. https://doi.org/10.1016/j. aca.2013.05.051 PMID: 23845487
33. Moriyama Y, Ohta D, Hachiya K, Mitsui Y, Takeda K. Fluorescence behavior of tryptophan residues of bovine and human serum albumins in ionic surfactant solutions: a comparative study of the two and one tryptophan (s) of bovine and human albumins. J Protein Chem. 1996;15:265-72. PMID: 8804574
34. Lackowicz J. Principle of Fluorescence Spectroscopy, 2006. Springer Science and Business Media, LLC, New York ISBN. 13:978-0.
35. Lakowicz JR, Weber G. Quenching of fluorescence by oxygen. Probe for structural fluctuations in macromolecules. Biochemistry. 1973;12:4161-70. PMID: 4795686
36. Hu Y-J, Liu Y, Wang J-B, Xiao X-H, Qu S-S. Study of the interaction between monoammonium glycyrrhizinate and bovine serum albumin. J Pharm Biomed Anal. 2004;36:915-9. https://doi.org/10.1016/j. jpba.2004.08.021 PMID: 15533690
37. Sudlow G, Birkett D, Wade D. Further characterization of specific drug binding sites on human serum albumin. Mol Pharmacol. 1976;12:1052-61. PMID: 1004490
38. Ni Y, Liu G, Kokot S. Fluorescence spectrometric study on the interactions of Isoprocarb and sodium 2-isopropylphenate with bovine serum albumin. Talanta. 2008;76:513-21. https://doi.org/10.1016/j. talanta.2008.03.037 PMID: 18585315
39. Ross PD, Subramanian S. Thermodynamics of protein association reactions: forces contributing to stability. Biochemistry. 1981;20:3096-102. PMID: 7248271
40. Cui F-L, Fan J, Li J-P, Hu Z-D. Interactions between 1-benzoyl-4-p-chlorophenyl thiosemicarbazide and serum albumin: investigation by fluorescence spectroscopy. Bioorg Med Chem. 2004;12:151-7. PMID: 14697780
41. Albert DH, Tapang P, Magoc TJ, Pease LJ, Reuter DR, Wei R-Q, et al. Preclinical activity of ABT-869, a multitargeted receptor tyrosine kinase inhibitor. Mol Cancer Ther. 2006;5:995-1006. https://doi.org/10. 1158/1535-7163. MCT-05-0410 PMID: 16648571
42. Clapp AR, Medintz IL, Mauro JM, Fisher BR, Bawendi MG, Mattoussi H. Fluorescence resonance energy transfer between quantum dot donors and dye-labeled protein acceptors. J Am Chem Soc. 2004;126:301-10. https://doi.org/10.1021/ja037088b PMID: 14709096
43. Gordon GW, Berry G, Liang XH, Levine B, Herman B. Quantitative fluorescence resonance energy transfer measurements using fluorescence microscopy. Biophysical journal. 1998;74(5):2702-13. https://doi.org/10.1016/S0006-3495 (98) 77976-7 PMID: 9591694