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Volumn 171, Issue , 2017, Pages 174-182

Fluorescence spectroscopic and molecular docking studies of the binding interaction between the new anaplastic lymphoma kinase inhibitor crizotinib and bovine serum albumin

Author keywords

Bovine serum albumin; Crizotinib; Fluorescence spectroscopy; Molecular docking

Indexed keywords

BINDING ENERGY; BINS; FLUORESCENCE; FLUORESCENCE SPECTROSCOPY; MAMMALS; MOLECULAR MODELING; SURFACE PLASMON RESONANCE;

EID: 84981484197     PISSN: 13861425     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.saa.2016.08.005     Document Type: Article
Times cited : (80)

References (47)
  • 2
    • 84876985187 scopus 로고    scopus 로고
    • Clinical use of crizotinib for the treatment of non-small cell lung cancer
    • [2] Roberts, P.J., Clinical use of crizotinib for the treatment of non-small cell lung cancer. Biologics Targets Ther. 7 (2013), 91–101.
    • (2013) Biologics Targets Ther. , vol.7 , pp. 91-101
    • Roberts, P.J.1
  • 3
    • 84859124139 scopus 로고    scopus 로고
    • Crizotinib: a novel and first-in-class multitargeted tyrosine kinase inhibitor for the treatment of anaplastic lymphoma kinase rearranged non-small cell lung cancer and beyond
    • [3] Ou, S., Crizotinib: a novel and first-in-class multitargeted tyrosine kinase inhibitor for the treatment of anaplastic lymphoma kinase rearranged non-small cell lung cancer and beyond. Drug Des. Dev. Ther. 5 (2011), 471–485.
    • (2011) Drug Des. Dev. Ther. , vol.5 , pp. 471-485
    • Ou, S.1
  • 4
    • 79952767398 scopus 로고    scopus 로고
    • Crizotinib, a small-molecule dual inhibitor of the c-Met and ALK receptor tyrosine kinases
    • [4] Rodig, S.J., Shapiro, G.I., Crizotinib, a small-molecule dual inhibitor of the c-Met and ALK receptor tyrosine kinases. Curr. Opin. Investig. Drugs (Lond. Engl. 11:2010 (2000), 1477–1490.
    • (2000) Curr. Opin. Investig. Drugs (Lond. Engl. , vol.11 , Issue.2010 , pp. 1477-1490
    • Rodig, S.J.1    Shapiro, G.I.2
  • 6
    • 80052806086 scopus 로고    scopus 로고
    • Structure based drug design of crizotinib (PF-02341066), a potent and selective dual inhibitor of mesenchymal–epithelial transition factor (c-MET) kinase and anaplastic lymphoma kinase (ALK)
    • [6] Cui, J.J., Tran-Dubé, M., Shen, H., Nambu, M., Kung, P.-P., Pairish, M., Jia, L., Meng, J., Funk, L., Botrous, I., Structure based drug design of crizotinib (PF-02341066), a potent and selective dual inhibitor of mesenchymal–epithelial transition factor (c-MET) kinase and anaplastic lymphoma kinase (ALK). J. Med. Chem. 54 (2011), 6342–6363.
    • (2011) J. Med. Chem. , vol.54 , pp. 6342-6363
    • Cui, J.J.1    Tran-Dubé, M.2    Shen, H.3    Nambu, M.4    Kung, P.-P.5    Pairish, M.6    Jia, L.7    Meng, J.8    Funk, L.9    Botrous, I.10
  • 7
    • 56949084877 scopus 로고    scopus 로고
    • Albumin as a drug carrier: design of prodrugs, drug conjugates and nanoparticles
    • [7] Kratz, F., Albumin as a drug carrier: design of prodrugs, drug conjugates and nanoparticles. J. Control. Release 132 (2008), 171–183.
    • (2008) J. Control. Release , vol.132 , pp. 171-183
    • Kratz, F.1
  • 8
    • 84929326649 scopus 로고    scopus 로고
    • Binding interaction of sorafenib with bovine serum albumin: spectroscopic methodologies and molecular docking
    • [8] Shi, J.-H., Chen, J., Wang, J., Zhu, Y.-Y., Wang, Q., Binding interaction of sorafenib with bovine serum albumin: spectroscopic methodologies and molecular docking. Spectrochim. Acta A Mol. Biomol. Spectrosc. 149 (2015), 630–637.
    • (2015) Spectrochim. Acta A Mol. Biomol. Spectrosc. , vol.149 , pp. 630-637
    • Shi, J.-H.1    Chen, J.2    Wang, J.3    Zhu, Y.-Y.4    Wang, Q.5
  • 9
    • 19444375863 scopus 로고    scopus 로고
    • Interaction of wogonin with bovine serum albumin
    • [9] Tian, J., Liu, J., Hu, Z., Chen, X., Interaction of wogonin with bovine serum albumin. Bioorg. Med. Chem. 13 (2005), 4124–4129.
    • (2005) Bioorg. Med. Chem. , vol.13 , pp. 4124-4129
    • Tian, J.1    Liu, J.2    Hu, Z.3    Chen, X.4
  • 10
    • 84859598351 scopus 로고    scopus 로고
    • Optical spectroscopic exploration of binding of cochineal red a with two homologous serum albumins
    • [10] Bolel, P., Mahapatra, N., Halder, M., Optical spectroscopic exploration of binding of cochineal red a with two homologous serum albumins. J. Agric. Food Chem. 60 (2012), 3727–3734.
    • (2012) J. Agric. Food Chem. , vol.60 , pp. 3727-3734
    • Bolel, P.1    Mahapatra, N.2    Halder, M.3
  • 11
    • 0028227096 scopus 로고
    • Structure of serum albumin
    • [11] Carter, D.C., Ho, J.X., Structure of serum albumin. Adv. Protein Chem. 45 (1994), 153–203.
    • (1994) Adv. Protein Chem. , vol.45 , pp. 153-203
    • Carter, D.C.1    Ho, J.X.2
  • 12
    • 84862791320 scopus 로고    scopus 로고
    • Spectroscopic, structural and thermodynamic properties of chlorpyrifos bound to serum albumin: a comparative study between BSA and HSA
    • [12] Han, X.-L., Tian, F.-F., Ge, Y.-S., Jiang, F.-L., Lai, L., Li, D.-W., Yu, Q.-L., Wang, J., Lin, C., Liu, Y., Spectroscopic, structural and thermodynamic properties of chlorpyrifos bound to serum albumin: a comparative study between BSA and HSA. J. Photochem. Photobiol. B Biol. 109 (2012), 1–11.
    • (2012) J. Photochem. Photobiol. B Biol. , vol.109 , pp. 1-11
    • Han, X.-L.1    Tian, F.-F.2    Ge, Y.-S.3    Jiang, F.-L.4    Lai, L.5    Li, D.-W.6    Yu, Q.-L.7    Wang, J.8    Lin, C.9    Liu, Y.10
  • 13
    • 84866661019 scopus 로고    scopus 로고
    • Structures of bovine, equine and leporine serum albumin
    • [13] Bujacz, A., Structures of bovine, equine and leporine serum albumin. Acta Crystallogr. D Biol. Crystallogr. 68 (2012), 1278–1289.
    • (2012) Acta Crystallogr. D Biol. Crystallogr. , vol.68 , pp. 1278-1289
    • Bujacz, A.1
  • 14
    • 84907153180 scopus 로고    scopus 로고
    • Spectroscopic analyses on interaction of bovine serum albumin with novel spiro [cyclopropane-pyrrolizin]
    • [14] Yu, X., Liao, Z., Jiang, B., Hu, X., Li, X., Spectroscopic analyses on interaction of bovine serum albumin with novel spiro [cyclopropane-pyrrolizin]. Spectrochim. Acta A Mol. Biomol. Spectrosc. 137 (2015), 129–136.
    • (2015) Spectrochim. Acta A Mol. Biomol. Spectrosc. , vol.137 , pp. 129-136
    • Yu, X.1    Liao, Z.2    Jiang, B.3    Hu, X.4    Li, X.5
  • 15
    • 84931070586 scopus 로고    scopus 로고
    • Spectrofluorimetric study of finasteride and bovine serum albumin interaction and its application for quantitative determination of finasteride in tablet dosage form
    • [15] Abdelhameed, A.S., Alanazi, A.M., Kadi, A.A., Spectrofluorimetric study of finasteride and bovine serum albumin interaction and its application for quantitative determination of finasteride in tablet dosage form. Anal. Methods, 2015.
    • (2015) Anal. Methods
    • Abdelhameed, A.S.1    Alanazi, A.M.2    Kadi, A.A.3
  • 16
    • 84926680562 scopus 로고    scopus 로고
    • Insight into the interaction between the HIV-1 integrase inhibitor elvitegravir and bovine serum albumin: a spectroscopic study
    • [16] Abdelhameed, A.S., Insight into the interaction between the HIV-1 integrase inhibitor elvitegravir and bovine serum albumin: a spectroscopic study. J. Spectrosc., 2015, 2015.
    • (2015) J. Spectrosc. , vol.2015
    • Abdelhameed, A.S.1
  • 17
    • 84946552894 scopus 로고    scopus 로고
    • Spectroscopic and molecular docking studies of binding interaction of gefitinib, lapatinib and sunitinib with bovine serum albumin (BSA)
    • [17] Shen, G.-F., Liu, T.-T., Wang, Q., Jiang, M., Shi, J.-H., Spectroscopic and molecular docking studies of binding interaction of gefitinib, lapatinib and sunitinib with bovine serum albumin (BSA). J. Photochem. Photobiol. B Biol. 153 (2015), 380–390.
    • (2015) J. Photochem. Photobiol. B Biol. , vol.153 , pp. 380-390
    • Shen, G.-F.1    Liu, T.-T.2    Wang, Q.3    Jiang, M.4    Shi, J.-H.5
  • 18
    • 84954532963 scopus 로고    scopus 로고
    • A spectroscopic approach to investigate the molecular interactions between the newly approved irreversible ErbB blocker “afatinib” and bovine serum albumin
    • [18] Alanazi, A.M., Abdelhameed, A.S., A spectroscopic approach to investigate the molecular interactions between the newly approved irreversible ErbB blocker “afatinib” and bovine serum albumin. PloS one, 11, 2016.
    • (2016) PloS one , vol.11
    • Alanazi, A.M.1    Abdelhameed, A.S.2
  • 19
    • 11844253806 scopus 로고    scopus 로고
    • Flavonoid–serum albumin complexation: determination of binding constants and binding sites by fluorescence spectroscopy
    • [19] Dufour, C., Dangles, O., Flavonoid–serum albumin complexation: determination of binding constants and binding sites by fluorescence spectroscopy. Biochim. Biophys. Acta Gen. Subj. 1721 (2005), 164–173.
    • (2005) Biochim. Biophys. Acta Gen. Subj. , vol.1721 , pp. 164-173
    • Dufour, C.1    Dangles, O.2
  • 20
    • 77953865084 scopus 로고    scopus 로고
    • Principles of Fluorescence Spectroscopy
    • Springer Science & Business Media
    • [20] Lakowicz, J.R., Principles of Fluorescence Spectroscopy. 2007, Springer Science & Business Media.
    • (2007)
    • Lakowicz, J.R.1
  • 21
    • 84866661019 scopus 로고    scopus 로고
    • Structures of bovine, equine and leporine serum albumin
    • [21] Bujacz, A., Structures of bovine, equine and leporine serum albumin. Acta Crystallogr., Sect. D: Biol. Crystallogr. 68 (2012), 1278–1289.
    • (2012) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.68 , pp. 1278-1289
    • Bujacz, A.1
  • 22
    • 84876432877 scopus 로고    scopus 로고
    • MVD 5.0 Molegro Virtual Docker, DK-8000
    • Aarhus C Denmark
    • [22] Molegro, A., MVD 5.0 Molegro Virtual Docker, DK-8000. 2011, Aarhus C, Denmark.
    • (2011)
    • Molegro, A.1
  • 23
    • 77951884633 scopus 로고    scopus 로고
    • Suite Kerwin, Sean M
    • [23] Ultra, C., Suite Kerwin, Sean M. J. Am. Chem. Soc. 132 (2010), 2466–2467.
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 2466-2467
    • Ultra, C.1
  • 24
    • 84893023464 scopus 로고    scopus 로고
    • Probing the interaction of lysozyme with ciprofloxacin in the presence of different-sized Ag nano-particles by multispectroscopic techniques and isothermal titration calorimetry
    • [24] Pasban Ziyarat, F., Asoodeh, A., Sharif Barfeh, Z., Pirouzi, M., Chamani, J., Probing the interaction of lysozyme with ciprofloxacin in the presence of different-sized Ag nano-particles by multispectroscopic techniques and isothermal titration calorimetry. J. Biomol. Struct. Dyn. 32 (2014), 613–629.
    • (2014) J. Biomol. Struct. Dyn. , vol.32 , pp. 613-629
    • Pasban Ziyarat, F.1    Asoodeh, A.2    Sharif Barfeh, Z.3    Pirouzi, M.4    Chamani, J.5
  • 25
    • 84873453386 scopus 로고    scopus 로고
    • Binding sites of resveratrol, Genistein, and curcumin with milk α- and β-caseins
    • [25] Bourassa, P., Bariyanga, J., Tajmir-Riahi, H.A., Binding sites of resveratrol, Genistein, and curcumin with milk α- and β-caseins. J. Phys. Chem. B 117 (2013), 1287–1295.
    • (2013) J. Phys. Chem. B , vol.117 , pp. 1287-1295
    • Bourassa, P.1    Bariyanga, J.2    Tajmir-Riahi, H.A.3
  • 26
    • 84887572498 scopus 로고    scopus 로고
    • Insights into the selective binding and toxic mechanism of microcystin to catalase
    • [26] Hu, Y., Da, L., Insights into the selective binding and toxic mechanism of microcystin to catalase. Spectrochim. Acta A Mol. Biomol. Spectrosc. 121 (2014), 230–237.
    • (2014) Spectrochim. Acta A Mol. Biomol. Spectrosc. , vol.121 , pp. 230-237
    • Hu, Y.1    Da, L.2
  • 27
    • 42149099792 scopus 로고    scopus 로고
    • Principle of Fluorescence Spectroscopy
    • second ed. Plemum Press New York
    • [27] Lakowicz, J.R., Principle of Fluorescence Spectroscopy. second ed., 1999, Plemum Press, New York.
    • (1999)
    • Lakowicz, J.R.1
  • 28
    • 84879685262 scopus 로고    scopus 로고
    • Fluorescence quenching of 4-tert-Octylphenol by room temperature ionic liquids and its application
    • [28] Wang, H., Mao, J., Duan, A., Che, B., Wang, W., Ma, M., Wang, X., Fluorescence quenching of 4-tert-Octylphenol by room temperature ionic liquids and its application. J. Fluoresc. 23 (2013), 323–331.
    • (2013) J. Fluoresc. , vol.23 , pp. 323-331
    • Wang, H.1    Mao, J.2    Duan, A.3    Che, B.4    Wang, W.5    Ma, M.6    Wang, X.7
  • 29
    • 0003955174 scopus 로고
    • Spectrofluorimetric Analytical Method
    • second ed. Science Press Beijing
    • [29] Chen, G.-Z., Huang, X.-Z., Xu, J.-G., Spectrofluorimetric Analytical Method. second ed., 1990, Science Press, Beijing.
    • (1990)
    • Chen, G.-Z.1    Huang, X.-Z.2    Xu, J.-G.3
  • 30
    • 33947357739 scopus 로고    scopus 로고
    • Spectroscopic studies on the interaction between silicotungstic acid and bovine serum albumin
    • [30] Wang, Y.Q., Zhang, H.M., Zhang, G.C., Tao, W.H., Fei, Z.H., Liu, Z.T., Spectroscopic studies on the interaction between silicotungstic acid and bovine serum albumin. J. Pharm. Biomed. Anal. 43 (2007), 1869–1875.
    • (2007) J. Pharm. Biomed. Anal. , vol.43 , pp. 1869-1875
    • Wang, Y.Q.1    Zhang, H.M.2    Zhang, G.C.3    Tao, W.H.4    Fei, Z.H.5    Liu, Z.T.6
  • 31
    • 17444414634 scopus 로고    scopus 로고
    • Dendrimer interactions with hydrophobic fluorescent probes and human serum albumin
    • [31] Shcharbin, D., Klajnert, B., Mazhul, V., Bryszewska, M., Dendrimer interactions with hydrophobic fluorescent probes and human serum albumin. J. Fluoresc. 15 (2005), 21–28.
    • (2005) J. Fluoresc. , vol.15 , pp. 21-28
    • Shcharbin, D.1    Klajnert, B.2    Mazhul, V.3    Bryszewska, M.4
  • 32
    • 0002388667 scopus 로고
    • The extinction period of fluorescence
    • [32] Stern, O., Volmer, M., The extinction period of fluorescence. Phys. Z. 20 (1919), 183–188.
    • (1919) Phys. Z. , vol.20 , pp. 183-188
    • Stern, O.1    Volmer, M.2
  • 33
    • 33751330608 scopus 로고
    • The determination of enzyme dissociation constants
    • [33] Lineweaver, H., Burk, D., The determination of enzyme dissociation constants. J. Am. Chem. Soc. 56 (1934), 658–666.
    • (1934) J. Am. Chem. Soc. , vol.56 , pp. 658-666
    • Lineweaver, H.1    Burk, D.2
  • 34
    • 0035808405 scopus 로고    scopus 로고
    • Flow-injection analysis chemiluminescence detection combined with microdialysis sampling for studying protein binding of drug
    • [34] Huang, Y., Zhang, Z., Zhang, D., Lv, J., Flow-injection analysis chemiluminescence detection combined with microdialysis sampling for studying protein binding of drug. Talanta 53 (2001), 835–841.
    • (2001) Talanta , vol.53 , pp. 835-841
    • Huang, Y.1    Zhang, Z.2    Zhang, D.3    Lv, J.4
  • 35
    • 0015907980 scopus 로고
    • Quenching of fluorescence by oxygen. Probe for structural fluctuations in macromolecules
    • [35] Lakowicz, J.R., Weber, G., Quenching of fluorescence by oxygen. Probe for structural fluctuations in macromolecules. Biochemistry 12 (1973), 4161–4170.
    • (1973) Biochemistry , vol.12 , pp. 4161-4170
    • Lakowicz, J.R.1    Weber, G.2
  • 36
    • 1842426864 scopus 로고
    • Oxygen quenching of fluorescence in solution: an experimental study of the diffusion process
    • [36] Ware, W.R., Oxygen quenching of fluorescence in solution: an experimental study of the diffusion process. J. Phys. Chem. 66 (1962), 455–458.
    • (1962) J. Phys. Chem. , vol.66 , pp. 455-458
    • Ware, W.R.1
  • 37
    • 0642316329 scopus 로고    scopus 로고
    • Interaction of magnolol with bovine serum albumin: a fluorescence-quenching study
    • [37] Liu, J., Tian, J.-n., Zhang, J., Hu, Z., Chen, X., Interaction of magnolol with bovine serum albumin: a fluorescence-quenching study. Anal. Bioanal. Chem. 376 (2003), 864–867.
    • (2003) Anal. Bioanal. Chem. , vol.376 , pp. 864-867
    • Liu, J.1    Tian, J.-N.2    Zhang, J.3    Hu, Z.4    Chen, X.5
  • 38
    • 0003468776 scopus 로고    scopus 로고
    • Modern Quantum Chemistry
    • Academic Press New York
    • [38] Forster, T., Sinanoglu, O., Modern Quantum Chemistry. 1996, Academic Press, New York.
    • (1996)
    • Forster, T.1    Sinanoglu, O.2
  • 39
    • 84903955016 scopus 로고    scopus 로고
    • Study on the interaction between amphiphilic drug and bovine serum albumin: a thermodynamic and spectroscopic description
    • [39] Rub, M.A., Khan, J.M., Asiri, A.M., Khan, R.H., ud-Din, K., Study on the interaction between amphiphilic drug and bovine serum albumin: a thermodynamic and spectroscopic description. J. Lumin. 155 (2014), 39–46.
    • (2014) J. Lumin. , vol.155 , pp. 39-46
    • Rub, M.A.1    Khan, J.M.2    Asiri, A.M.3    Khan, R.H.4    ud-Din, K.5
  • 40
    • 0019889063 scopus 로고
    • Thermodynamics of protein association reactions: forces contributing to stability
    • [40] Ross, P.D., Subramanian, S., Thermodynamics of protein association reactions: forces contributing to stability. Biochemistry 20 (1981), 3096–3102.
    • (1981) Biochemistry , vol.20 , pp. 3096-3102
    • Ross, P.D.1    Subramanian, S.2
  • 41
    • 2342509585 scopus 로고    scopus 로고
    • Spectrofluorimetric study of the binding of daphnetin to bovine serum albumin
    • [41] Liu, J., Tian, J., He, W., Xie, J., Hu, Z., Chen, X., Spectrofluorimetric study of the binding of daphnetin to bovine serum albumin. J. Pharm. Biomed. Anal. 35 (2004), 671–677.
    • (2004) J. Pharm. Biomed. Anal. , vol.35 , pp. 671-677
    • Liu, J.1    Tian, J.2    He, W.3    Xie, J.4    Hu, Z.5    Chen, X.6
  • 42
    • 84919341467 scopus 로고    scopus 로고
    • Elucidating the interaction of limonene with bovine serum albumin: a multi-technique approach
    • [42] Chaturvedi, S.K., Ahmad, E., Khan, J.M., Alam, P., Ishtikhar, M., Khan, R.H., Elucidating the interaction of limonene with bovine serum albumin: a multi-technique approach. Mol. BioSyst. 11 (2015), 307–316.
    • (2015) Mol. BioSyst. , vol.11 , pp. 307-316
    • Chaturvedi, S.K.1    Ahmad, E.2    Khan, J.M.3    Alam, P.4    Ishtikhar, M.5    Khan, R.H.6
  • 43
    • 68749119350 scopus 로고    scopus 로고
    • Interaction between levamisole hydrochloride and bovine serum albumin and the influence of alcohol: spectra
    • [43] Yan, H., Zhao, S., Yang, J., Zhu, X., Dai, G., Liang, H., Pan, F., Weng, L., Interaction between levamisole hydrochloride and bovine serum albumin and the influence of alcohol: spectra. J. Solut. Chem. 38 (2009), 1183–1192.
    • (2009) J. Solut. Chem. , vol.38 , pp. 1183-1192
    • Yan, H.1    Zhao, S.2    Yang, J.3    Zhu, X.4    Dai, G.5    Liang, H.6    Pan, F.7    Weng, L.8
  • 44
    • 43349091039 scopus 로고    scopus 로고
    • Interaction between Glyoxal-bis-(2-hydroxyanil) and bovine serum albumin in solution
    • [44] Zhang, H.-X., Huang, X., Mei, P., Gao, S., Interaction between Glyoxal-bis-(2-hydroxyanil) and bovine serum albumin in solution. J. Solut. Chem. 37 (2008), 631–640.
    • (2008) J. Solut. Chem. , vol.37 , pp. 631-640
    • Zhang, H.-X.1    Huang, X.2    Mei, P.3    Gao, S.4
  • 45
    • 0037009311 scopus 로고    scopus 로고
    • Interaction of drugs with bovine and human serum albumin
    • [45] Sułkowska, A., Interaction of drugs with bovine and human serum albumin. J. Mol. Struct. 614 (2002), 227–232.
    • (2002) J. Mol. Struct. , vol.614 , pp. 227-232
    • Sułkowska, A.1
  • 47
    • 84898647419 scopus 로고    scopus 로고
    • Molecular interaction study of flavonoid derivative 3d with human serum albumin using multispectroscopic and molecular modeling approach
    • [47] Wei, J., Jin, F., Wu, Q., Jiang, Y., Gao, D., Liu, H., Molecular interaction study of flavonoid derivative 3d with human serum albumin using multispectroscopic and molecular modeling approach. Talanta 126 (2014), 116–121.
    • (2014) Talanta , vol.126 , pp. 116-121
    • Wei, J.1    Jin, F.2    Wu, Q.3    Jiang, Y.4    Gao, D.5    Liu, H.6


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