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Volumn 78, Issue 1-4, 2014, Pages 405-413

A spectroscopic study on the interaction between the anticancer drug erlotinib and human serum albumin

Author keywords

Circular dichroism; Erlotinib; Fluorescence; FTIR; Serum albumin; UV Vis

Indexed keywords


EID: 84893812083     PISSN: 09230750     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10847-013-0311-4     Document Type: Article
Times cited : (21)

References (34)
  • 1
    • 85081455739 scopus 로고    scopus 로고
    • Pseudo-enzymatic hydrolysis of 4-nitrophenyl myristate by human serum albumin
    • Ascenzi, P.; Fasano, M.: Pseudo-enzymatic hydrolysis of 4-nitrophenyl myristate by human serum albumin. Biochem. Biophys. Res. Commun. 424, 3 (2012)
    • (2012) Biochem. Biophys. Res. Commun. , vol.424 , pp. 3
    • Ascenzi, P.1    Fasano, M.2
  • 3
    • 84862776506 scopus 로고    scopus 로고
    • Recent progress and perspectives on the toxicity of carbon nanotubes at organism, organ, cell, and biomacromolecule levels
    • 1:CAS:528:DC%2BC38XhsFylt7s%3D 10.1016/j.envint.2011.12.003
    • Zhao, X.C.; Liu, R.T.: Recent progress and perspectives on the toxicity of carbon nanotubes at organism, organ, cell, and biomacromolecule levels. Environ. Int. 40, 244-255 (2012)
    • (2012) Environ. Int. , vol.40 , pp. 244-255
    • Zhao, X.C.1    Liu, R.T.2
  • 4
    • 67651230412 scopus 로고    scopus 로고
    • Probing the interaction of magnetic iron oxide nanoparticles with bovine serum albumin by spectroscopic techniques
    • 1:CAS:528:DC%2BD1MXot1ejurY%3D 10.1021/jp904004w
    • Yang, Q.Q.; Liang, J.G.; Han, H.Y.: Probing the interaction of magnetic iron oxide nanoparticles with bovine serum albumin by spectroscopic techniques. J. Phys. Chem. B 113(30), 10454-10458 (2009)
    • (2009) J. Phys. Chem. B , vol.113 , Issue.30 , pp. 10454-10458
    • Yang, Q.Q.1    Liang, J.G.2    Han, H.Y.3
  • 5
    • 59849124286 scopus 로고    scopus 로고
    • Interaction of malachite green with bovine serum albumin: Determination of the binding mechanism and binding site by spectroscopic methods
    • 1:CAS:528:DC%2BD1MXhvFaitr0%3D 10.1016/j.jhazmat.2008.07.132
    • Zhang, Y.Z.; Zhou, B.; Zhang, X.P.; Huang, P.; Li, C.H.; Liu, Y.: Interaction of malachite green with bovine serum albumin: determination of the binding mechanism and binding site by spectroscopic methods. J. Hazard. Mater. 163(2-3), 1345-1352 (2009)
    • (2009) J. Hazard. Mater. , vol.163 , Issue.2-3 , pp. 1345-1352
    • Zhang, Y.Z.1    Zhou, B.2    Zhang, X.P.3    Huang, P.4    Li, C.H.5    Liu, Y.6
  • 7
    • 34249933404 scopus 로고    scopus 로고
    • Erlotinib plus gemcitabine compared with gemcitabine alone in patients with advanced pancreatic cancer: A phase III trial of the national cancer institute of Canada clinical trials group
    • 1:CAS:528:DC%2BD2sXmvVWmsr0%3D 10.1200/JCO.2006.07.9525
    • Moore, M.J.; Goldstein, D.; Hamm, J.; Figer, A.; Hecht, J.R.; Gallinger, S.; Au, H.J.; Murawa, P.; Walde, D.; Wolff, R.A.: Erlotinib plus gemcitabine compared with gemcitabine alone in patients with advanced pancreatic cancer: a phase III trial of the national cancer institute of Canada clinical trials group. J. Clin. Oncol. 25(15), 1960-1966 (2007)
    • (2007) J. Clin. Oncol. , vol.25 , Issue.15 , pp. 1960-1966
    • Moore, M.J.1    Goldstein, D.2    Hamm, J.3    Figer, A.4    Hecht, J.R.5    Gallinger, S.6    Au, H.J.7    Murawa, P.8    Walde, D.9    Wolff, R.A.10
  • 9
    • 84155167751 scopus 로고    scopus 로고
    • Spectroscopic investigation of the interaction of the toxicant, 2-naphthylamine, with bovine serum albumin
    • 10.1002/jbt.20400
    • Liu, Y.; Chen, M.; Bian, G.; Liu, J.; Song, L.: Spectroscopic investigation of the interaction of the toxicant, 2-naphthylamine, with bovine serum albumin. J. Biochem. Mol. Toxicol. 25, 362 (2011)
    • (2011) J. Biochem. Mol. Toxicol. , vol.25 , pp. 362
    • Liu, Y.1    Chen, M.2    Bian, G.3    Liu, J.4    Song, L.5
  • 10
    • 79960570363 scopus 로고    scopus 로고
    • Composition and stability of anthocyanins from purple Solanum tuberosum and their protective influence on Cr(VI) targeted to bovine serum albumin
    • 1:CAS:528:DC%2BC3MXnslKju7Y%3D 10.1021/jf2011408
    • Zhao, X.; Sheng, F.; Zheng, J.; Liu, R.: Composition and stability of anthocyanins from purple Solanum tuberosum and their protective influence on Cr(VI) targeted to bovine serum albumin. J. Agric. Food Chem. 59(14), 7902-7909 (2011)
    • (2011) J. Agric. Food Chem. , vol.59 , Issue.14 , pp. 7902-7909
    • Zhao, X.1    Sheng, F.2    Zheng, J.3    Liu, R.4
  • 11
    • 79955975049 scopus 로고    scopus 로고
    • Separate and simultaneous binding effects of aspirin and amlodipine to human serum albumin based on fluorescence spectroscopic and molecular modeling characterizations: A mechanistic insight for determining usage drugs doses
    • 1:CAS:528:DC%2BC3MXmvFyitb8%3D 10.1016/j.jlumin.2011.04.043
    • Abdollahpour, N.; Asoodeh, A.; Saberi, M.R.; Chamani, J.: Separate and simultaneous binding effects of aspirin and amlodipine to human serum albumin based on fluorescence spectroscopic and molecular modeling characterizations: a mechanistic insight for determining usage drugs doses. J. Lumin. 131(9), 1885-1899 (2011)
    • (2011) J. Lumin. , vol.131 , Issue.9 , pp. 1885-1899
    • Abdollahpour, N.1    Asoodeh, A.2    Saberi, M.R.3    Chamani, J.4
  • 12
    • 80054853074 scopus 로고    scopus 로고
    • Binding of Sudan II and Sudan IV to bovine serum albumin: Comparison studies
    • 1:CAS:528:DC%2BC3MXhsFSjt7jL 10.1016/j.fct.2011.09.011
    • Lu, D.W.; Zhao, X.C.; Zhao, Y.C.; Zhang, B.C.; Zhang, B.; Geng, M.Y.; Liu, R.T.: Binding of Sudan II and Sudan IV to bovine serum albumin: comparison studies. Food Chem. Toxicol. 49(12), 3158-3164 (2011)
    • (2011) Food Chem. Toxicol. , vol.49 , Issue.12 , pp. 3158-3164
    • Lu, D.W.1    Zhao, X.C.2    Zhao, Y.C.3    Zhang, B.C.4    Zhang, B.5    Geng, M.Y.6    Liu, R.T.7
  • 13
    • 33750171095 scopus 로고    scopus 로고
    • Study of the interaction of artemisinin with bovine serum albumin
    • 1:CAS:528:DC%2BD28XhtFCjsrvO 10.1016/j.ijbiomac.2006.04.008
    • Bian, H.; Li, M.; Yu, Q.; Chen, Z.; Tian, J.; Liang, H.: Study of the interaction of artemisinin with bovine serum albumin. Int. J. Biol. Macromol. 39(4), 291-297 (2006)
    • (2006) Int. J. Biol. Macromol. , vol.39 , Issue.4 , pp. 291-297
    • Bian, H.1    Li, M.2    Yu, Q.3    Chen, Z.4    Tian, J.5    Liang, H.6
  • 14
    • 61949432567 scopus 로고    scopus 로고
    • Structural analysis of human serum albumin complexes with cationic lipids
    • 1:CAS:528:DC%2BD1MXls1eisQ%3D%3D 10.1021/jp8092012
    • Charbonneau, D.; Beauregard, M.; Tajmir-Riahi, H.A.: Structural analysis of human serum albumin complexes with cationic lipids. J. Phys. Chem. B 113(6), 1777-1784 (2009)
    • (2009) J. Phys. Chem. B , vol.113 , Issue.6 , pp. 1777-1784
    • Charbonneau, D.1    Beauregard, M.2    Tajmir-Riahi, H.A.3
  • 15
    • 75649126908 scopus 로고    scopus 로고
    • Study on the interaction of cationic lipids with bovine serum albumin
    • 1:CAS:528:DC%2BD1MXhsFWmur%2FL 10.1021/jp910077h
    • Charbonneau, D.M.; Tajmir-Riahi, H.A.: Study on the interaction of cationic lipids with bovine serum albumin. J. Phys. Chem. B 114(2), 1148-1155 (2010)
    • (2010) J. Phys. Chem. B , vol.114 , Issue.2 , pp. 1148-1155
    • Charbonneau, D.M.1    Tajmir-Riahi, H.A.2
  • 16
    • 80054885852 scopus 로고    scopus 로고
    • New insight into molecular interactions of imidazolium ionic liquids with bovine serum albumin
    • 1:CAS:528:DC%2BC3MXht1Kkt7%2FP 10.1021/jp2071925
    • Shu, Y.; Liu, M.; Chen, S.; Chen, X.; Wang, J.: New insight into molecular interactions of imidazolium ionic liquids with bovine serum albumin. J. Phys. Chem. B 115(42), 12306-12314 (2011)
    • (2011) J. Phys. Chem. B , vol.115 , Issue.42 , pp. 12306-12314
    • Shu, Y.1    Liu, M.2    Chen, S.3    Chen, X.4    Wang, J.5
  • 17
    • 78651497578 scopus 로고    scopus 로고
    • The interaction between Ag(+) and bovine serum albumin: A spectroscopic investigation
    • 1:CAS:528:DC%2BC3MXnvVehuw%3D%3D 10.1016/j.scitotenv.2010.11.004
    • Zhao, X.; Liu, R.; Teng, Y.; Liu, X.: The interaction between Ag(+) and bovine serum albumin: a spectroscopic investigation. Sci. Total Environ. 409(5), 892-897 (2011)
    • (2011) Sci. Total Environ. , vol.409 , Issue.5 , pp. 892-897
    • Zhao, X.1    Liu, R.2    Teng, Y.3    Liu, X.4
  • 18
    • 79951768026 scopus 로고    scopus 로고
    • Lomefloxacin promotes the interaction between human serum albumin and transferrin: A mechanistic insight into the emergence of antibiotic's side effects
    • 1:CAS:528:DC%2BC3MXisFyqtr0%3D 10.1016/j.jpba.2010.12.029
    • Chamani, J.; Vahedian-Movahed, H.; Saberi, M.R.: 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. 55(1), 114-124 (2011)
    • (2011) J. Pharm. Biomed. Anal. , vol.55 , Issue.1 , pp. 114-124
    • Chamani, J.1    Vahedian-Movahed, H.2    Saberi, M.R.3
  • 19
    • 84871622499 scopus 로고    scopus 로고
    • Interaction between triazine herbicide and catalase by fluorescence spectrum
    • 1:CAS:528:DC%2BD3sXovFGrsbc%3D
    • Liu, W.P.; Yang, W.C.; Liu, H.J.; Tong, S.L.; Fang, Z.H.: Interaction between triazine herbicide and catalase by fluorescence spectrum. Spectrosc. Spectr. Anal. 23(5), 926-929 (2003)
    • (2003) Spectrosc. Spectr. Anal. , vol.23 , Issue.5 , pp. 926-929
    • Liu, W.P.1    Yang, W.C.2    Liu, H.J.3    Tong, S.L.4    Fang, Z.H.5
  • 20
    • 38549113419 scopus 로고    scopus 로고
    • Potential protein toxicity of synthetic pigments: Binding of poncean S to human serum albumin
    • 1:CAS:528:DC%2BD1cXhsVahsLo%3D 10.1529/biophysj.107.120865
    • Gao, H.-W.; Xu, Q.; Chen, L.; Wang, S.-L.; Wang, Y.; Wu, L.-L.; Yuan, Y.: Potential protein toxicity of synthetic pigments: binding of poncean S to human serum albumin. Biophys. J. 94(3), 906-917 (2008)
    • (2008) Biophys. J. , vol.94 , Issue.3 , pp. 906-917
    • Gao, H.-W.1    Xu, Q.2    Chen, L.3    Wang, S.-L.4    Wang, Y.5    Wu, L.-L.6    Yuan, Y.7
  • 21
    • 0019889063 scopus 로고
    • Thermodynamics of protein association reactions: Forces contributing to stability
    • 1:CAS:528:DyaL3MXktF2qsb0%3D 10.1021/bi00514a017
    • Ross, P.D.; Subramanian, S.: Thermodynamics of protein association reactions: forces contributing to stability. Biochemistry 20(11), 3096-3102 (1981)
    • (1981) Biochemistry , vol.20 , Issue.11 , pp. 3096-3102
    • Ross, P.D.1    Subramanian, S.2
  • 22
    • 77951939147 scopus 로고    scopus 로고
    • Spectroscopic studies on the binding of cobalt(II) 1,10-phenanthroline complex to bovine serum albumin
    • 1:CAS:528:DC%2BC3cXlsVGisb0%3D 10.1007/s12011-009-8502-y
    • Zhang, Y.Z.; Li, H.R.; Dai, J.; Chen, W.J.; Zhang, J.; Liu, Y.: Spectroscopic studies on the binding of cobalt(II) 1,10-phenanthroline complex to bovine serum albumin. Biol. Trace Elem. Res. 135(1-3), 136-152 (2010)
    • (2010) Biol. Trace Elem. Res. , vol.135 , Issue.1-3 , pp. 136-152
    • Zhang, Y.Z.1    Li, H.R.2    Dai, J.3    Chen, W.J.4    Zhang, J.5    Liu, Y.6
  • 23
    • 84858994128 scopus 로고    scopus 로고
    • Use of spectroscopic, zeta potential and molecular dynamic techniques to study the interaction between human holo-transferrin and two antagonist drugs: Comparison of binary and ternary systems
    • 1:CAS:528:DC%2BC38Xks1Gqtrg%3D 10.3390/molecules17033114
    • Kabiri, M.; Amiri-Tehranizadeh, Z.; Baratian, A.; Saberi, M.R.; Chamani, J.: Use of spectroscopic, zeta potential and molecular dynamic techniques to study the interaction between human holo-transferrin and two antagonist drugs: comparison of binary and ternary systems. Molecules 17(3), 3114-3147 (2012)
    • (2012) Molecules , vol.17 , Issue.3 , pp. 3114-3147
    • Kabiri, M.1    Amiri-Tehranizadeh, Z.2    Baratian, A.3    Saberi, M.R.4    Chamani, J.5
  • 24
    • 65249134878 scopus 로고    scopus 로고
    • Investigation of the interaction between berberine and human serum albumin
    • 1:CAS:528:DC%2BD1MXhtVOgt7g%3D 10.1021/bm801120k
    • Hu, Y.J.; Liu, Y.; Xiao, X.H.: Investigation of the interaction between berberine and human serum albumin. Biomacromolecules 10(3), 517-521 (2009)
    • (2009) Biomacromolecules , vol.10 , Issue.3 , pp. 517-521
    • Hu, Y.J.1    Liu, Y.2    Xiao, X.H.3
  • 25
    • 84856228563 scopus 로고    scopus 로고
    • Separate and simultaneous binding effects through a non-cooperative behavior between cyclophosphamide hydrochloride and fluoxymesterone upon interaction with human serum albumin: Multi-spectroscopic and molecular modeling approaches
    • 1:CAS:528:DC%2BC38XhsVahs74%3D 10.1016/j.saa.2011.12.026
    • Zohoorian-Abootorabi, T.; Sanee, H.; Iranfar, H.; Saberi, M.R.; Chamani, J.: Separate and simultaneous binding effects through a non-cooperative behavior between cyclophosphamide hydrochloride and fluoxymesterone upon interaction with human serum albumin: multi-spectroscopic and molecular modeling approaches. Spectrochim. Acta A 88, 177-191 (2012)
    • (2012) Spectrochim. Acta A , vol.88 , pp. 177-191
    • Zohoorian-Abootorabi, T.1    Sanee, H.2    Iranfar, H.3    Saberi, M.R.4    Chamani, J.5
  • 26
    • 84863042617 scopus 로고    scopus 로고
    • Binding of phthalate plasticizers to human serum albumin in vitro: A multispectroscopic approach and molecular modeling
    • 1:CAS:528:DC%2BC3MXhs12hsLfJ 10.1021/jf204380r
    • Zhou, X.-M.; Lue, W.-J.; Su, L.; Shan, Z.-J.; Chen, X.-G.: Binding of phthalate plasticizers to human serum albumin in vitro: a multispectroscopic approach and molecular modeling. J. Agric. Food Chem. 60(4), 1135-1145 (2012)
    • (2012) J. Agric. Food Chem. , vol.60 , Issue.4 , pp. 1135-1145
    • Zhou, X.-M.1    Lue, W.-J.2    Su, L.3    Shan, Z.-J.4    Chen, X.-G.5
  • 27
    • 84863362068 scopus 로고    scopus 로고
    • Probing the binding of the flavonoid diosmetin to human serum albumin by multispectroscopic techniques
    • 1:CAS:528:DC%2BC38Xis1Ogtbo%3D 10.1021/jf205260g
    • Zhang, G.; Wang, L.; Pan, J.: Probing the binding of the flavonoid diosmetin to human serum albumin by multispectroscopic techniques. J. Agric. Food Chem. 60(10), 2721-2729 (2012)
    • (2012) J. Agric. Food Chem. , vol.60 , Issue.10 , pp. 2721-2729
    • Zhang, G.1    Wang, L.2    Pan, J.3
  • 28
    • 80053996719 scopus 로고    scopus 로고
    • Investigation of three flavonoids binding to bovine serum albumin using molecular fluorescence technique
    • 1:CAS:528:DC%2BC3MXhtlWltr3P 10.1016/j.jlumin.2011.08.014
    • Bi, S.; Yan, L.; Pang, B.; Wang, Y.: Investigation of three flavonoids binding to bovine serum albumin using molecular fluorescence technique. J. Lumin. 132(1), 132-140 (2012)
    • (2012) J. Lumin. , vol.132 , Issue.1 , pp. 132-140
    • Bi, S.1    Yan, L.2    Pang, B.3    Wang, Y.4
  • 29
    • 79952489321 scopus 로고    scopus 로고
    • Spectroscopic studies of 7,8-dihydroxy-4-methylcoumarin and its interaction with bovine serum albumin
    • 1:CAS:528:DC%2BC3MXjtVCqtL4%3D 10.1016/j.jlumin.2010.12.021
    • Hussein, B.H.M.: Spectroscopic studies of 7,8-dihydroxy-4-methylcoumarin and its interaction with bovine serum albumin. J. Lumin. 131(5), 900-908 (2011)
    • (2011) J. Lumin. , vol.131 , Issue.5 , pp. 900-908
    • Hussein, B.H.M.1
  • 30
    • 77951545330 scopus 로고    scopus 로고
    • New insights into the behavior of bovine serum albumin adsorbed onto carbon nanotubes: Comprehensive spectroscopic studies
    • 1:CAS:528:DC%2BC3cXksVamtbY%3D 10.1021/jp100903x
    • Zhao, X.C.; Liu, R.T.; Chi, Z.X.; Teng, Y.; Qin, P.F.: New insights into the behavior of bovine serum albumin adsorbed onto carbon nanotubes: comprehensive spectroscopic studies. J. Phys. Chem. B 114(16), 5625-5631 (2010)
    • (2010) J. Phys. Chem. B , vol.114 , Issue.16 , pp. 5625-5631
    • Zhao, X.C.1    Liu, R.T.2    Chi, Z.X.3    Teng, Y.4    Qin, P.F.5
  • 31
    • 78650240100 scopus 로고    scopus 로고
    • The effect of anti-tubercular drug, ethionamide on the secondary structure of serum albumins: A biophysical study
    • 10.1016/j.jpba.2010.10.027
    • Katrahalli, U.; Kalalbandi, V.K.A.; Jaldappagari, S.: The effect of anti-tubercular drug, ethionamide on the secondary structure of serum albumins: a biophysical study. J. Pharm. Biomed. Anal. 54, 807-811 (2011)
    • (2011) J. Pharm. Biomed. Anal. , vol.54 , pp. 807-811
    • Katrahalli, U.1    Kalalbandi, V.K.A.2    Jaldappagari, S.3
  • 32
    • 19444375863 scopus 로고    scopus 로고
    • Interaction of wogonin with bovine serum albumin
    • 1:CAS:528:DC%2BD2MXks1Gjs70%3D 10.1016/j.bmc.2005.02.065
    • Tian, J.N.; Liu, J.Q.; Hu, Z.; Chen, X.G.: Interaction of wogonin with bovine serum albumin. Bioorg. Med. Chem. 13(12), 4124-4129 (2005)
    • (2005) Bioorg. Med. Chem. , vol.13 , Issue.12 , pp. 4124-4129
    • Tian, J.N.1    Liu, J.Q.2    Hu, Z.3    Chen, X.G.4
  • 33
    • 20644463474 scopus 로고    scopus 로고
    • Electrospray ionization mass spectrometry as a tool for determination of drug binding sites to human serum albumin by noncovalent interaction
    • 1:CAS:528:DC%2BD2MXls1Gls78%3D 10.1002/rcm.1967
    • Benkestock, K.; Edlund, P.O.; Roeraade, J.: Electrospray ionization mass spectrometry as a tool for determination of drug binding sites to human serum albumin by noncovalent interaction. Rapid Commun. Mass Spectrom. 19(12), 1637-1643 (2005)
    • (2005) Rapid Commun. Mass Spectrom. , vol.19 , Issue.12 , pp. 1637-1643
    • Benkestock, K.1    Edlund, P.O.2    Roeraade, J.3
  • 34
    • 84861233617 scopus 로고    scopus 로고
    • Molecular spectroscopic studies on the interaction of morin with bovine serum albumin
    • 1:CAS:528:DC%2BC38XntlOgtLw%3D 10.1016/j.jphotobiol.2012.04.001
    • Hu, Y.J.; Yue, H.L.; Li, X.L.; Zhang, S.S.; Tang, E.; Zhang, L.P.: Molecular spectroscopic studies on the interaction of morin with bovine serum albumin. J. Photochem. Photobiol B 112, 16 (2012)
    • (2012) J. Photochem. Photobiol B , vol.112 , pp. 16
    • Hu, Y.J.1    Yue, H.L.2    Li, X.L.3    Zhang, S.S.4    Tang, E.5    Zhang, L.P.6


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