메뉴 건너뛰기




Volumn 105, Issue 2, 2011, Pages 126-132

Studies on the interaction between docetaxel and human hemoglobin by spectroscopic analysis and molecular docking

Author keywords

Docetaxel; Human hemoglobin; Interaction; Molecular docking; Spectroscopy

Indexed keywords

DOCETAXEL; HEMOGLOBIN;

EID: 80053978827     PISSN: 10111344     EISSN: 18732682     Source Type: Journal    
DOI: 10.1016/j.jphotobiol.2011.07.004     Document Type: Article
Times cited : (47)

References (29)
  • 1
    • 28144445570 scopus 로고    scopus 로고
    • Docetaxel: A review of its use in metastatic breast cancer
    • DOI 10.2165/00003495-200565170-00007
    • K.A. Lyseng-Williamson, and C. Fenton Docetaxel: a review of its use in metastatic breast cancer Drugs 65 17 2005 2513 2531 (Pubitemid 41697318)
    • (2005) Drugs , vol.65 , Issue.17 , pp. 2513-2531
    • Lyseng-Williamson, K.A.1    Fenton, C.2
  • 2
    • 0033034008 scopus 로고    scopus 로고
    • Clinical pharmacokinetics of docetaxel
    • S.J. Clarke, and L.P. Rivory Clinical pharmacokinetics of docetaxel Clin. Pharmacokinet. 36 2 1999 99 114 (Pubitemid 29121684)
    • (1999) Clinical Pharmacokinetics , vol.36 , Issue.2 , pp. 99-114
    • Clarke, S.J.1    Rivory, L.P.2
  • 4
    • 6344250910 scopus 로고    scopus 로고
    • Interaction of oxaliplatin, cisplatin, and carboplatin with hemoglobin and the resulting release of a heme group
    • DOI 10.1021/tx049868j
    • R. Mandal, R. Kalke, and X.F. Li Interaction of oxaliplatin, cisplatin, and carboplatin with hemoglobin and the resulting release of a heme group Chem. Res. Toxicol. 17 2004 1391 1397 (Pubitemid 39391217)
    • (2004) Chemical Research in Toxicology , vol.17 , Issue.10 , pp. 1391-1397
    • Mandal, R.1    Kalke, R.2    Li, X.-F.3
  • 6
    • 62549138744 scopus 로고    scopus 로고
    • Study on the interaction of caffeine with bovine hemoglobin
    • Y.Q. Wang, H.M. Zhang, and Q.H. Zhou Study on the interaction of caffeine with bovine hemoglobin Eur. J. Med. Chem. 44 2009 2100 2105
    • (2009) Eur. J. Med. Chem. , vol.44 , pp. 2100-2105
    • Wang, Y.Q.1    Zhang, H.M.2    Zhou, Q.H.3
  • 7
    • 67349227114 scopus 로고    scopus 로고
    • Binding of mitomycin C to blood proteins: A spectroscopic analysis and molecular docking
    • J.C. Jang, H. Liu, W. Chen, and G.L. Zou Binding of mitomycin C to blood proteins: a spectroscopic analysis and molecular docking J. Mol. Struct. 928 2009 72 77
    • (2009) J. Mol. Struct. , vol.928 , pp. 72-77
    • Jang, J.C.1    Liu, H.2    Chen, W.3    Zou, G.L.4
  • 9
    • 33646701208 scopus 로고    scopus 로고
    • Interaction between silicotungstic heteropolyacid and bovine hemoglobin (BHb)
    • Y.Q. Wang, H.M. Zhang, and G.C. Zhang Interaction between silicotungstic heteropolyacid and bovine hemoglobin (BHb) Chin. J. Inorg. Chem. 22 2006 895 899
    • (2006) Chin. J. Inorg. Chem. , vol.22 , pp. 895-899
    • Wang, Y.Q.1    Zhang, H.M.2    Zhang, G.C.3
  • 10
    • 55249103413 scopus 로고    scopus 로고
    • Characteristics of the isomeric flavonoids apigenin and enistein binding to hemoglobin by spectroscopic methods
    • J.L. Yuan, H. Liu, X. Kang, Z. Lu, and G.L. Zou Characteristics of the isomeric flavonoids apigenin and enistein binding to hemoglobin by spectroscopic methods J. Mol. Struct. 891 2008 333 339
    • (2008) J. Mol. Struct. , vol.891 , pp. 333-339
    • Yuan, J.L.1    Liu, H.2    Kang, X.3    Lu, Z.4    Zou, G.L.5
  • 11
    • 0001943903 scopus 로고    scopus 로고
    • Fluorescence spectroscopy in peptide and protein analysis
    • R.A. Meyers, John Wiley Chichester
    • A.S. Ladokhin Fluorescence spectroscopy in peptide and protein analysis R.A. Meyers, Encyclopedia of Analytical Chemistry 2000 John Wiley Chichester 5762 5779
    • (2000) Encyclopedia of Analytical Chemistry , pp. 5762-5779
    • Ladokhin, A.S.1
  • 12
    • 0037009311 scopus 로고    scopus 로고
    • Interaction of drugs with bovine and human serum albumin
    • DOI 10.1016/S0022-2860(02)00256-9, PII S0022286002002569
    • A. Sulkowska Interaction of drugs with bovine and human serum albumin J. Mol. Struct. 614 2002 227 232 (Pubitemid 34987732)
    • (2002) Journal of Molecular Structure , vol.614 , Issue.1-3 , pp. 227-232
    • Sulkowska, A.1
  • 13
    • 0037123057 scopus 로고    scopus 로고
    • Interaction of ochratoxin a with human serum albumin. Preferential binding of the dianion and pH effects
    • DOI 10.1021/jp012314u
    • Y.V. Ilichev, J.L. Perry, and J.D. Simon Interaction of ochratoxin A with human serum albumin. Preferential binding of the dianion and pH effects J. Phys. Chem. B 106 2002 452 459 (Pubitemid 35281734)
    • (2002) Journal of Physical Chemistry B , vol.106 , Issue.2 , pp. 452-459
    • Il'ichev, Y.V.1    Perry, J.L.2    Simon, J.D.3
  • 14
    • 0036629604 scopus 로고    scopus 로고
    • Declining hemoglobin during chemoradiotherapy for locally advanced non-small cell lung cancer is significant
    • DOI 10.1016/S0167-8140(02)00151-2, PII S0167814002001512
    • Rob MacRae, Yu Shyr, David Johnson, and Hak Choy Declining hemoglobin during chemoradiotherapy for locally advanced non-small cell lung cancer is significant Radiother. Oncol. 64 2002 37 40 (Pubitemid 35229986)
    • (2002) Radiotherapy and Oncology , vol.64 , Issue.1 , pp. 37-40
    • MacRae, R.1    Shyr, Y.2    Johnson, D.3    Choy, H.4
  • 15
    • 0035857492 scopus 로고    scopus 로고
    • Lanthanide ions induce hydrolysis of hemoglobin-bound 2,3-diphosphoglycerate (2,3-DPG), conformational changes of globin and bidirectional changes of 2,3-DPG-hemoglobin's oxygen affinity
    • DOI 10.1016/S0925-4439(00)00100-9, PII S0925443900001009
    • Y. Cheng, H.K. Lin, D.P. Xue, R.Ch. Li, and K. Wang Lanthanide ions induce hydrolysis of hemoglobin-bound 2,3-diphosphoglycerate (2,3-DPG), conformational changes of globin and bidirectional changes of 2,3-DPG-hemoglobin's oxygen affinity Biochim. Biophys. Acta 1535 2001 200 216 (Pubitemid 32114143)
    • (2001) Biochimica et Biophysica Acta - Molecular Basis of Disease , vol.1535 , Issue.2 , pp. 200-216
    • Cheng, Y.1    Lin, H.2    Xue, D.3    Li, R.4    Wang, K.5
  • 16
    • 67650552908 scopus 로고    scopus 로고
    • Spectroscopic investigation of the interaction between riboflavin and bovine serum albumin
    • X.J. Guo, X.D. Sun, and S.K. Xu Spectroscopic investigation of the interaction between riboflavin and bovine serum albumin J. Mol. Struct. 931 2009 55 59
    • (2009) J. Mol. Struct. , vol.931 , pp. 55-59
    • Guo, X.J.1    Sun, X.D.2    Xu, S.K.3
  • 18
    • 33947451752 scopus 로고
    • Physical chemistry of protein solution. IV. The combination of human serum albumin with chloride ion
    • G. Scatchard, I.H. Scheiberg, and S.H. Armstorng Physical chemistry of protein solution. IV. The combination of human serum albumin with chloride ion J. Am. Chem. Soc. 72 1950 535 540
    • (1950) J. Am. Chem. Soc. , vol.72 , pp. 535-540
    • Scatchard, G.1    Scheiberg, I.H.2    Armstorng, S.H.3
  • 19
    • 0019889063 scopus 로고
    • Thermodynamics of protein association reactions: Forces contributing to stability
    • P.D. Ross, and S. Subramanian 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
  • 20
    • 61349128416 scopus 로고    scopus 로고
    • Molecular interaction between phosphomolybdate acid and bovine hemoglobin
    • H.M. Zhang, Y.Q. Wang, Q.H. Zhou, and G.L. Wang Molecular interaction between phosphomolybdate acid and bovine hemoglobin J. Mol. Struct. 921 2009 156 162
    • (2009) J. Mol. Struct. , vol.921 , pp. 156-162
    • Zhang, H.M.1    Wang, Y.Q.2    Zhou, Q.H.3    Wang, G.L.4
  • 21
    • 34347352255 scopus 로고    scopus 로고
    • Binding of the Environmental pollutant naphthol to bovine serum albumin
    • DOI 10.1021/bm061189v
    • T.Q. Wu, Q. Wu, S.Y. Guan, H.X. Su, and Z.J. Cai Binding of the environmental pollutant naphthol to bovine serum albumin Biomacromolecules 8 2007 1899 1906 (Pubitemid 47009969)
    • (2007) Biomacromolecules , vol.8 , Issue.6 , pp. 1899-1906
    • Wu, T.1    Wu, Q.2    Guan, S.3    Su, H.4    Cai, Z.5
  • 22
    • 34548177312 scopus 로고    scopus 로고
    • Transport of a cancer chemopreventive polyphenol, resveratrol: Interaction with serum albumin and hemoglobin
    • DOI 10.1007/s10895-007-0220-2
    • Z. Lu, Y.Y. Zhang, H. Liu, and J.L. Yuan Transport of a cancer chemopreventive polyphenol, resveratrol: interaction with serum albumin and hemoglobin J. Fluoresc. 17 2007 580 587 (Pubitemid 47310330)
    • (2007) Journal of Fluorescence , vol.17 , Issue.5 , pp. 580-587
    • Lu, Z.1    Zhang, Y.2    Liu, H.3    Yuan, J.4    Zheng, Z.5    Zou, G.6
  • 23
    • 0031861753 scopus 로고    scopus 로고
    • Characterization of the structural and functional changes of hemoglobin in dimethyl sulfoxide by spectroscopic techniques
    • C.W. Liu, A.L. Bo, G.J. Cheng, X.Q. Lin, and S.J. Dong Characterization of the structural and functional changes of hemoglobin in dimethyl sulfoxide by spectroscopic techniques Biochim. Biophys. Acta. 1385 1998 53 60
    • (1998) Biochim. Biophys. Acta. , vol.1385 , pp. 53-60
    • Liu, C.W.1    Bo, A.L.2    Cheng, G.J.3    Lin, X.Q.4    Dong, S.J.5
  • 24
    • 0033751174 scopus 로고    scopus 로고
    • Changes of tyrosine and tryptophan residues in human hemoglobin by oxygen binding: Near- and far-UV circular dichroism of isolated chains and recombined hemoglobin
    • R. Li, Y. Nagai, and M. Nagai Changes of tyrosine and tryptophan residues in human hemoglobin by oxygen binding: near- and far-UV circular dichroism of isolated chains and recombined hemoglobin J. Inorg. Biochem. 82 2000 93 101
    • (2000) J. Inorg. Biochem. , vol.82 , pp. 93-101
    • Li, R.1    Nagai, Y.2    Nagai, M.3
  • 26
    • 0030271385 scopus 로고    scopus 로고
    • Secondary structure determination of proteins in aqueous solution by infrared spectroscopy: A comparison of multivariate data analysis methods
    • DOI 10.1006/abio.1996.0369
    • K. Rahmelow, and W. Hubner Secondary structure determination of protein aqueous solution by infrared spectroscopy: a comparison of multivariate data analysis methods Anal. Biochem. 241 1996 5 13 (Pubitemid 26337205)
    • (1996) Analytical Biochemistry , vol.241 , Issue.1 , pp. 5-13
    • Rahmelow, K.1    Hubner, W.2
  • 27
    • 0025357111 scopus 로고
    • Protein secondary structures in water from second-derivative amide I infrared spectra
    • A.C. Dong, P. Huang, and W.S. Caughey Protein secondary structures in water from second derivative amide I infrared spectra Biochemistry 29 1990 3303 3308 (Pubitemid 20131472)
    • (1990) Biochemistry , vol.29 , Issue.13 , pp. 3303-3308
    • Dong, A.1    Huang, P.2    Caughey, W.S.3
  • 29
    • 39749177161 scopus 로고    scopus 로고
    • Investigation of the interaction between naringin and human serum albumin
    • DOI 10.1016/j.molstruc.2007.03.063, PII S0022286007002992
    • Y.H. Zhang, Y. Li, L.J. Dong, J. Li, W.Y. He, X.G. Chen, and Z.D. Hu Investigation of the interaction between naringin and human serum albumin J. Mol. Struct. 875 2008 1 8 (Pubitemid 351305213)
    • (2008) Journal of Molecular Structure , vol.875 , Issue.1-3 , pp. 1-8
    • Zhang, Y.1    Li, Y.2    Dong, L.3    Li, J.4    He, W.5    Chen, X.6    Hu, Z.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.