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Volumn 64, Issue 6, 2012, Pages 792-801

Enantioselective drug-protein interaction between mexiletine and plasma protein

Author keywords

1 acid glycoprotein; enantioselectivity; human serum albumin; mexiletine; molecular dynamics

Indexed keywords

ARGININE; LEUCINE; MEXILETINE; OROSOMUCOID; PHENYLALANINE; SERINE; SERUM ALBUMIN;

EID: 84862826304     PISSN: 00223573     EISSN: 20427158     Source Type: Journal    
DOI: 10.1111/j.2042-7158.2012.01487.x     Document Type: Article
Times cited : (10)

References (37)
  • 1
    • 0025783759 scopus 로고
    • Resolution and electrophysiological effects of mexiletine enantiomers
    • Turgeon J, et al,. Resolution and electrophysiological effects of mexiletine enantiomers. J Pharm Pharmacol 1991; 43: 630-635.
    • (1991) J Pharm Pharmacol , vol.43 , pp. 630-635
    • Turgeon, J.1
  • 2
    • 0028844521 scopus 로고
    • Stereoselective effects of mexiletine enantiomers on sodium currents and excitability characteristics of adult skeletal muscle fibers
    • De Luca A, et al,. Stereoselective effects of mexiletine enantiomers on sodium currents and excitability characteristics of adult skeletal muscle fibers. Naunyn Schmiedebergs Arch Pharmacol 1995; 352: 653-661.
    • (1995) Naunyn Schmiedebergs Arch Pharmacol , vol.352 , pp. 653-661
    • De Luca, A.1
  • 3
    • 0024405787 scopus 로고
    • The pharmacokinetics of the enantiomers of mexiletine in humans
    • Igwemezie L, et al,. The pharmacokinetics of the enantiomers of mexiletine in humans. Xenobiotica 1989; 19: 677-682. (Pubitemid 19147786)
    • (1989) Xenobiotica , vol.19 , Issue.6 , pp. 677-682
    • Igwemezie, L.1    Kerr, C.R.2    McErlane, K.M.3
  • 5
    • 0028789288 scopus 로고
    • Pharmacokinetics of mexiletine enantiomers in healthy human subjects. A study of the in vivo serum protein binding, salivary excretion and red blood cell distribution of the enantiomers
    • Kwok DW, et al,. Pharmacokinetics of mexiletine enantiomers in healthy human subjects. A study of the in vivo serum protein binding, salivary excretion and red blood cell distribution of the enantiomers. Xenobitica 1995; 25: 1127-1142.
    • (1995) Xenobitica , vol.25 , pp. 1127-1142
    • Kwok, D.W.1
  • 7
    • 0032894348 scopus 로고    scopus 로고
    • Enantioselective analysis of N-hydroxymexiletine glucuronide in human plasma for pharmacokinetic studies
    • DOI 10.1002/(SICI)1520-636X(1999)11:2<85::AID-CHIR1>3.0.CO;2-P
    • Lanchote VL, et al,. Enantioselective analysis of N-hydroxymexiletine glucuronide in human plasma for pharmacokinetic studies. Chirality 1999; 11: 85-90. (Pubitemid 29053042)
    • (1999) Chirality , vol.11 , Issue.2 , pp. 85-90
    • Lanchote, V.L.1    Santos, V.J.2    Cesarino, E.J.3    Dreossi, S.A.C.4    Mere Jr., Y.5    Santos, S.R.C.J.6
  • 8
    • 34447538480 scopus 로고    scopus 로고
    • Determination of mexiletine enantiomers in human serum albumin after derivatization with GITC by RP-HPLC
    • Jin YX, Zeng S,. Determination of mexiletine enantiomers in human serum albumin after derivatization with GITC by RP-HPLC. Chin Pharm J 2007; 42: 860-862. (Pubitemid 47066213)
    • (2007) Chinese Pharmaceutical Journal , vol.42 , Issue.11 , pp. 860-862
    • Jin, Y.-X.1    Zeng, S.2
  • 9
    • 55349100930 scopus 로고    scopus 로고
    • Alpha7 nicotinic acetylcholine receptor agonists: Prediction of their binding affinity through a Molecular Mechanics Poisson-Boltzmann Surface Area approach
    • Grazioso G, et al,. Alpha7 nicotinic acetylcholine receptor agonists: prediction of their binding affinity through a Molecular Mechanics Poisson-Boltzmann Surface Area approach. J Comput Chem 2008; 29: 2593-2603.
    • (2008) J Comput Chem , vol.29 , pp. 2593-2603
    • Grazioso, G.1
  • 10
    • 77957845983 scopus 로고    scopus 로고
    • Binding modes of flavones to human serum albumin: Insights from experimental and computational studies
    • Liu W, et al,. Binding modes of flavones to human serum albumin: insights from experimental and computational studies. J Phys Chem B 2010; 114: 12938-12947.
    • (2010) J Phys Chem B , vol.114 , pp. 12938-12947
    • Liu, W.1
  • 11
    • 67650035452 scopus 로고    scopus 로고
    • Molecular insights into 14-membered macrolides using the MM-PBSA method
    • Yam WK, Wahab HA,. Molecular insights into 14-membered macrolides using the MM-PBSA method. J Chem Inf Model 2009; 49: 1558-1567.
    • (2009) J Chem Inf Model , vol.49 , pp. 1558-1567
    • Yam, W.K.1    Wahab, H.A.2
  • 13
    • 70349932423 scopus 로고    scopus 로고
    • AutoDock4 and AutoDockTools4: Automated docking with selective receptor flexibility
    • Morris GM, et al,. AutoDock4 and AutoDockTools4: automated docking with selective receptor flexibility. J Comput Chem 2009; 30: 2785-2791.
    • (2009) J Comput Chem , vol.30 , pp. 2785-2791
    • Morris, G.M.1
  • 14
    • 0038626673 scopus 로고    scopus 로고
    • Wallingford, CT: Gaussian, Inc
    • Frisch MJ, et al,. Gaussian 03. Wallingford, CT: Gaussian, Inc, 2004.
    • (2004) Gaussian 03
    • Frisch, M.J.1
  • 15
    • 54949158207 scopus 로고    scopus 로고
    • The 1.8-A crystal structure of alpha1-acid glycoprotein (Orosomucoid) solved by UV RIP reveals the broad drug-binding activity of this human plasma lipocalin
    • Schönfeld DL, et al,. The 1.8-A crystal structure of alpha1-acid glycoprotein (Orosomucoid) solved by UV RIP reveals the broad drug-binding activity of this human plasma lipocalin. J Mol Biol 2008; 384: 393-405.
    • (2008) J Mol Biol , vol.384 , pp. 393-405
    • Schönfeld, D.L.1
  • 16
    • 11644261806 scopus 로고    scopus 로고
    • Automated docking using a Lamarckian Genetic Algorithm and an empirical binding free energy function
    • Morris MG, et al,. Automated docking using a Lamarckian Genetic Algorithm and an empirical binding free energy function. J Comput Chem 1998; 19: 1639-1662.
    • (1998) J Comput Chem , vol.19 , pp. 1639-1662
    • Morris, M.G.1
  • 17
    • 58049201323 scopus 로고    scopus 로고
    • San Francisco, CA: University of California
    • Case DA, et al,. Amber 10. San Francisco, CA: University of California, 2008.
    • (2008) Amber 10
    • Case, D.A.1
  • 18
    • 0242663237 scopus 로고    scopus 로고
    • A point-charge force field for molecular mechanics simulations of proteins based on condensed-phase quantum mechanical calculations
    • Duan Y, et al,. A point-charge force field for molecular mechanics simulations of proteins based on condensed-phase quantum mechanical calculations. J Comput Chem 2003; 24: 1999-2012.
    • (2003) J Comput Chem , vol.24 , pp. 1999-2012
    • Duan, Y.1
  • 19
    • 2942532422 scopus 로고    scopus 로고
    • Development and testing of a general amber force field
    • Wang J, et al,. Development and testing of a general amber force field. J Comput Chem 2004; 25: 1157-1174.
    • (2004) J Comput Chem , vol.25 , pp. 1157-1174
    • Wang, J.1
  • 20
    • 84988087911 scopus 로고
    • Calculating the electrostatic potential of molecules in solution
    • Gilson MK, et al,. Calculating the electrostatic potential of molecules in solution. J Comput Chem 1988; 9: 327-335.
    • (1988) J Comput Chem , vol.9 , pp. 327-335
    • Gilson, M.K.1
  • 21
    • 3242886771 scopus 로고    scopus 로고
    • PDB2PQR: An automated pipeline for the setup, execution, and analysis of Poisson-Boltzmann electrostatics calculations
    • Dolinsky TJ, et al,. PDB2PQR: an automated pipeline for the setup, execution, and analysis of Poisson-Boltzmann electrostatics calculations. Nucleic Acids Res 2004; 32: 665-667.
    • (2004) Nucleic Acids Res , vol.32 , pp. 665-667
    • Dolinsky, T.J.1
  • 22
    • 0004016501 scopus 로고
    • Comparison of simple potential functions for simulating liquid water
    • Jorgensen WL, et al,. Comparison of simple potential functions for simulating liquid water. J Chem Phys 1983; 79: 926-935.
    • (1983) J Chem Phys , vol.79 , pp. 926-935
    • Jorgensen, W.L.1
  • 23
    • 33646940952 scopus 로고
    • Numerical integration of the cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes
    • Rychaert JP, et al,. Numerical integration of the cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes. J Comput Phys 1977; 23: 327-341.
    • (1977) J Comput Phys , vol.23 , pp. 327-341
    • Rychaert, J.P.1
  • 25
    • 1842479952 scopus 로고    scopus 로고
    • Exploring Protein Native States and Large-Scale Conformational Changes with a Modified Generalized Born Model
    • DOI 10.1002/prot.20033
    • Onufriev A, et al,. Exploring protein native states and large-scale conformational changes with a modified generalized born model. Proteins 2004; 55: 383-394. (Pubitemid 38437495)
    • (2004) Proteins: Structure, Function and Genetics , vol.55 , Issue.2 , pp. 383-394
    • Onufriev, A.1    Bashford, D.2    Case, D.A.3
  • 26
    • 0000408363 scopus 로고    scopus 로고
    • Approximate atomic surfaces from linear combinations of pairwise overlaps (LCPO)
    • Weiser J, et al,. Approximate atomic surfaces from linear combinations of pairwise overlaps (LCPO). J Comput Chem 1999; 20: 217-230. (Pubitemid 129653030)
    • (1999) Journal of Computational Chemistry , vol.20 , Issue.2 , pp. 217-230
    • Weiser, J.1    Shenkin, P.S.2    Still, W.C.3
  • 27
    • 33748637571 scopus 로고    scopus 로고
    • Recent advances in free energy calculations with a combination of molecular mechanics and continuum models
    • DOI 10.2174/157340906778226454
    • Wang JM, et al,. Recent advances in free energy calculations with a combination of molecular mechanics and continuum models. Curr Comput Aided Drug Des 2006; 2: 287-306. (Pubitemid 44383230)
    • (2006) Current Computer-Aided Drug Design , vol.2 , Issue.3 , pp. 287-306
    • Wang, J.M.1    Hou, T.2    Xu, X.3
  • 28
    • 0035847290 scopus 로고    scopus 로고
    • Chromatographic and electrophoretic studies of protein binding to chiral solutes
    • Hage DS,. Chromatographic and electrophoretic studies of protein binding to chiral solutes. J Chromatogr A 2001; 906: 459-481.
    • (2001) J Chromatogr A , vol.906 , pp. 459-481
    • Hage, D.S.1
  • 29
    • 0023717477 scopus 로고
    • Isoelectric focusing of alpha-1 acid glycoprotein (orosomucoid) in immobilized pH-gradients with 8 M urea: Detection of its desialylated variants using an alkaline phosphatase-linked secondary antibody system
    • DOI 10.1002/elps.1150091005
    • Eap CB, Baumann P,. Isoelectric focusing of alpha-1-acid glycoprotein (orosomucoid) in immobilized pH gradients with 8 M urea: detection of its desialylated variants using an alkaline phosphatase-linked secondary antibody system. Electrophoresis 1988; 9: 650-654. (Pubitemid 18259874)
    • (1988) Electrophoresis , vol.9 , Issue.10 , pp. 650-654
    • Eap, C.B.1    Baumann, P.2
  • 30
    • 0642274950 scopus 로고    scopus 로고
    • 1-acid glycoprotein using capillary electrophoresis
    • Kuroda Y, et al,. Drug binding analysis of human a1-acid glycoprotein using capillary electrophoresis. Yakugaku Zasshi 2003; 123: 781-788. [in Japanese]. (Pubitemid 41327449)
    • (2003) Yakugaku Zasshi , vol.123 , Issue.9 , pp. 781-788
    • Kuroda, Y.1    Shibukawa, A.2    Nakagawa, T.3
  • 33
    • 70349557614 scopus 로고    scopus 로고
    • Enantioselective plasma protein binding of propafenone: Mechanism, drug interaction, and species difference
    • Hong YJ, et al,. Enantioselective plasma protein binding of propafenone: mechanism, drug interaction, and species difference. Chirality 2009; 21: 692-698.
    • (2009) Chirality , vol.21 , pp. 692-698
    • Hong, Y.J.1
  • 34
    • 0031901772 scopus 로고    scopus 로고
    • Species differences of serum albumins: III. Analysis of structural characteristics and ligand binding properties during N-B transitions
    • DOI 10.1023/A:1011986028529
    • Kosa T, et al,. Species differences of serum albumins: Analysis of structural characteristics and ligand binding properties during N-B transitions. Pharm Res 1998; 15: 592-598. (Pubitemid 28214953)
    • (1998) Pharmaceutical Research , vol.15 , Issue.4 , pp. 592-598
    • Kosa, T.1    Maruyama, T.2    Sakai, N.3    Yonemura, N.4    Yahara, S.5    Otagiri, M.6
  • 35
    • 0035659618 scopus 로고    scopus 로고
    • In vitro and in vivo properties of recombinant human serum albumin from pichia pastoris purified by a method of short processing time
    • DOI 10.1023/A:1013391001141
    • Watanabe H, et al,. In vitro and in vivo properties of recombinant human serum albumin from pichia pastoris purified by a method of short processing time. Pharm Res 2001; 18: 1775-1781. (Pubitemid 34020436)
    • (2001) Pharmaceutical Research , vol.18 , Issue.12 , pp. 1775-1781
    • Watanabe, H.1    Yamasaki, K.2    Kragh-Hansen, U.3    Tanase, S.4    Harada, K.5    Suenaga, A.6    Otagiri, M.7


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