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Volumn 345, Issue 2, 2005, Pages 214-226

A surface plasmon resonance-based assay for small molecule inhibitors of human cyclophilin A

Author keywords

Competition binding assay; Cyclophilin A; Cyclosporin A; Surface plasmon resonance

Indexed keywords

AMINES; DISSOCIATION; MOLECULES; PLASMONS; RATE CONSTANTS; RESONANCE;

EID: 25444507171     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2005.06.037     Document Type: Article
Times cited : (62)

References (47)
  • 1
    • 0034581194 scopus 로고    scopus 로고
    • Kinetic, equilibrium, and thermodynamic analysis of macromolecular interactions with Biacore
    • D.G. Myszka Kinetic, equilibrium, and thermodynamic analysis of macromolecular interactions with Biacore Methods Enzymol. 323 2000 325 340
    • (2000) Methods Enzymol. , vol.323 , pp. 325-340
    • Myszka, D.G.1
  • 2
    • 0035478125 scopus 로고    scopus 로고
    • Surface plasmon resonance: Towards an understanding of the mechanisms of biological molecular recognition
    • J.M. McDonnell Surface plasmon resonance: towards an understanding of the mechanisms of biological molecular recognition Curr. Opin. Chem. Biol. 5 2001 572 577
    • (2001) Curr. Opin. Chem. Biol. , vol.5 , pp. 572-577
    • McDonnell, J.M.1
  • 3
    • 0035231629 scopus 로고    scopus 로고
    • Surface plasmon resonance applied to DNA-protein complexes
    • M. Buckle Surface plasmon resonance applied to DNA-protein complexes Methods Mol. Biol. 148 2001 535 546
    • (2001) Methods Mol. Biol. , vol.148 , pp. 535-546
    • Buckle, M.1
  • 4
    • 0842331880 scopus 로고    scopus 로고
    • A survey of the year 2002 commercial optical biosensor literature
    • R.L. Rich, and D.G. Myszka A survey of the year 2002 commercial optical biosensor literature J. Mol. Recognit. 16 2003 351 382
    • (2003) J. Mol. Recognit. , vol.16 , pp. 351-382
    • Rich, R.L.1    Myszka, D.G.2
  • 5
    • 0034282271 scopus 로고    scopus 로고
    • Implementing surface plasmon resonance biosensors in drug discovery
    • D.G. Myszka, and R.L. Rich Implementing surface plasmon resonance biosensors in drug discovery Pharm. Sci. Technol. Today 3 2000 310 317
    • (2000) Pharm. Sci. Technol. Today , vol.3 , pp. 310-317
    • Myszka, D.G.1    Rich, R.L.2
  • 6
    • 0036853993 scopus 로고    scopus 로고
    • Surface plasmon resonance characterization of drug/liposome interactions
    • C.L. Baird, E.S. Courtenay, and D.G. Myszka Surface plasmon resonance characterization of drug/liposome interactions Anal. Biochem. 310 2002 93 99
    • (2002) Anal. Biochem. , vol.310 , pp. 93-99
    • Baird, C.L.1    Courtenay, E.S.2    Myszka, D.G.3
  • 7
    • 2142767300 scopus 로고    scopus 로고
    • Probing the mechanism of drug/lipid membrane interactions using Biacore
    • Y.N. Abdiche, and D.G. Myszka Probing the mechanism of drug/lipid membrane interactions using Biacore Anal. Biochem. 328 2004 233 243
    • (2004) Anal. Biochem. , vol.328 , pp. 233-243
    • Abdiche, Y.N.1    Myszka, D.G.2
  • 8
    • 2542474493 scopus 로고    scopus 로고
    • Analysis of small-molecule interactions using Biacore S51 technology
    • D.G. Myszka Analysis of small-molecule interactions using Biacore S51 technology Anal. Biochem. 329 2004 316 323
    • (2004) Anal. Biochem. , vol.329 , pp. 316-323
    • Myszka, D.G.1
  • 9
  • 10
    • 4644324195 scopus 로고    scopus 로고
    • Optimizing the hit-to-lead process using SPR analysis
    • S. Lofas Optimizing the hit-to-lead process using SPR analysis Assay Drug Dev. Technol. 2 2004 407 415
    • (2004) Assay Drug Dev. Technol. , vol.2 , pp. 407-415
    • Lofas, S.1
  • 11
    • 4043100606 scopus 로고    scopus 로고
    • Integration of surface plasmon resonance with mass spectrometry: Automated ligand fishing and sample preparation for MALDI MS using a Biacore 3000 biosensor
    • A. Zhukov, M. Schurenberg, O. Jansson, D. Areskoug, and J. Buijs Integration of surface plasmon resonance with mass spectrometry: automated ligand fishing and sample preparation for MALDI MS using a Biacore 3000 biosensor J. Biomol. Tech. 15 2004 112 119
    • (2004) J. Biomol. Tech. , vol.15 , pp. 112-119
    • Zhukov, A.1    Schurenberg, M.2    Jansson, O.3    Areskoug, D.4    Buijs, J.5
  • 13
    • 0141707715 scopus 로고    scopus 로고
    • Peptidylprolyl cis/trans isomerases (immunophilins): Biological diversity-targets-functions
    • A. Galat Peptidylprolyl cis/trans isomerases (immunophilins): biological diversity-targets-functions Curr. Top. Med. Chem. 3 2003 1315 1347
    • (2003) Curr. Top. Med. Chem. , vol.3 , pp. 1315-1347
    • Galat, A.1
  • 16
    • 0141595904 scopus 로고    scopus 로고
    • Structures of immunophilins and their ligand complexes
    • J. Dornan, P. Taylor, and M.D. Walkinshaw Structures of immunophilins and their ligand complexes Curr. Top. Med. Chem. 3 2003 1392 1409
    • (2003) Curr. Top. Med. Chem. , vol.3 , pp. 1392-1409
    • Dornan, J.1    Taylor, P.2    Walkinshaw, M.D.3
  • 18
    • 0034129915 scopus 로고    scopus 로고
    • The impact of immunosuppressive drugs on the analysis of T cell activation
    • P. Rovira, L. Mascarell, and P. Truffa-Bachi The impact of immunosuppressive drugs on the analysis of T cell activation Curr. Med. Chem. 7 2000 673 692
    • (2000) Curr. Med. Chem. , vol.7 , pp. 673-692
    • Rovira, P.1    Mascarell, L.2    Truffa-Bachi, P.3
  • 19
    • 0028884932 scopus 로고
    • Cyclosporin analogs modified in the 3,7,8-positions: Substituent effects on peptidylprolyl isomerase inhibition and immunosuppressive activity are nonadditive
    • M.K. Hu, A. Badger, and D.H. Rich Cyclosporin analogs modified in the 3,7,8-positions: substituent effects on peptidylprolyl isomerase inhibition and immunosuppressive activity are nonadditive J. Med. Chem. 38 1995 4164 4170
    • (1995) J. Med. Chem. , vol.38 , pp. 4164-4170
    • Hu, M.K.1    Badger, A.2    Rich, D.H.3
  • 20
    • 0032561136 scopus 로고    scopus 로고
    • X-ray structures and analysis of 11 cyclosporin derivatives complexed with cyclophilin a
    • J. Kallen, V. Mikol, P. Taylor, and M.D. Walkinshaw X-ray structures and analysis of 11 cyclosporin derivatives complexed with cyclophilin A J. Mol. Biol. 283 1998 435 449
    • (1998) J. Mol. Biol. , vol.283 , pp. 435-449
    • Kallen, J.1    Mikol, V.2    Taylor, P.3    Walkinshaw, M.D.4
  • 21
    • 10744221220 scopus 로고    scopus 로고
    • Synthesis of non-immunosuppressive cyclophilin-binding cyclosporin a derivatives as potential anti-HIV-1 drugs
    • M. Evers, J.C. Barriere, G. Bashiardes, A. Bousseau, J.C. Carry, and N. Dereu Synthesis of non-immunosuppressive cyclophilin-binding cyclosporin A derivatives as potential anti-HIV-1 drugs Bioorg. Med. Chem. Lett. 13 2003 4415 4419
    • (2003) Bioorg. Med. Chem. Lett. , vol.13 , pp. 4415-4419
    • Evers, M.1    Barriere, J.C.2    Bashiardes, G.3    Bousseau, A.4    Carry, J.C.5    Dereu, N.6
  • 22
    • 3843110265 scopus 로고    scopus 로고
    • Synthesis and neurotrophic activity of nonimmunosuppressant cyclosporin a derivatives
    • L. Wei, J.P. Steiner, G.S. Hamilton, and Y.Q. Wu Synthesis and neurotrophic activity of nonimmunosuppressant cyclosporin A derivatives Bioorg. Med. Chem. Lett. 14 2004 4549 4551
    • (2004) Bioorg. Med. Chem. Lett. , vol.14 , pp. 4549-4551
    • Wei, L.1    Steiner, J.P.2    Hamilton, G.S.3    Wu, Y.Q.4
  • 23
    • 1642494718 scopus 로고    scopus 로고
    • Substitution in position 3 of cyclosporin a abolishes the cyclophilin-mediated gain-of-function mechanism but not immunosuppression
    • R. Baumgrass, Y. Zhang, F. Erdmann, A. Thiel, M. Weiwad, A. Radbruch, and G. Fischer Substitution in position 3 of cyclosporin A abolishes the cyclophilin-mediated gain-of-function mechanism but not immunosuppression J. Biol. Chem. 279 2004 2470 2479
    • (2004) J. Biol. Chem. , vol.279 , pp. 2470-2479
    • Baumgrass, R.1    Zhang, Y.2    Erdmann, F.3    Thiel, A.4    Weiwad, M.5    Radbruch, A.6    Fischer, G.7
  • 24
    • 8544277247 scopus 로고    scopus 로고
    • In vitro anti-parasitic activity of cyclosporin a analogs on Trypanosoma cruzi
    • J. Bua, A.M. Ruiz, M. Potenza, and L.E. Fichera In vitro anti-parasitic activity of cyclosporin A analogs on Trypanosoma cruzi Bioorg. Med. Chem. Lett. 14 2004 4633 4637
    • (2004) Bioorg. Med. Chem. Lett. , vol.14 , pp. 4633-4637
    • Bua, J.1    Ruiz, A.M.2    Potenza, M.3    Fichera, L.E.4
  • 25
    • 14244258607 scopus 로고    scopus 로고
    • Unexpected side chain effects at residue 8 of cyclosporin a derivatives allow photoswitching of immunosuppression
    • Y. Zhang, F. Erdmann, R. Baumgrass, M. Schutkowski, and G. Fischer Unexpected side chain effects at residue 8 of cyclosporin A derivatives allow photoswitching of immunosuppression J. Biol. Chem. 280 2005 4842 4850
    • (2005) J. Biol. Chem. , vol.280 , pp. 4842-4850
    • Zhang, Y.1    Erdmann, F.2    Baumgrass, R.3    Schutkowski, M.4    Fischer, G.5
  • 27
    • 10744229880 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of non-peptidic cyclophilin ligands
    • Y.Q. Wu, S. Belyakov, C. Choi, D. Limburg, I.B. Thomas, and M. Vaal Synthesis and biological evaluation of non-peptidic cyclophilin ligands J. Med. Chem. 46 2003 1112 1115
    • (2003) J. Med. Chem. , vol.46 , pp. 1112-1115
    • Wu, Y.Q.1    Belyakov, S.2    Choi, C.3    Limburg, D.4    Thomas, I.B.5    Vaal, M.6
  • 29
    • 0036740693 scopus 로고    scopus 로고
    • The chaperone activity of protein disulfide isomerase is affected by cyclophilin B and cyclosporin a in vitro
    • T. Horibe, C. Yosho, S. Okada, M. Tsukamoto, H. Nagai, and Y. Hagiwara The chaperone activity of protein disulfide isomerase is affected by cyclophilin B and cyclosporin A in vitro J. Biochem. (Tokyo) 132 2002 401 407
    • (2002) J. Biochem. (Tokyo) , vol.132 , pp. 401-407
    • Horibe, T.1    Yosho, C.2    Okada, S.3    Tsukamoto, M.4    Nagai, H.5    Hagiwara, Y.6
  • 30
    • 4344612246 scopus 로고    scopus 로고
    • Nucleocapsid protein of SARS coronavirus tightly binds to human cyclophilin a
    • C. Luo, H. Luo, S. Zheng, C. Gui, L. Yue, and C. Yu Nucleocapsid protein of SARS coronavirus tightly binds to human cyclophilin A Biochem. Biophys. Res. Commun. 321 2004 557 565
    • (2004) Biochem. Biophys. Res. Commun. , vol.321 , pp. 557-565
    • Luo, C.1    Luo, H.2    Zheng, S.3    Gui, C.4    Yue, L.5    Yu, C.6
  • 31
    • 7444270321 scopus 로고    scopus 로고
    • Enzymatic and structural characterization of non-peptide ligand-cyclophilin complexes
    • G. Kontopidis, P. Taylor, and M.D. Walkinshaw Enzymatic and structural characterization of non-peptide ligand-cyclophilin complexes Acta Crystallogr. D Biol. Crystallogr. 60 2004 479 485
    • (2004) Acta Crystallogr. D Biol. Crystallogr. , vol.60 , pp. 479-485
    • Kontopidis, G.1    Taylor, P.2    Walkinshaw, M.D.3
  • 32
    • 4644340688 scopus 로고    scopus 로고
    • SPR-based interaction studies with small molecular weight ligands using hAGT fusion proteins
    • W. Huber, S. Perspicace, J. Kohler, F. Muller, and D. Schlatter SPR-based interaction studies with small molecular weight ligands using hAGT fusion proteins Anal. Biochem. 333 2004 280 288
    • (2004) Anal. Biochem. , vol.333 , pp. 280-288
    • Huber, W.1    Perspicace, S.2    Kohler, J.3    Muller, F.4    Schlatter, D.5
  • 33
    • 0025858482 scopus 로고
    • Structure of human cyclophilin and its binding site for cyclosporin a determined by X-ray crystallography and NMR spectroscopy
    • J. Kallen, C. Spitzfaden, M.G. Zurini, G. Wider, H. Widmer, K. Wuthrich, and M.D. Walkinshaw Structure of human cyclophilin and its binding site for cyclosporin A determined by X-ray crystallography and NMR spectroscopy Nature 353 1991 276 279
    • (1991) Nature , vol.353 , pp. 276-279
    • Kallen, J.1    Spitzfaden, C.2    Zurini, M.G.3    Wider, G.4    Widmer, H.5    Wuthrich, K.6    Walkinshaw, M.D.7
  • 34
    • 0033151950 scopus 로고    scopus 로고
    • Tryptophan microstate reshuffling upon the binding of cyclosporin a to human cyclophilin a
    • M. Gastmans, G. Volckaert, and Y. Engelborghs Tryptophan microstate reshuffling upon the binding of cyclosporin A to human cyclophilin A Proteins 35 1999 464 474
    • (1999) Proteins , vol.35 , pp. 464-474
    • Gastmans, M.1    Volckaert, G.2    Engelborghs, Y.3
  • 35
    • 0025944815 scopus 로고
    • Immobilization of proteins to a carboxymethyldextran-modified gold surface for biospecific interaction analysis in surface plasmon resonance sensors
    • B. Johnsson, S. Lofas, and G. Lindquist Immobilization of proteins to a carboxymethyldextran-modified gold surface for biospecific interaction analysis in surface plasmon resonance sensors Anal. Biochem. 198 1991 268 277
    • (1991) Anal. Biochem. , vol.198 , pp. 268-277
    • Johnsson, B.1    Lofas, S.2    Lindquist, G.3
  • 36
    • 0037438354 scopus 로고    scopus 로고
    • Thermodynamic characterization of the interaction of human cyclophilin 18 with cyclosporin a
    • J. Fanghänel, and G. Fischer Thermodynamic characterization of the interaction of human cyclophilin 18 with cyclosporin A Biophys. Chem. 100 2003 351 366
    • (2003) Biophys. Chem. , vol.100 , pp. 351-366
    • Fanghänel, J.1    Fischer, G.2
  • 39
    • 0027280841 scopus 로고
    • Interaction of cyclosporin a with an Fab fragment or cyclophilin: Affinity measurements and time-dependent changes in binding
    • G. Zeder-Lutz, R. Wenger, M.H. Van Regenmortel, and D. Altschuh Interaction of cyclosporin A with an Fab fragment or cyclophilin: affinity measurements and time-dependent changes in binding FEBS Lett. 326 1993 153 157
    • (1993) FEBS Lett. , vol.326 , pp. 153-157
    • Zeder-Lutz, G.1    Wenger, R.2    Van Regenmortel, M.H.3    Altschuh, D.4
  • 40
    • 0028020074 scopus 로고
    • Interaction of cyclosporin a and two cyclosporin analogs with cyclophilin: Relationship between structure and binding
    • G. Zeder-Lutz, M.H. Van Regenmortel, R. Wenger, and D. Altschuh Interaction of cyclosporin A and two cyclosporin analogs with cyclophilin: relationship between structure and binding J. Chromatogr. B Biomed. Appl. 662 1994 301 306
    • (1994) J. Chromatogr. B Biomed. Appl. , vol.662 , pp. 301-306
    • Zeder-Lutz, G.1    Van Regenmortel, M.H.2    Wenger, R.3    Altschuh, D.4
  • 41
    • 0029018580 scopus 로고
    • Analysis of cyclosporin interactions with antibodies and cyclophilin using the BIAcore
    • G. Zeder-Lutz, N. Rauffer, D. Altschuh, and M.H. Van Regenmortel Analysis of cyclosporin interactions with antibodies and cyclophilin using the BIAcore J. Immunol. Methods 183 1995 131 140
    • (1995) J. Immunol. Methods , vol.183 , pp. 131-140
    • Zeder-Lutz, G.1    Rauffer, N.2    Altschuh, D.3    Van Regenmortel, M.H.4
  • 42
    • 0242321993 scopus 로고    scopus 로고
    • Cyclophilin a interacts with HIV-1 Vpr and is required for its functional expression
    • K. Zander, M.P. Sherman, U. Tessmer, K. Bruns, V. Wray, and A.T. Prechtel Cyclophilin A interacts with HIV-1 Vpr and is required for its functional expression J. Biol. Chem. 278 2003 43202 43213
    • (2003) J. Biol. Chem. , vol.278 , pp. 43202-43213
    • Zander, K.1    Sherman, M.P.2    Tessmer, U.3    Bruns, K.4    Wray, V.5    Prechtel, A.T.6
  • 43
    • 0025325366 scopus 로고
    • Peptidyl-prolyl cis-trans-isomerase from Escherichia coli: A periplasmic homolog of cyclophilin that is not inhibited by cyclosporin a
    • J. Liu, and C.T. Walsh Peptidyl-prolyl cis-trans-isomerase from Escherichia coli: a periplasmic homolog of cyclophilin that is not inhibited by cyclosporin A Proc. Natl. Acad. Sci. USA 87 1990 4028 4032
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4028-4032
    • Liu, J.1    Walsh, C.T.2
  • 44
    • 0028058243 scopus 로고
    • Calorimetric measurements of the complexation of cyclosporine A, ascomycin, fujimycin, and rapamycin with lithium-chloride and with an immunophilin
    • D. Seebach, H.G. Bossler, R. Flowers, and E.M. Arnett Calorimetric measurements of the complexation of cyclosporine A, ascomycin, fujimycin, and rapamycin with lithium-chloride and with an immunophilin Helv. Chim. Acta 77 1994 291 305
    • (1994) Helv. Chim. Acta , vol.77 , pp. 291-305
    • Seebach, D.1    Bossler, H.G.2    Flowers, R.3    Arnett, E.M.4
  • 45
    • 0025868143 scopus 로고
    • Determination of kinetic constants for peptidyl prolyl cis-trans isomerases by an improved spectrophotometric assay
    • J.L. Kofron, P. Kuzmic, V. Kishore, E. Colon-Bonilla, and D.H. Rich Determination of kinetic constants for peptidyl prolyl cis-trans isomerases by an improved spectrophotometric assay Biochemistry 30 1991 6127 6134
    • (1991) Biochemistry , vol.30 , pp. 6127-6134
    • Kofron, J.L.1    Kuzmic, P.2    Kishore, V.3    Colon-Bonilla, E.4    Rich, D.H.5
  • 46
    • 0025923446 scopus 로고
    • A single Trp121 to Ala121 mutation in human cyclophilin alters cyclosporin a affinity and peptidyl-prolyl isomerase activity
    • M.J. Bossard, P.L. Koser, M. Brandt, D.J. Bergsma, and M.A. Levy A single Trp121 to Ala121 mutation in human cyclophilin alters cyclosporin A affinity and peptidyl-prolyl isomerase activity Biochem. Biophys. Res. Commun. 176 1991 1142 1148
    • (1991) Biochem. Biophys. Res. Commun. , vol.176 , pp. 1142-1148
    • Bossard, M.J.1    Koser, P.L.2    Brandt, M.3    Bergsma, D.J.4    Levy, M.A.5
  • 47
    • 0026651050 scopus 로고
    • Lithium chloride perturbation of cis-trans peptide bond equilibria: Effect on conformational equilibria in cyclosporin-A and on time-dependent inhibition of cyclophilin
    • J.L. Kofron, P. Kuzmic, V. Kishore, G. Gemmecker, S.W. Fesik, and D.H. Rich Lithium chloride perturbation of cis-trans peptide bond equilibria: effect on conformational equilibria in cyclosporin-A and on time-dependent inhibition of cyclophilin J. Am. Chem. Soc. 114 1992 2670 2675
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 2670-2675
    • Kofron, J.L.1    Kuzmic, P.2    Kishore, V.3    Gemmecker, G.4    Fesik, S.W.5    Rich, D.H.6


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