메뉴 건너뛰기




Volumn 23, Issue 5, 2012, Pages 908-922

Improved accuracy of low affinity protein-ligand equilibrium dissociation constants directly determined by electrospray ionization mass spectrometry

Author keywords

Accuracy; Aggregation; Equilibrium dissociation constant; ESI; Gas phase dissociation; Interaction; KD; Low affinity; Mass spectrometry; Model; Protein ligand

Indexed keywords

ACCURACY; EQUILIBRIUM DISSOCIATION CONSTANT; ESI; GAS-PHASE DISSOCIATION; INTERACTION; KD; LOW AFFINITY; PROTEIN-LIGAND;

EID: 84862515709     PISSN: 10440305     EISSN: 18791123     Source Type: Journal    
DOI: 10.1007/s13361-011-0305-7     Document Type: Article
Times cited : (22)

References (43)
  • 1
    • 0001413545 scopus 로고
    • Detection of noncovalent receptor-ligand complexes by mass spectrometry
    • Ganem, B., Li, Y.T., Henion, J.D.: Detection of noncovalent receptor-ligand complexes by mass spectrometry. J. Am. Chem. Soc. 113, 6294-6296 (1991)
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 6294-6296
    • Ganem, B.1    Li, Y.T.2    Henion, J.D.3
  • 2
    • 0343071628 scopus 로고
    • Observation of noncovalent enzyme-substrate and enzyme-product complexes by ion-spray mass spectrometry
    • Ganem, B., Li, Y.T., Henion, J.D.: Observation of noncovalent enzyme-substrate and enzyme-product complexes by ion-spray mass spectrometry. J. Am. Chem. Soc. 113, 7818-7819 (1991)
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 7818-7819
    • Ganem, B.1    Li, Y.T.2    Henion, J.D.3
  • 3
    • 0001401150 scopus 로고
    • Observation of the heme-globin complex in native myoglobin by electrospray-ionization mass spectrometry
    • Katta, V., Chait, B.T.: Observation of the heme-globin complex in native myoglobin by electrospray-ionization mass spectrometry. J. Am. Chem. Soc. 113, 8534-8535 (1991)
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 8534-8535
    • Katta, V.1    Chait, B.T.2
  • 4
    • 0000876636 scopus 로고
    • Measurement of macromolecular binding using electrospray mass spectrometry. Determination of dissociation constants for oligonucleotide: Serum albumin complexes
    • Greig, M.J., Gaus, H., Cummins, L.L., Sasmor, H., Griffey, R.H.: Measurement of macromolecular binding using electrospray mass spectrometry. Determination of dissociation constants for oligonucleotide: Serum albumin complexes. J. Am. Chem. Soc. 117, 10765-10766 (1995)
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 10765-10766
    • Greig, M.J.1    Gaus, H.2    Cummins, L.L.3    Sasmor, H.4    Griffey, R.H.5
  • 5
    • 0029035380 scopus 로고
    • Recognition of cell-wall peptide ligands by vancomycin group antibiotics: Studies using ion spray mass spectrometry
    • Lim, H., Hsieh, Y.L., Ganem, B., Henion, J.: Recognition of cell-wall peptide ligands by vancomycin group antibiotics: Studies using ion spray mass spectrometry. J. Mass Spectrom. 30, 708-714 (1995)
    • (1995) J. Mass Spectrom. , vol.30 , pp. 708-714
    • Lim, H.1    Hsieh, Y.L.2    Ganem, B.3    Henion, J.4
  • 7
    • 0038293125 scopus 로고    scopus 로고
    • Quantification of protein-ligand interactions by mass spectrometry, titration, and H/D exchange: PLIMSTEX
    • DOI 10.1021/ja029460d
    • Zhu, M.M., Rempel, D.L., Du, Z., Gross, M.L.: Quantification of protein-ligand interactions by mass spectrometry, titration, and H/D exchange: PLIMSTEX. J. Am. Chem. Soc. 125, 5252-5253 (2003) (Pubitemid 36582715)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.18 , pp. 5252-5253
    • Zhu, M.M.1    Rempel, D.L.2    Du, Z.3    Gross, M.L.4
  • 8
    • 10844277304 scopus 로고    scopus 로고
    • SUPREX (Stability of Unpurified Proteins from Rates of H/D Exchange) analysis of the thermodynamics of synergistic anion binding by ferric-binding protein (FbpA), a bacterial transferring
    • DOI 10.1021/bi0481848
    • Roulhac, P.L., Powell, K.D., Dhungana, S., Weaver, K.D., Mietzner, T. A., Crumbliss, A.L., Fitzgerald, M.C.: SUPREX (Stability of unpurified proteins from rates of H/D exchange) analysis of the thermodynamics of synergistic anion binding by Ferric-Binding Protein (FbpA), a bacterial transferrin. Biochemistry 43, 15767-15774 (2004) (Pubitemid 39665076)
    • (2004) Biochemistry , vol.43 , Issue.50 , pp. 15767-15774
    • Roulhac, P.L.1    Powell, K.D.2    Dhungana, S.3    Weaver, K.D.4    Mietzner, T.A.5    Crumbliss, A.L.6    Fitzgerald, M.C.7
  • 9
    • 0001169698 scopus 로고
    • Fritz, H., Tschesche, H., Greene, L.J., Truscheit, E. (eds.). Springer Verlag, New York
    • Bieth, J.: In: Fritz, H., Tschesche, H., Greene, L.J., Truscheit, E. (eds.) Bayer Symposium V, Proteinase Inhibitors, pp. 463-469. Springer Verlag, New York (1974)
    • (1974) Bayer Symposium V, Proteinase Inhibitors , pp. 463-469
    • Bieth, J.1
  • 10
    • 0033994459 scopus 로고    scopus 로고
    • Binding of selected carbohydrates to apo-concanavalin A studied by electrospray ionization mass spectrometry
    • DOI 10.1039/a907957b
    • van Dongen, W.D., Heck, A.J.R.: Binding of selected carbohydrates to apo-concanavalin A studied by electrospray ionization mass spectrometry. Analyst 125, 583-589 (2000) (Pubitemid 30223642)
    • (2000) Analyst , vol.125 , Issue.4 , pp. 583-589
    • Van Dongen, W.D.1    Heck, A.J.R.2
  • 11
    • 10044271179 scopus 로고    scopus 로고
    • Determination of ligand-protein dissociation constants by electrospray mass spectrometry-based diffusion measurements
    • DOI 10.1021/ac049344o
    • Clark, S.M., Konermann, L.: Determination of ligand-protein dissociation constants by electrospray mass spectrometry-based diffusion measurements. Anal. Chem. 76, 7077-7083 (2004) (Pubitemid 39600883)
    • (2004) Analytical Chemistry , vol.76 , Issue.23 , pp. 7077-7083
    • Clark, S.M.1    Konermann, L.2
  • 12
    • 33846194221 scopus 로고    scopus 로고
    • Method for stabilizing protein-ligand complexes in nanoelectrospray ionization mass spectrometry
    • DOI 10.1021/ac061109d
    • Sun, J., Kitova, E.N., Klassen, J.S.: Method for stabilizing protein-ligand complexes in nanoelectrospray ionization mass spectrometry. Anal. Chem. 79, 416-425 (2007) (Pubitemid 46106105)
    • (2007) Analytical Chemistry , vol.79 , Issue.2 , pp. 416-425
    • Sun, J.1    Kitova, E.N.2    Klassen, J.S.3
  • 13
    • 0141958921 scopus 로고    scopus 로고
    • Influence of solution and gas phase processes on protein-carbohydrate binding affinities determined by nanoelectrospray fourier transform ion cyclotron resonance mass spectrometry
    • DOI 10.1021/ac034300l
    • Wang, W., Kitova, E.N., Klassen, J.S.: Influence of solution and gas phase processes on protein-carbohydrate binding affinities determined by nanoelectrospray Fourier transform ion cyclotron resonance mass spectrometry. Anal. Chem. 75, 4945-4955 (2003) (Pubitemid 37238544)
    • (2003) Analytical Chemistry , vol.75 , Issue.19 , pp. 4945-4955
    • Wang, W.1    Kitova, E.N.2    Klassen, J.S.3
  • 14
    • 25144435539 scopus 로고    scopus 로고
    • Blackbody infrared radiative dissociation of nonspecific protein-carbohydrate complexes produced by nanoelectrospray ionization: The nature of the noncovalent interactions
    • DOI 10.1016/j.jasms.2005.05.008, PII S1044030505004423
    • Wang, W., Kitova, E.N., Sun, J., Klassen, J.S.: Blackbody infrared radiative dissociation of nonspecific protein-carbohydrate complexes produced by nanoelectrospray ionization: The nature of the noncovalent interactions. J. Am. Soc. Mass Spectrom. 16, 1583-1594 (2005) (Pubitemid 41348685)
    • (2005) Journal of the American Society for Mass Spectrometry , vol.16 , Issue.10 , pp. 1583-1594
    • Wang, W.1    Kitova, E.N.2    Sun, J.3    Klassen, J.S.4
  • 15
    • 4744344760 scopus 로고    scopus 로고
    • Features of the ESI mechanism that affect the observation of multiply charged noncovalent protein complexes and the determination of the association constant by the titration method
    • DOI 10.1016/j.jasms.2004.05.005, PII S1044030504003411
    • Peschke, M., Verkerk, U.H., Kebarle, P.: Features of the ESI mechanism that affect the observation of multiply charged noncovalent protein complexes and the determination of the association constant by the titration method. J. Am. Soc. Mass Spectrom. 15, 1424-1434 (2004) (Pubitemid 39311693)
    • (2004) Journal of the American Society for Mass Spectrometry , vol.15 , Issue.10 , pp. 1424-1434
    • Peschke, M.1    Verkerk, U.H.2    Kebarle, P.3
  • 16
    • 33747889827 scopus 로고    scopus 로고
    • A deconvolution method for the separation of specific versus nonspecific interactions in noncovalent protein-ligand complexes analyzed by ESI-FT-ICR mass spectrometry
    • DOI 10.1016/j.jasms.2006.05.005, PII S104403050600482X
    • Daubenfeld, T., Bouin, A.-P., van der Rest, G.: A deconvolution method for the separation of specific versus nonspecific interactions in noncovalent protein-ligand complexes analyzed by ESI-FT-ICR mass spectrometry. J. Am. Soc. Mass Spectrom. 17, 1239-1248 (2006) (Pubitemid 44292005)
    • (2006) Journal of the American Society for Mass Spectrometry , vol.17 , Issue.9 , pp. 1239-1248
    • Daubenfeld, T.1    Bouin, A.-P.2    Van Der Rest, G.3
  • 17
    • 33646589615 scopus 로고    scopus 로고
    • Method for distinguishing specific from nonspecific protein-ligand complexes in nanoelectrospray ionization mass spectrometry
    • DOI 10.1021/ac0522005
    • Sun, J., Kitova, E.N., Wang, W., Klassen, J.S.: Method for distinguishing specific from nonspecific protein-ligand complexes in nanoelectrospray ionization mass spectrometry. Anal. Chem. 78, 3010-3018 (2006) (Pubitemid 43726119)
    • (2006) Analytical Chemistry , vol.78 , Issue.9 , pp. 3010-3018
    • Sun, J.1    Kitova, E.N.2    Wang, W.3    Klassen, J.S.4
  • 18
    • 58249083162 scopus 로고    scopus 로고
    • How to deal with weak interactions in noncovalent complexes analyzed by electrospray mass spectrometry: Cyclopeptidic inhibitors of the nuclear receptor coactivator 1-STAT6
    • Touboul, D., Maillard, L., Grässlin, A., Moumne, R., Seitz, M., Robinson, J., Zenobi, R.: How to deal with weak interactions in noncovalent complexes analyzed by electrospray mass spectrometry: Cyclopeptidic inhibitors of the nuclear receptor coactivator 1-STAT6. J. Am. Soc. Mass Spectrom. 20, 303-311 (2009)
    • (2009) J. Am. Soc. Mass Spectrom. , vol.20 , pp. 303-311
    • Touboul, D.1    Maillard, L.2    Grässlin, A.3    Moumne, R.4    Seitz, M.5    Robinson, J.6    Zenobi, R.7
  • 19
    • 0035894046 scopus 로고    scopus 로고
    • Influence of pressure in the first pumping stage on analyte desolvation and fragmentation in Nano-ESI MS
    • DOI 10.1021/ac010451h
    • Schmidt, A., Bahr, U., Karas, M.: Influence of pressure in the first pumping stage on analyte desolvation and fragmentation in nano-ESI MS. Anal. Chem. 73, 6040-6046 (2001) (Pubitemid 34042222)
    • (2001) Analytical Chemistry , vol.73 , Issue.24 , pp. 6040-6046
    • Schmidt, A.1    Bahr, U.2    Karas, M.3
  • 20
    • 0035029535 scopus 로고    scopus 로고
    • The effect of the source pressure on the abundance of ions of noncovalent protein assemblies in an electrospray ionization orthogonal time-of-flight instrument
    • DOI 10.1002/rcm.275
    • Tahallah, N., Pinkse, M., Maier, C.S., Heck, A.J.: The effect of the source pressure on the abundance of ions of noncovalent protein assemblies in an electrospray ionization orthogonal time-of-flight instrument. Rapid Commun. Mass Spectrom. 15, 596-601 (2001) (Pubitemid 32391094)
    • (2001) Rapid Communications in Mass Spectrometry , vol.15 , Issue.8 , pp. 596-601
    • Tahallah, N.1    Pinkse, M.2    Maier, C.S.3    Heck, A.J.R.4
  • 21
    • 60349097912 scopus 로고    scopus 로고
    • Nondenaturing mass spectrometry to study noncovalent protein/protein and protein/ligand complexes: Technical aspects and application to the determination of binding stoichiometries
    • Sanglier, S., Atmanene, C., Chevreux, G., Dorsselaer, A.V.: Nondenaturing mass spectrometry to study noncovalent protein/protein and protein/ligand complexes: Technical aspects and application to the determination of binding stoichiometries. Methods Mol. Biol. 484, 217-243 (2008)
    • (2008) Methods Mol. Biol. , vol.484 , pp. 217-243
    • Sanglier, S.1    Atmanene, C.2    Chevreux, G.3    Dorsselaer, A.V.4
  • 22
    • 70349126310 scopus 로고    scopus 로고
    • Gas phase stabilization of noncovalent protein complexes formed by electrospray ionization
    • Bagal, D., Kitova, E.N., Liu, L., El-Hawiet, A., Schnier, P.D., Klassen, J.S.: Gas phase stabilization of noncovalent protein complexes formed by electrospray ionization. Anal. Chem. 81, 7801-7806 (2009)
    • (2009) Anal. Chem. , vol.81 , pp. 7801-7806
    • Bagal, D.1    Kitova, E.N.2    Liu, L.3    El-Hawiet, A.4    Schnier, P.D.5    Klassen, J.S.6
  • 23
    • 3543008337 scopus 로고    scopus 로고
    • Determination of dissociation constants for protein-ligand complexes by electrospray ionization mass spectrometry
    • DOI 10.1021/ac0497914
    • Tjernberg, A., Carnö, S., Oliv, F., Benkestock, K., Edlund, P.-O., Griffiths, W.J., Hallén, D.: Determination of dissociation constants for protein-ligand complexes by electrospray ionization mass spectrometry. Anal. Chem. 76, 4325-4331 (2004) (Pubitemid 39014001)
    • (2004) Analytical Chemistry , vol.76 , Issue.15 , pp. 4325-4331
    • Tjernberg, A.1    Carno, S.2    Oliv, F.3    Benkestock, K.4    Edlund, P.-O.5    Griffiths, W.J.6    Hallen, D.7
  • 25
  • 28
    • 0001962888 scopus 로고
    • Molecular mass measurement of intact ribonucleic acids via electrospray ionization quadrupole mass spectrometry
    • Limbach, P.A., Crain, P.F., McCloskey, J.A.: Molecular mass measurement of intact ribonucleic acids via electrospray ionization quadrupole mass spectrometry. J. Am. Soc. Mass Spectrom. 6, 27-39 (1995)
    • (1995) J. Am. Soc. Mass Spectrom. , vol.6 , pp. 27-39
    • Limbach, P.A.1    Crain, P.F.2    McCloskey, J.A.3
  • 30
    • 0028104165 scopus 로고
    • Relationships between molecular interactions (nucleotides, lipids and proteins) and structural features of the bovine brain 21-kDa protein
    • DOI 10.1111/j.1432-1033.1994.1203b.x
    • Bucquoy, S., Jollès, P., Schoentgen, F.: Relationships between molecular interactions (nucleotides, lipids and proteins) and structural features of the bovine brain 21-kDa protein. Eur. J. Biochem. 225, 1203-1210 (1994) (Pubitemid 24342567)
    • (1994) European Journal of Biochemistry , vol.225 , Issue.3 , pp. 1203-1210
    • Bucquoy, S.1    Jolles, P.2    Schoentgen, F.3
  • 31
    • 0038338887 scopus 로고    scopus 로고
    • Quantitative determination of noncovalent binding interactions using automated nanoelectrospray mass spectrometry
    • DOI 10.1021/ac034089d
    • Zhang, S., Van Pelt, C.K., Wilson, D.B.: Quantitative determination of noncovalent binding interactions using automated nanoelectrospray mass spectrometry. Anal. Chem. 75, 3010-3018 (2003) (Pubitemid 36830427)
    • (2003) Analytical Chemistry , vol.75 , Issue.13 , pp. 3010-3018
    • Zhang, S.1    Van Pelt, C.K.2    Wilson, D.B.3
  • 32
    • 0026734102 scopus 로고
    • Two-dimensional differential scanning calorimetry: Simultaneous resolution of intrinsic protein structural energetics and ligand binding interactions by global linkage analysis
    • Straume, M., Freire, E.: Two-dimensional differential scanning calorimetry: Simultaneous resolution of intrinsic protein structural energetics and ligand binding interactions by global linkage analysis. Anal. Biochem. 203, 259-268 (1992)
    • (1992) Anal. Biochem. , vol.203 , pp. 259-268
    • Straume, M.1    Freire, E.2
  • 33
    • 0024356301 scopus 로고
    • Rapid measurement of binding constants and heats of binding using a new titration calorimeter
    • DOI 10.1016/0003-2697(89)90213-3
    • Wiseman, T., Williston, S., Brandts, J.F., Lin, L.N.: Rapid measurement of binding constants and heats of binding using a new titration calorimeter. Anal. Biochem. 179, 131-137 (1989) (Pubitemid 19149635)
    • (1989) Analytical Biochemistry , vol.179 , Issue.1 , pp. 131-137
    • Wiseman, T.1    Williston, S.2    Brandts, J.F.3    Lin, L.-N.4
  • 34
    • 0037086395 scopus 로고    scopus 로고
    • Determination of RNase A/2′-cytidine monophosphate binding affinity and enthalpy by a global fit of thermal unfolding curves
    • DOI 10.1006/abio.2001.5529
    • Jones, C.L., Fish, F., Muccio, D.D.: Determination of RNase A/2'-cytidine monophosphate binding affinity and enthalpy by a global fit of thermal unfolding curves. Anal. Biochem. 302, 184-190 (2002) (Pubitemid 34229722)
    • (2002) Analytical Biochemistry , vol.302 , Issue.2 , pp. 184-190
    • Jones, C.L.1    Fish, F.2    Muccio, D.D.3
  • 35
    • 33750992148 scopus 로고    scopus 로고
    • Regulation of RKIP binding to the N-region of the Raf-1 kinase
    • DOI 10.1016/j.febslet.2006.10.054, PII S001457930601283X
    • Park, S., Rath, O., Beach, S., Xiang, X., Kelly, S.M., Luo, Z., Kolch, W., Yeung, K.C.: Regulation of RKIP binding to the N-region of the Raf-1 kinase. FEBS Lett. 580, 6405-6412 (2006) (Pubitemid 44750928)
    • (2006) FEBS Letters , vol.580 , Issue.27 , pp. 6405-6412
    • Park, S.1    Rath, O.2    Beach, S.3    Xiang, X.4    Kelly, S.M.5    Luo, Z.6    Kolch, W.7    Yeung, K.C.8
  • 36
    • 0017350198 scopus 로고
    • Mechanism of lysozyme catalysis: Role of ground state strain in subsite D in hen egg white and human lysozymes
    • DOI 10.1021/bi00622a013
    • Schindler, M., Assaf, Y., Sharon, N., Chipman, D.M.: Mechanism of lysozyme catalysis: Role of ground-state strain in subsite D in hen eggwhite and human lysozymes. Biochemistry 16, 423-431 (1977) (Pubitemid 8036372)
    • (1977) Biochemistry , vol.16 , Issue.3 , pp. 423-431
    • Schindler, M.1    Assaf, Y.2    Sharon, N.3    Chipman, D.M.4
  • 37
    • 0024310710 scopus 로고
    • Internal thermodynamics of enzymes determined by equilibrium quench: Values of K(int) for enolase and creatine kinase
    • DOI 10.1021/bi00450a010
    • Burbaum, J.J., Knowles, J.R.: Internal thermodynamics of enzymes determined by equilibrium quench: Values of Kint for enolase and creatine kinase. Biochemistry 28, 9306-9317 (1989) (Pubitemid 20000701)
    • (1989) Biochemistry , vol.28 , Issue.24 , pp. 9306-9317
    • Burbaum, J.J.1    Knowles, J.R.2
  • 38
    • 76749128036 scopus 로고    scopus 로고
    • Nonspecific interactions between proteins and charged biomolecules in electrospray ionization mass spectrometry
    • Sun, N., Soya, N., Kitova, E.N., Klassen, J.S.: Nonspecific interactions between proteins and charged biomolecules in electrospray ionization mass spectrometry. J. Am. Soc. Mass Spectrom. 21, 472-481 (2010)
    • (2010) J. Am. Soc. Mass Spectrom. , vol.21 , pp. 472-481
    • Sun, N.1    Soya, N.2    Kitova, E.N.3    Klassen, J.S.4
  • 39
    • 77958179943 scopus 로고    scopus 로고
    • Quantifying labile protein-ligand interactions using electrospray ionization mass spectrometry
    • El-Hawiet, A., Kitova, E.N., Liu, L., Klassen, J.S.: Quantifying labile protein-ligand interactions using electrospray ionization mass spectrometry. J. Am. Soc. Mass Spectrom. 21, 1893-1899 (2010)
    • (2010) J. Am. Soc. Mass Spectrom. , vol.21 , pp. 1893-1899
    • El-Hawiet, A.1    Kitova, E.N.2    Liu, L.3    Klassen, J.S.4
  • 42
    • 0026551529 scopus 로고
    • Refinement of an enzyme complex with inhibitor bound at partial occupancy: Hen eggwhite lysozyme and tri-N-acetylchitotriose at 1.75 A resolution
    • Cheetham, J.C., Artymiuk, P.J., Phillips, D.C.: Refinement of an enzyme complex with inhibitor bound at partial occupancy: Hen eggwhite lysozyme and tri-N-acetylchitotriose at 1.75 A resolution. J. Mol. Biol. 224, 613-628 (1992)
    • (1992) J. Mol. Biol. , vol.224 , pp. 613-628
    • Cheetham, J.C.1    Artymiuk, P.J.2    Phillips, D.C.3
  • 43
    • 40249115327 scopus 로고    scopus 로고
    • Which electrospray-based ionization method best reflects protein-ligand interactions found in solution? A comparison of ESI, nanoESI, and ESSI for the determination of dissociation constants with mass spectrometry
    • Jecklin, M.C., Touboul, D., Bovet, C., Wortmann, A., Zenobi, R.: Which electrospray-based ionization method best reflects protein-ligand interactions found in solution? A comparison of ESI, nanoESI, and ESSI for the determination of dissociation constants with mass spectrometry. J. Am. Soc. Mass Spectrom. 19, 332-343 (2008)
    • (2008) J. Am. Soc. Mass Spectrom. , vol.19 , pp. 332-343
    • Jecklin, M.C.1    Touboul, D.2    Bovet, C.3    Wortmann, A.4    Zenobi, R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.