메뉴 건너뛰기




Volumn 408, Issue 1, 2011, Pages 46-52

Nanodiscs allow the use of integral membrane proteins as analytes in surface plasmon resonance studies

Author keywords

Biacore; Nanodisc; Single cycle kinetics; Surface plasmon resonance

Indexed keywords

ACTIVATION ANALYSIS; AMINO ACIDS; ANTIBODIES; MEMBRANES; PLASMONS; RESONANCE;

EID: 77958499580     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2010.08.028     Document Type: Article
Times cited : (51)

References (44)
  • 1
    • 60149096311 scopus 로고    scopus 로고
    • Properties and identification of human protein drug targets
    • Bakheet T.M., Doig A.J. Properties and identification of human protein drug targets. Bioinformatics 2009, 25:451-457.
    • (2009) Bioinformatics , vol.25 , pp. 451-457
    • Bakheet, T.M.1    Doig, A.J.2
  • 3
    • 2542465914 scopus 로고    scopus 로고
    • SPR for molecular interaction analysis: a review of emerging application areas
    • Karlsson R. SPR for molecular interaction analysis: a review of emerging application areas. J. Mol. Recognit. 2004, 17:151-161.
    • (2004) J. Mol. Recognit. , vol.17 , pp. 151-161
    • Karlsson, R.1
  • 4
    • 0010345821 scopus 로고
    • Kinetic and concentration analysis using BIA technology
    • Karlsson R., Roos H., Fägerstam L., Persson B. Kinetic and concentration analysis using BIA technology. Methods 1994, 6:99-110.
    • (1994) Methods , vol.6 , pp. 99-110
    • Karlsson, R.1    Roos, H.2    Fägerstam, L.3    Persson, B.4
  • 5
    • 0031239424 scopus 로고    scopus 로고
    • Biotechnological applications of surface plasmon resonance
    • Silin V., Plant A. Biotechnological applications of surface plasmon resonance. Trends Biotechnol. 1997, 15:353-359.
    • (1997) Trends Biotechnol. , vol.15 , pp. 353-359
    • Silin, V.1    Plant, A.2
  • 6
    • 0037080991 scopus 로고    scopus 로고
    • Flow-mediated on-surface reconstitution of G-protein coupled receptors for applications in surface plasmon resonance biosensors
    • Karlsson O.P., Lofas S. Flow-mediated on-surface reconstitution of G-protein coupled receptors for applications in surface plasmon resonance biosensors. Anal. Biochem. 2002, 300:132-138.
    • (2002) Anal. Biochem. , vol.300 , pp. 132-138
    • Karlsson, O.P.1    Lofas, S.2
  • 7
    • 33745902222 scopus 로고    scopus 로고
    • Analyzing ligand and small molecule binding activity of solubilized GPCRs using biosensor technology
    • Navratilova I., Dioszegi M., Myszka D.G. Analyzing ligand and small molecule binding activity of solubilized GPCRs using biosensor technology. Anal. Biochem. 2006, 355:132-139.
    • (2006) Anal. Biochem. , vol.355 , pp. 132-139
    • Navratilova, I.1    Dioszegi, M.2    Myszka, D.G.3
  • 8
    • 0345236608 scopus 로고    scopus 로고
    • Capture and reconstitution of G protein-coupled receptors on a biosensor surface
    • Stenlund P., Babcock G.J., Sodroski J., Myszka D.G. Capture and reconstitution of G protein-coupled receptors on a biosensor surface. Anal. Biochem. 2003, 316:243-250.
    • (2003) Anal. Biochem. , vol.316 , pp. 243-250
    • Stenlund, P.1    Babcock, G.J.2    Sodroski, J.3    Myszka, D.G.4
  • 9
    • 22944468181 scopus 로고    scopus 로고
    • Plasmon resonance methods in GPCR signaling and other membrane events
    • Alves I.D., Park C.K., Hruby V.J. Plasmon resonance methods in GPCR signaling and other membrane events. Curr. Protein Pept. Sci. 2005, 6:293-312.
    • (2005) Curr. Protein Pept. Sci. , vol.6 , pp. 293-312
    • Alves, I.D.1    Park, C.K.2    Hruby, V.J.3
  • 10
  • 11
    • 0036391231 scopus 로고    scopus 로고
    • Surface plasmon resonance spectroscopy: an emerging tool for the study of peptide-membrane interactions
    • Mozsolits H., Aguilar M.I. Surface plasmon resonance spectroscopy: an emerging tool for the study of peptide-membrane interactions. Biopolymers 2002, 66:3-18.
    • (2002) Biopolymers , vol.66 , pp. 3-18
    • Mozsolits, H.1    Aguilar, M.I.2
  • 13
    • 0001439414 scopus 로고
    • Self-assembled phospholipid/alkanethiol biomimetic bilayers on gold
    • Plant A.L. Self-assembled phospholipid/alkanethiol biomimetic bilayers on gold. Langmuir 1993, 9:2764-2767.
    • (1993) Langmuir , vol.9 , pp. 2764-2767
    • Plant, A.L.1
  • 14
    • 0034650303 scopus 로고    scopus 로고
    • A vesicle capture sensor chip for kinetic analysis of interactions with membrane-bound receptors
    • Cooper M.A., Hansson A., Lofas S., Williams D.H. A vesicle capture sensor chip for kinetic analysis of interactions with membrane-bound receptors. Anal. Biochem. 2000, 277:196-205.
    • (2000) Anal. Biochem. , vol.277 , pp. 196-205
    • Cooper, M.A.1    Hansson, A.2    Lofas, S.3    Williams, D.H.4
  • 15
    • 50049101521 scopus 로고    scopus 로고
    • Nanodiscs for immobilization of lipid bilayers and membrane receptors: kinetic analysis of cholera toxin binding to a glycolipid receptor
    • Borch J., Torta F., Sligar S.G., Roepstorff P. Nanodiscs for immobilization of lipid bilayers and membrane receptors: kinetic analysis of cholera toxin binding to a glycolipid receptor. Anal. Chem. 2008, 80:6245-6252.
    • (2008) Anal. Chem. , vol.80 , pp. 6245-6252
    • Borch, J.1    Torta, F.2    Sligar, S.G.3    Roepstorff, P.4
  • 16
    • 34250365394 scopus 로고    scopus 로고
    • The local phospholipid environment modulates the activation of blood clotting
    • Shaw A.W., Pureza V.S., Sligar S.G., Morrissey J.H. The local phospholipid environment modulates the activation of blood clotting. J. Biol. Chem. 2007, 282:6556-6563.
    • (2007) J. Biol. Chem. , vol.282 , pp. 6556-6563
    • Shaw, A.W.1    Pureza, V.S.2    Sligar, S.G.3    Morrissey, J.H.4
  • 17
    • 66149100484 scopus 로고    scopus 로고
    • Screening of type I and II drug binding to human cytochrome P450-3A4 in nanodiscs by localized surface plasmon resonance spectroscopy
    • Das A., Zhao J., Schatz G.C., Sligar S.G., Van Duyne R.P. Screening of type I and II drug binding to human cytochrome P450-3A4 in nanodiscs by localized surface plasmon resonance spectroscopy. Anal. Chem. 2009, 81:3754-3759.
    • (2009) Anal. Chem. , vol.81 , pp. 3754-3759
    • Das, A.1    Zhao, J.2    Schatz, G.C.3    Sligar, S.G.4    Van Duyne, R.P.5
  • 18
    • 0043007514 scopus 로고    scopus 로고
    • Self-assembly of discoidal phospholipid bilayer nanoparticles with membrane scaffold proteins
    • Bayburt T.H., Grinkova Y.V., Sligar S.G. Self-assembly of discoidal phospholipid bilayer nanoparticles with membrane scaffold proteins. Nano Lett. 2002, 8:853-856.
    • (2002) Nano Lett. , vol.8 , pp. 853-856
    • Bayburt, T.H.1    Grinkova, Y.V.2    Sligar, S.G.3
  • 19
    • 0142179052 scopus 로고    scopus 로고
    • Self-assembly of single integral membrane proteins into soluble nanoscale phospholipid bilayers
    • Bayburt T.H., Sligar S.G. Self-assembly of single integral membrane proteins into soluble nanoscale phospholipid bilayers. Protein Sci. 2003, 12:2476-2481.
    • (2003) Protein Sci. , vol.12 , pp. 2476-2481
    • Bayburt, T.H.1    Sligar, S.G.2
  • 20
    • 0042691480 scopus 로고    scopus 로고
    • Direct solubilization of heterologously expressed membrane proteins by incorporation into nanoscale lipid bilayers
    • Civjan N.R., Bayburt T.H., Schuler M.A., Sligar S.G. Direct solubilization of heterologously expressed membrane proteins by incorporation into nanoscale lipid bilayers. BioTechniques 2003, 35:556-563.
    • (2003) BioTechniques , vol.35 , pp. 556-563
    • Civjan, N.R.1    Bayburt, T.H.2    Schuler, M.A.3    Sligar, S.G.4
  • 21
    • 77951903021 scopus 로고    scopus 로고
    • Membrane protein assembly into nanodiscs
    • Bayburt T.H., Sligar S.G. Membrane protein assembly into nanodiscs. FEBS Lett. 2010, 584:1721-1727.
    • (2010) FEBS Lett. , vol.584 , pp. 1721-1727
    • Bayburt, T.H.1    Sligar, S.G.2
  • 22
    • 33847639732 scopus 로고    scopus 로고
    • Applications of phospholipid bilayer nanodiscs in the study of membranes and membrane proteins
    • Nath A., Atkins W.M., Sligar S.G. Applications of phospholipid bilayer nanodiscs in the study of membranes and membrane proteins. Biochemistry 2007, 46:2059-2069.
    • (2007) Biochemistry , vol.46 , pp. 2059-2069
    • Nath, A.1    Atkins, W.M.2    Sligar, S.G.3
  • 23
    • 40849130624 scopus 로고    scopus 로고
    • Rapid incorporation of functional rhodopsin into nanoscale apolipoprotein bound bilayer (NABB) particles
    • Banerjee S., Huber T., Sakmar T.P. Rapid incorporation of functional rhodopsin into nanoscale apolipoprotein bound bilayer (NABB) particles. J. Mol. Biol. 2008, 377:1067-1081.
    • (2008) J. Mol. Biol. , vol.377 , pp. 1067-1081
    • Banerjee, S.1    Huber, T.2    Sakmar, T.P.3
  • 24
    • 34447509986 scopus 로고    scopus 로고
    • Transducin activation by nanoscale lipid bilayers containing one and two rhodopsins
    • Bayburt T.H., Leitz A.J., Xie G., Oprian D.D., Sligar S.G. Transducin activation by nanoscale lipid bilayers containing one and two rhodopsins. J. Biol. Chem. 2007, 282:14875-14881.
    • (2007) J. Biol. Chem. , vol.282 , pp. 14875-14881
    • Bayburt, T.H.1    Leitz, A.J.2    Xie, G.3    Oprian, D.D.4    Sligar, S.G.5
  • 25
    • 33746856934 scopus 로고    scopus 로고
    • Nanodiscs separate chemoreceptor oligomeric states and reveal their signaling properties
    • Boldog T., Grimme S., Li M., Sligar S.G., Hazelbauer G.L. Nanodiscs separate chemoreceptor oligomeric states and reveal their signaling properties. Proc. Natl. Acad. Sci. USA 2006, 103:11509-11514.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 11509-11514
    • Boldog, T.1    Grimme, S.2    Li, M.3    Sligar, S.G.4    Hazelbauer, G.L.5
  • 26
    • 34247214427 scopus 로고    scopus 로고
    • Nanodiscs unravel the interaction between the SecYEG channel and its cytosolic partner SecA
    • Alami M., Dalal K., Lelj-Garolla B., Sligar S.G., Duong F. Nanodiscs unravel the interaction between the SecYEG channel and its cytosolic partner SecA. EMBO J. 2007, 26:1995-2004.
    • (2007) EMBO J. , vol.26 , pp. 1995-2004
    • Alami, M.1    Dalal, K.2    Lelj-Garolla, B.3    Sligar, S.G.4    Duong, F.5
  • 27
    • 36849060525 scopus 로고    scopus 로고
    • Structural characterization of the transmembrane and cytoplasmic domains of human CD4
    • Wittlich M., Koenig B.W., Hoffmann S., Willbold D. Structural characterization of the transmembrane and cytoplasmic domains of human CD4. Biochim. Biophys. Acta 2007, 1768:2949-2960.
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 2949-2960
    • Wittlich, M.1    Koenig, B.W.2    Hoffmann, S.3    Willbold, D.4
  • 28
    • 34547919582 scopus 로고    scopus 로고
    • Expression, purification, and membrane reconstitution of a CD4 fragment comprising the transmembrane and cytoplasmic domains of the receptor
    • Wittlich M., Wiesehan K., Koenig B.W., Willbold D. Expression, purification, and membrane reconstitution of a CD4 fragment comprising the transmembrane and cytoplasmic domains of the receptor. Protein Expr. Purif. 2007, 55:198-207.
    • (2007) Protein Expr. Purif. , vol.55 , pp. 198-207
    • Wittlich, M.1    Wiesehan, K.2    Koenig, B.W.3    Willbold, D.4
  • 29
    • 0032111031 scopus 로고    scopus 로고
    • A new general method for the biosynthesis of stable isotope-enriched peptides using a decahistidine-tagged ubiquitin fusion system: an application to the production of mastoparan-X uniformly enriched with 15N and 15N/13C
    • Kohno T., Kusunoki H., Sato K., Wakamatsu K. A new general method for the biosynthesis of stable isotope-enriched peptides using a decahistidine-tagged ubiquitin fusion system: an application to the production of mastoparan-X uniformly enriched with 15N and 15N/13C. J. Biomol. NMR 1998, 12:109-121.
    • (1998) J. Biomol. NMR , vol.12 , pp. 109-121
    • Kohno, T.1    Kusunoki, H.2    Sato, K.3    Wakamatsu, K.4
  • 30
    • 1642382983 scopus 로고    scopus 로고
    • Directed self-assembly of monodisperse phospholipid bilayer nanodiscs with controlled size
    • Denisov I.G., Grinkova Y.V., Lazarides A.A., Sligar S.G. Directed self-assembly of monodisperse phospholipid bilayer nanodiscs with controlled size. J. Am. Chem. Soc. 2004, 126:3477-3487.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 3477-3487
    • Denisov, I.G.1    Grinkova, Y.V.2    Lazarides, A.A.3    Sligar, S.G.4
  • 32
    • 0032701484 scopus 로고    scopus 로고
    • Improving biosensor analysis
    • Myszka D.G. Improving biosensor analysis. J. Mol. Recognit. 1999, 12:279-284.
    • (1999) J. Mol. Recognit. , vol.12 , pp. 279-284
    • Myszka, D.G.1
  • 34
    • 33745166596 scopus 로고    scopus 로고
    • New multi-step kinetics using common affinity biosensors saves time and sample at full access to kinetics and concentration
    • Trutnau H.H. New multi-step kinetics using common affinity biosensors saves time and sample at full access to kinetics and concentration. J. Biotechnol. 2006, 124:191-195.
    • (2006) J. Biotechnol. , vol.124 , pp. 191-195
    • Trutnau, H.H.1
  • 36
    • 0027198367 scopus 로고
    • Antigen-antibody binding and mass transport by convection and diffusion to a surface. A two-dimensional computer model of binding and dissociation kinetics
    • Glaser R.W. Antigen-antibody binding and mass transport by convection and diffusion to a surface. A two-dimensional computer model of binding and dissociation kinetics. Anal. Biochem. 1993, 213:152-161.
    • (1993) Anal. Biochem. , vol.213 , pp. 152-161
    • Glaser, R.W.1
  • 37
    • 0032752117 scopus 로고    scopus 로고
    • The influence of transport on the kinetics of binding to surface receptors: application to cells and BIAcore
    • Goldstein B., Coombs D., He X., Pineda A.R., Wofsy C. The influence of transport on the kinetics of binding to surface receptors: application to cells and BIAcore. J. Mol. Recognit. 1999, 12:293-299.
    • (1999) J. Mol. Recognit. , vol.12 , pp. 293-299
    • Goldstein, B.1    Coombs, D.2    He, X.3    Pineda, A.R.4    Wofsy, C.5
  • 38
    • 0031848098 scopus 로고    scopus 로고
    • Extending the range of rate constants available from Biacore: interpreting mass transport-influenced binding data
    • Myszka D.G., He X., Dembo M., Morton T.A., Goldstein B. Extending the range of rate constants available from Biacore: interpreting mass transport-influenced binding data. Biophys. J. 1998, 75:583-594.
    • (1998) Biophys. J. , vol.75 , pp. 583-594
    • Myszka, D.G.1    He, X.2    Dembo, M.3    Morton, T.A.4    Goldstein, B.5
  • 39
    • 77958498315 scopus 로고    scopus 로고
    • Biacore, BIAevaluation Software Handbook, GE Healthcare, Freiburg, Germany
    • Biacore, BIAevaluation Software Handbook, GE Healthcare, Freiburg, Germany, 2007.
    • (2007)
  • 40
    • 0042846629 scopus 로고    scopus 로고
    • Tandem immobilized metal-ion affinity chromatography/immunoaffinity purification of His-tagged proteins: evaluation of two anti-His-tag monoclonal antibodies
    • Müller K.M., Arndt K.M., Bauer K., Plückthun A. Tandem immobilized metal-ion affinity chromatography/immunoaffinity purification of His-tagged proteins: evaluation of two anti-His-tag monoclonal antibodies. Anal. Biochem. 1998, 259:54-61.
    • (1998) Anal. Biochem. , vol.259 , pp. 54-61
    • Müller, K.M.1    Arndt, K.M.2    Bauer, K.3    Plückthun, A.4
  • 41
    • 0001973959 scopus 로고
    • On diffusion-controlled dissociation
    • Berg O.G. On diffusion-controlled dissociation. Chem. Phys. 1978, 31:47-57.
    • (1978) Chem. Phys. , vol.31 , pp. 47-57
    • Berg, O.G.1
  • 43
    • 33947237358 scopus 로고    scopus 로고
    • Accessible NMR experiments studying the hydrodynamics of 15N-enriched ubiquitin at low fields
    • Thompson L.E., Rovnyak D. Accessible NMR experiments studying the hydrodynamics of 15N-enriched ubiquitin at low fields. Biochem. Mol. Biol. Educ. 2007, 35:49-56.
    • (2007) Biochem. Mol. Biol. Educ. , vol.35 , pp. 49-56
    • Thompson, L.E.1    Rovnyak, D.2
  • 44
    • 0027733616 scopus 로고
    • Use of fast protein size-exclusion liquid chromatography to study the unfolding of proteins which denature through the molten globule
    • Uversky V.N. Use of fast protein size-exclusion liquid chromatography to study the unfolding of proteins which denature through the molten globule. Biochemistry 1993, 32:13288-13298.
    • (1993) Biochemistry , vol.32 , pp. 13288-13298
    • Uversky, V.N.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.