메뉴 건너뛰기




Volumn 340, Issue 1, 2005, Pages 74-79

Using surface plasmon resonance to directly determine binding affinities of combinatorially selected cyclopeptides and their linear analogs to a streptavidin chip

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; DISSOCIATION; EQUILIBRIUM CONSTANTS; LIGANDS; PLASMONS; PROTEINS; RESONANCE;

EID: 15544374363     PISSN: 00032697     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ab.2005.01.020     Document Type: Article
Times cited : (20)

References (31)
  • 1
    • 0032497399 scopus 로고    scopus 로고
    • Tight-binding streptavidin ligands from a cyclic peptide library
    • X. Zang, Z. Yu, and Y.-H. Chu Tight-binding streptavidin ligands from a cyclic peptide library Bioorg. Med. Chem. Lett. 8 1998 2327 2332
    • (1998) Bioorg. Med. Chem. Lett. , vol.8 , pp. 2327-2332
    • Zang, X.1    Yu, Z.2    Chu, Y.-H.3
  • 2
    • 0342264386 scopus 로고    scopus 로고
    • Methods of screening combinatorial libraries using immobilized or restrained receptors
    • C.P. Woodbury Jr., and D.L. Venton Methods of screening combinatorial libraries using immobilized or restrained receptors J. Chromatogr. B 725 1999 113 137
    • (1999) J. Chromatogr. B , vol.725 , pp. 113-137
    • Woodbury Jr., C.P.1    Venton, D.L.2
  • 3
    • 0035884143 scopus 로고    scopus 로고
    • High-resolution and high-throughput protocols for measuring drug/human serum albumin interactions using BIACORE
    • R.L. Rich, Y.S.N. Day, T.A. Morton, and D.G. Myszka High-resolution and high-throughput protocols for measuring drug/human serum albumin interactions using BIACORE Anal. Biochem. 296 2001 197 207
    • (2001) Anal. Biochem. , vol.296 , pp. 197-207
    • Rich, R.L.1    Day, Y.S.N.2    Morton, T.A.3    Myszka, D.G.4
  • 4
    • 0036633640 scopus 로고    scopus 로고
    • Optical biosensors in drug discovery
    • M.A. Cooper Optical biosensors in drug discovery Nat. Rev. Drug. Discov. 1 2002 515 528
    • (2002) Nat. Rev. Drug. Discov. , vol.1 , pp. 515-528
    • Cooper, M.A.1
  • 5
    • 2542465914 scopus 로고    scopus 로고
    • SPR for molecular interaction analysis: A review of emerging application areas
    • R. Karlsson SPR for molecular interaction analysis: a review of emerging application areas J. Mol. Recogn. 17 2004 151 161
    • (2004) J. Mol. Recogn. , vol.17 , pp. 151-161
    • Karlsson, R.1
  • 6
    • 0242617623 scopus 로고
    • The properties of streptavidin, a biotin-binding protein produced by streptomycetes
    • L. Chaiet, and F. Wolf The properties of streptavidin, a biotin-binding protein produced by streptomycetes Arch. Biochem. Biophys. 108 1964 1 5
    • (1964) Arch. Biochem. Biophys. , vol.108 , pp. 1-5
    • Chaiet, L.1    Wolf, F.2
  • 8
    • 0026419328 scopus 로고
    • A new type of synthetic peptide library for identifying ligand-binding activity
    • K.S. Lam, S.E. Salmon, E.M. Hersh, V.J. Hruby, W.M. Kazmierski, and R.J. Knapp A new type of synthetic peptide library for identifying ligand-binding activity Nature 354 1991 82 84
    • (1991) Nature , vol.354 , pp. 82-84
    • Lam, K.S.1    Salmon, S.E.2    Hersh, E.M.3    Hruby, V.J.4    Kazmierski, W.M.5    Knapp, R.J.6
  • 9
    • 0028303677 scopus 로고
    • Structure-based design of synthetic azobenzene ligands for streptavidin
    • P.C. Weber, M.W. Pantoliano, D.M. Simons, and F.R. Salemme Structure-based design of synthetic azobenzene ligands for streptavidin J. Am. Chem. Soc. 116 1994 2717 2724
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 2717-2724
    • Weber, P.C.1    Pantoliano, M.W.2    Simons, D.M.3    Salemme, F.R.4
  • 10
  • 11
    • 0028921285 scopus 로고
    • Novel avidin and streptavidin binding sequences found in synthetic peptide libraries
    • S. Ostergaard, P.H. Hansen, M. Olsen, and A. Holm Novel avidin and streptavidin binding sequences found in synthetic peptide libraries FEBS Lett. 362 1995 306 308
    • (1995) FEBS Lett. , vol.362 , pp. 306-308
    • Ostergaard, S.1    Hansen, P.H.2    Olsen, M.3    Holm, A.4
  • 12
    • 0028808005 scopus 로고
    • Screening of cyclic peptide phage libraries identifies ligands that bind streptavidin with high affinities
    • L.B. Giebel, R.T. Cass, D.L. Milligan, D.C. Young, R. Arze, and C.R. Johnson Screening of cyclic peptide phage libraries identifies ligands that bind streptavidin with high affinities Biochemistry 34 1995 15430 15435
    • (1995) Biochemistry , vol.34 , pp. 15430-15435
    • Giebel, L.B.1    Cass, R.T.2    Milligan, D.L.3    Young, D.C.4    Arze, R.5    Johnson, C.R.6
  • 13
    • 0037014692 scopus 로고    scopus 로고
    • A novel peptide-based encoding system for "one-bead one-compound" peptidomimetic and small molecule combinatorial libraries
    • R. Liu, J. Marik, and K.S. Lam A novel peptide-based encoding system for "one-bead one-compound" peptidomimetic and small molecule combinatorial libraries J. Am. Chem. Soc. 124 2002 7678 7680
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 7678-7680
    • Liu, R.1    Marik, J.2    Lam, K.S.3
  • 14
    • 0037951325 scopus 로고    scopus 로고
    • A novel and rapid encoding method based on mass spectrometry for "one-bead one-compound" small molecule combinatorial libraries
    • A. Song, J. Zhang, C.B. Lebrilla, and K.S. Lam A novel and rapid encoding method based on mass spectrometry for "one-bead one-compound" small molecule combinatorial libraries J. Am. Chem. Soc. 125 2003 6180 6188
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 6180-6188
    • Song, A.1    Zhang, J.2    Lebrilla, C.B.3    Lam, K.S.4
  • 16
    • 2442431392 scopus 로고    scopus 로고
    • Encoding method for OBOC small molecule libraries using a biphasic approach for ladder-synthesis of coding tags
    • X. Wang, J. Zhang, A. Song, C.B. Lebrilla, and K.S. Lam Encoding method for OBOC small molecule libraries using a biphasic approach for ladder-synthesis of coding tags J. Am. Chem. Soc. 126 2004 5740 5749
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 5740-5749
    • Wang, X.1    Zhang, J.2    Song, A.3    Lebrilla, C.B.4    Lam, K.S.5
  • 17
    • 0032400532 scopus 로고    scopus 로고
    • Lowering the entropic barrier for binding conformationally flexible inhibitors to enzymes
    • A.R. Khan, J.C. Parrish, M.E. Fraser, W.W. Smith, P.A. Bartlett, and M.N.G. James Lowering the entropic barrier for binding conformationally flexible inhibitors to enzymes Biochemistry 37 1998 16839 16845
    • (1998) Biochemistry , vol.37 , pp. 16839-16845
    • Khan, A.R.1    Parrish, J.C.2    Fraser, M.E.3    Smith, W.W.4    Bartlett, P.A.5    James, M.N.G.6
  • 18
    • 0037067398 scopus 로고    scopus 로고
    • Synthesis of macrocyclic, potential protease inhibitors using a generic scaffold
    • E. Dumez, J.S. Snaith, and R.F.W. Jackson Synthesis of macrocyclic, potential protease inhibitors using a generic scaffold J. Org. Chem. 67 2002 4882 4892
    • (2002) J. Org. Chem. , vol.67 , pp. 4882-4892
    • Dumez, E.1    Snaith, J.S.2    Jackson, R.F.W.3
  • 19
    • 2542528563 scopus 로고    scopus 로고
    • Conformationally constrained peptide analogues of pTyr-Glu-Glu-Ile as inhibitors of the Src SH2 domain binding
    • N.-H. Nam, G. Ye, G. Sun, and K. Parang Conformationally constrained peptide analogues of pTyr-Glu-Glu-Ile as inhibitors of the Src SH2 domain binding J. Med. Chem. 47 2004 3131 3141
    • (2004) J. Med. Chem. , vol.47 , pp. 3131-3141
    • Nam, N.-H.1    Ye, G.2    Sun, G.3    Parang, K.4
  • 20
    • 3242768357 scopus 로고    scopus 로고
    • Macrocyclic diacylglycerol-bis-lactones as conformationally constrained analogues of diacylglycerol-lactones. Interactions with protein kinase C
    • J.-H. Kang, S.Y. Kim, J. Lee, V.E. Marquez, N.E. Lewin, L.V. Pearce, and P.M. Blumberg Macrocyclic diacylglycerol-bis-lactones as conformationally constrained analogues of diacylglycerol-lactones. Interactions with protein kinase C J. Med. Chem. 47 2004 4000 4007
    • (2004) J. Med. Chem. , vol.47 , pp. 4000-4007
    • Kang, J.-H.1    Kim, S.Y.2    Lee, J.3    Marquez, V.E.4    Lewin, N.E.5    Pearce, L.V.6    Blumberg, P.M.7
  • 21
    • 3142691160 scopus 로고    scopus 로고
    • Cyclization increases the antimicrobial activity and selectivity of arginine- and tryptophan-containing hexapeptides
    • M. Dathe, H. Nikolenko, J. Klose, and M. Bienert Cyclization increases the antimicrobial activity and selectivity of arginine- and tryptophan- containing hexapeptides Biochemistry 43 2004 9140 9150
    • (2004) Biochemistry , vol.43 , pp. 9140-9150
    • Dathe, M.1    Nikolenko, H.2    Klose, J.3    Bienert, M.4
  • 22
    • 0001325298 scopus 로고    scopus 로고
    • Macrocyclic peptidomimetics: Potential for drug development
    • R.P. McGeary, and D.P. Fairlie Macrocyclic peptidomimetics: potential for drug development Curr. Opin. Drug Discov. Dev. 1 1998 208 217
    • (1998) Curr. Opin. Drug Discov. Dev. , vol.1 , pp. 208-217
    • McGeary, R.P.1    Fairlie, D.P.2
  • 23
    • 0033566586 scopus 로고    scopus 로고
    • Analysis of the binding of the Fab fragment of monoclonal antibody NC10 to influenza virus N9 neuraminidase from tern and whale using the BIAcore biosensor: Effect of immobilization level and flow rate on kinetic analysis
    • A.A. Kortt, E. Nice, and L.C. Gruen Analysis of the binding of the Fab fragment of monoclonal antibody NC10 to influenza virus N9 neuraminidase from tern and whale using the BIAcore biosensor: effect of immobilization level and flow rate on kinetic analysis Anal. Biochem. 273 1999 133 141
    • (1999) Anal. Biochem. , vol.273 , pp. 133-141
    • Kortt, A.A.1    Nice, E.2    Gruen, L.C.3
  • 24
    • 0025232814 scopus 로고
    • Solid phase peptide synthesis utilizing 9-fluorenylmethoxycarbonyl amino acids
    • G.B. Fields, and R.L. Noble Solid phase peptide synthesis utilizing 9-fluorenylmethoxycarbonyl amino acids Int. J. Pept. Protein Res. 35 1990 161 214
    • (1990) Int. J. Pept. Protein Res. , vol.35 , pp. 161-214
    • Fields, G.B.1    Noble, R.L.2
  • 25
    • 0031983804 scopus 로고    scopus 로고
    • MALDI-MS determination of cyclic peptidomimetic sequences on single beads directed toward the generation of libraries
    • Z. Yu, X.C. Yu, and Y.-H. Chu MALDI-MS determination of cyclic peptidomimetic sequences on single beads directed toward the generation of libraries Tetrahedron Lett. 39 1998 1 4
    • (1998) Tetrahedron Lett. , vol.39 , pp. 1-4
    • Yu, Z.1    Yu, X.C.2    Chu, Y.-H.3
  • 26
    • 0025944815 scopus 로고
    • Immobilization of proteins to carboxy methyl dextran-modified gold surfaces for biospecific analysis in surface plasmon resonance sensors
    • B. Johnsson, S. Lofas, and G. Lindquist Immobilization of proteins to carboxy methyl dextran-modified gold surfaces for biospecific 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
  • 27
    • 0032701484 scopus 로고    scopus 로고
    • Improving biosensor analysis
    • D.G. Myszka Improving biosensor analysis J. Mol. Recogn. 12 1999 279 284
    • (1999) J. Mol. Recogn. , vol.12 , pp. 279-284
    • Myszka, D.G.1
  • 28
    • 0029152204 scopus 로고
    • Structure-based design of high affinity streptavidin binding cyclic peptide ligands containing thioether crosslinks
    • B.A. Katz, C.R. Johnson, and R.T. Cass Structure-based design of high affinity streptavidin binding cyclic peptide ligands containing thioether crosslinks J. Am. Chem. Soc. 117 1995 8541 8547
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 8541-8547
    • Katz, B.A.1    Johnson, C.R.2    Cass, R.T.3
  • 29
    • 0025876152 scopus 로고
    • Kinetic analysis of monoclonal antibody-antigen interactions with a new biosensor based analytical system
    • R. Karlsson, A. Michaelsson, and L. Mattson Kinetic analysis of monoclonal antibody-antigen interactions with a new biosensor based analytical system J. Immunol. Methods 145 1991 229 246
    • (1991) J. Immunol. Methods , vol.145 , pp. 229-246
    • Karlsson, R.1    Michaelsson, A.2    Mattson, L.3
  • 30
    • 0032476812 scopus 로고    scopus 로고
    • Polyvalent interactions in biological systems: Implications for design and use of multivalent ligands and inhibitors
    • M. Mammen, S.K. Choi, and G.M. Whitesides Polyvalent interactions in biological systems: Implications for design and use of multivalent ligands and inhibitors Angew. Chem. Intl. Ed. 37 1998 2754 2794
    • (1998) Angew. Chem. Intl. Ed. , vol.37 , pp. 2754-2794
    • Mammen, M.1    Choi, S.K.2    Whitesides, G.M.3
  • 31
    • 11144266576 scopus 로고    scopus 로고
    • Using surface plasmon resonance to directly identify molecules in a tripeptide library that bind tightly to a vancomycin chip
    • M.-C. Tseng, and Y.-H. Chu Using surface plasmon resonance to directly identify molecules in a tripeptide library that bind tightly to a vancomycin chip Anal. Biochem. 336 2005 172 177
    • (2005) Anal. Biochem. , vol.336 , pp. 172-177
    • Tseng, M.-C.1    Chu, Y.-H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.