메뉴 건너뛰기




Volumn 27, Issue 1, 2016, Pages 159-169

Covalent Chemical Ligation Strategy for Mono- and Polyclonal Immunoglobulins at Their Nucleotide Binding Sites

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BINDING SITES; NUCLEOTIDES;

EID: 84956839369     PISSN: 10431802     EISSN: 15204812     Source Type: Journal    
DOI: 10.1021/acs.bioconjchem.5b00574     Document Type: Article
Times cited : (17)

References (43)
  • 1
    • 0035524114 scopus 로고    scopus 로고
    • Improving the efficacy of antibody-based cancer therapies
    • Carter, P. (2001) Improving the efficacy of antibody-based cancer therapies Nature Reviews Cancer 1, 118-129 10.1038/35101072
    • (2001) Nature Reviews Cancer , vol.1 , pp. 118-129
    • Carter, P.1
  • 3
    • 27144550160 scopus 로고    scopus 로고
    • Arming antibodies: prospects and challenges for immunoconjugates
    • Wu, A. M. and Senter, P. D. (2005) Arming antibodies: prospects and challenges for immunoconjugates Nat. Biotechnol. 23, 1137-1146 10.1038/nbt1141
    • (2005) Nat. Biotechnol. , vol.23 , pp. 1137-1146
    • Wu, A.M.1    Senter, P.D.2
  • 4
    • 84923228905 scopus 로고    scopus 로고
    • Site-specific antibody-drug conjugates: the nexus of bioorthogonal chemistry, protein engineering, and drug development
    • Agarwal, P. and Bertozzi, C. R. (2015) Site-specific antibody-drug conjugates: the nexus of bioorthogonal chemistry, protein engineering, and drug development Bioconjugate Chem. 26, 176-92 10.1021/bc5004982
    • (2015) Bioconjugate Chem. , vol.26 , pp. 176-192
    • Agarwal, P.1    Bertozzi, C.R.2
  • 5
    • 84892615120 scopus 로고    scopus 로고
    • Site-specific antibody drug conjugates for cancer therapy
    • Panowski, S., Bhakta, S., Raab, H., Polakis, P., and Junutula, J. R. (2014) Site-specific antibody drug conjugates for cancer therapy mAbs 6, 34-45 10.4161/mabs.27022
    • (2014) MAbs , vol.6 , pp. 34-45
    • Panowski, S.1    Bhakta, S.2    Raab, H.3    Polakis, P.4    Junutula, J.R.5
  • 7
    • 84868561570 scopus 로고    scopus 로고
    • U.S. Food and Drug Administration Approval Summary: Brentuximab Vedotin for the Treatment of Relapsed Hodgkin Lymphoma or Relapsed Systemic Anaplastic Large-Cell Lymphoma
    • de Claro, R. A., McGinn, K., Kwitkowski, V., Bullock, J., Khandelwal, A., Habtemariam, B., Ouyang, Y. L., Saber, H., Lee, K., and Koti, K. et al. 2012, U.S. Food and Drug Administration Approval Summary: Brentuximab Vedotin for the Treatment of Relapsed Hodgkin Lymphoma or Relapsed Systemic Anaplastic Large-Cell Lymphoma Clin. Cancer Res. 18, 5845-5849 10.1158/1078-0432.CCR-12-1803
    • (2012) Clin. Cancer Res. , vol.18 , pp. 5845-5849
    • De Claro, R.A.1    McGinn, K.2    Kwitkowski, V.3    Bullock, J.4    Khandelwal, A.5    Habtemariam, B.6    Ouyang, Y.L.7    Saber, H.8    Lee, K.9    Koti, K.10
  • 9
    • 84910150181 scopus 로고    scopus 로고
    • Recent Advances in Antibody-Drug Conjugates
    • (Jones, L. H. and McKnight, A. J. Eds.) Royal Society of Chemistry, Cambridge
    • Graziani, E. I. and Tumey, L. N. (2013) Recent Advances in Antibody-Drug Conjugates, in Biotherapeutics: Recent Developments Using Chemical and Molecular Biology (Jones, L. H. and McKnight, A. J., Eds.) pp 145-175, Royal Society of Chemistry, Cambridge.
    • (2013) Biotherapeutics: Recent Developments Using Chemical and Molecular Biology , pp. 145-175
    • Graziani, E.I.1    Tumey, L.N.2
  • 11
    • 50449091735 scopus 로고    scopus 로고
    • An engineered selenocysteine defines a unique class of antibody derivatives
    • Hofer, T., Thomas, J. D., Burke, T. R., and Rader, C. (2008) An engineered selenocysteine defines a unique class of antibody derivatives Proc. Natl. Acad. Sci. U. S. A. 105, 12451-12456 10.1073/pnas.0800800105
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 12451-12456
    • Hofer, T.1    Thomas, J.D.2    Burke, T.R.3    Rader, C.4
  • 14
    • 78649499554 scopus 로고    scopus 로고
    • Identification of Highly Reactive Sequences for PLP-Mediated Bioconjugation Using a Combinatorial Peptide Library
    • Witus, L. S., Moore, T., Thuronyi, B. W., Esser-Kahn, A. P., Scheck, R. A., Iavarone, A. T., and Francis, M. B. (2010) Identification of Highly Reactive Sequences For PLP-Mediated Bioconjugation Using a Combinatorial Peptide Library J. Am. Chem. Soc. 132, 16812-16817 10.1021/ja105429n
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 16812-16817
    • Witus, L.S.1    Moore, T.2    Thuronyi, B.W.3    Esser-Kahn, A.P.4    Scheck, R.A.5    Iavarone, A.T.6    Francis, M.B.7
  • 16
    • 76149123221 scopus 로고    scopus 로고
    • Tyrosine Bioconjugation through Aqueous Ene-Type Reactions: A Click-Like Reaction for Tyrosine
    • Ban, H., Gavrilyuk, J., and Barbas, C. F. (2010) Tyrosine Bioconjugation through Aqueous Ene-Type Reactions: A Click-Like Reaction for Tyrosine J. Am. Chem. Soc. 132, 1523-1525 10.1021/ja909062q
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 1523-1525
    • Ban, H.1    Gavrilyuk, J.2    Barbas, C.F.3
  • 17
    • 84871307240 scopus 로고    scopus 로고
    • Formylbenzene Diazonium Hexafluorophosphate Reagent for Tyrosine-Selective Modification of Proteins and the Introduction of a Bioorthogonal Aldehyde
    • Gavrilyuk, J., Ban, H., Nagano, M., Hakamata, W., and Barbas, C. F. (2012) Formylbenzene Diazonium Hexafluorophosphate Reagent for Tyrosine-Selective Modification of Proteins and the Introduction of a Bioorthogonal Aldehyde Bioconjugate Chem. 23, 2321-2328 10.1021/bc300410p
    • (2012) Bioconjugate Chem. , vol.23 , pp. 2321-2328
    • Gavrilyuk, J.1    Ban, H.2    Nagano, M.3    Hakamata, W.4    Barbas, C.F.5
  • 18
    • 0034705643 scopus 로고    scopus 로고
    • Use of microbial transglutaminase for the enzymatic biotinylation of antibodies
    • Josten, A. E., Haalck, L., Spener, F., and Meusel, M. (2000) Use of microbial transglutaminase for the enzymatic biotinylation of antibodies J. Immunol. Methods 240, 47-54 10.1016/S0022-1759(00)00172-1
    • (2000) J. Immunol. Methods , vol.240 , pp. 47-54
    • Josten, A.E.1    Haalck, L.2    Spener, F.3    Meusel, M.4
  • 19
    • 0041429215 scopus 로고    scopus 로고
    • Site-specific cross-linking of functional proteins by transglutamination
    • Kamiya, N., Takazawa, T., Tanaka, T., Ueda, H., and Nagamune, T. (2003) Site-specific cross-linking of functional proteins by transglutamination Enzyme Microb. Technol. 33, 492-496 10.1016/S0141-0229(03)00154-6
    • (2003) Enzyme Microb. Technol. , vol.33 , pp. 492-496
    • Kamiya, N.1    Takazawa, T.2    Tanaka, T.3    Ueda, H.4    Nagamune, T.5
  • 20
    • 38949104404 scopus 로고    scopus 로고
    • Modification of different IgG1 antibodies via glutamine and lysine using bacterial and human tissue transglutaminase
    • Mindt, T. L., Jungi, V., Wyss, S., Friedli, A., Pla, G., Novak-Hofer, I., Grunberg, J., and Schibli, R. (2008) Modification of different IgG1 antibodies via glutamine and lysine using bacterial and human tissue transglutaminase Bioconjugate Chem. 19, 271-278 10.1021/bc700306n
    • (2008) Bioconjugate Chem. , vol.19 , pp. 271-278
    • Mindt, T.L.1    Jungi, V.2    Wyss, S.3    Friedli, A.4    Pla, G.5    Novak-Hofer, I.6    Grunberg, J.7    Schibli, R.8
  • 21
    • 33747880302 scopus 로고    scopus 로고
    • N-terminal protein modification through a biomimetic transamination reaction
    • Gilmore, J. M., Scheck, R. A., Esser-Kahn, A. P., Joshi, N. S., and Francis, M. B. (2006) N-terminal protein modification through a biomimetic transamination reaction Angew. Chem., Int. Ed. 45, 5307-5311 10.1002/anie.200600368
    • (2006) Angew. Chem., Int. Ed. , vol.45 , pp. 5307-5311
    • Gilmore, J.M.1    Scheck, R.A.2    Esser-Kahn, A.P.3    Joshi, N.S.4    Francis, M.B.5
  • 24
    • 84879530135 scopus 로고    scopus 로고
    • Oriented antibody immobilization by site-specific UV photocrosslinking of biotin at the conserved nucleotide binding site for enhanced antigen detection
    • Alves, N. J., Mustafaoglu, N., and Bilgicer, B. (2013) Oriented antibody immobilization by site-specific UV photocrosslinking of biotin at the conserved nucleotide binding site for enhanced antigen detection Biosens. Bioelectron. 49, 387-393 10.1016/j.bios.2013.05.052
    • (2013) Biosens. Bioelectron. , vol.49 , pp. 387-393
    • Alves, N.J.1    Mustafaoglu, N.2    Bilgicer, B.3
  • 25
    • 80053150163 scopus 로고    scopus 로고
    • Design of a heterobivalent ligand to inhibit IgE clustering on mast cells
    • Handlogten, M. W., Kiziltepe, T., Moustakas, D. T., and Bilgicer, B. (2011) Design of a heterobivalent ligand to inhibit IgE clustering on mast cells Chem. Biol. 18, 1179-1188 10.1016/j.chembiol.2011.06.012
    • (2011) Chem. Biol. , vol.18 , pp. 1179-1188
    • Handlogten, M.W.1    Kiziltepe, T.2    Moustakas, D.T.3    Bilgicer, B.4
  • 26
    • 84866412630 scopus 로고    scopus 로고
    • Small-molecule-based affinity chromatography method for antibody purification via nucleotide binding site targeting
    • Alves, N. J., Stimple, S. D., Handlogten, M. W., Ashley, J. D., Kiziltepe, T., and Bilgicer, B. (2012) Small-molecule-based affinity chromatography method for antibody purification via nucleotide binding site targeting Anal. Chem. 84, 7721-8 10.1021/ac300952r
    • (2012) Anal. Chem. , vol.84 , pp. 7721-7728
    • Alves, N.J.1    Stimple, S.D.2    Handlogten, M.W.3    Ashley, J.D.4    Kiziltepe, T.5    Bilgicer, B.6
  • 28
    • 0037434791 scopus 로고    scopus 로고
    • Structure of the extracellular region of HER2 alone and in complex with the Herceptin Fab
    • Cho, H. S., Mason, K., Ramyar, K. X., Stanley, A. M., Gabelli, S. B., Denney, D. W., and Leahy, D. J. (2003) Structure of the extracellular region of HER2 alone and in complex with the Herceptin Fab Nature 421, 756-760 10.1038/nature01392
    • (2003) Nature , vol.421 , pp. 756-760
    • Cho, H.S.1    Mason, K.2    Ramyar, K.X.3    Stanley, A.M.4    Gabelli, S.B.5    Denney, D.W.6    Leahy, D.J.7
  • 30
    • 0026419328 scopus 로고
    • A new type of synthetic peptide library for identifying ligand-binding activity
    • Lam, K. S., Salmon, S. E., Hersh, E. M., Hruby, V. J., Kazmierski, W. M., and Knapp, R. J. (1991) A new type of synthetic peptide library for identifying ligand-binding activity Nature 354, 82-4 10.1038/354082a0
    • (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
  • 31
    • 33746330426 scopus 로고    scopus 로고
    • Image subtraction approach to screening one-bead-one-compound combinatorial libraries with complex protein mixtures
    • Lehman, A., Gholami, S., Hahn, M., and Lam, K. S. (2006) Image subtraction approach to screening one-bead-one-compound combinatorial libraries with complex protein mixtures J. Comb. Chem. 8, 562-570 10.1021/cc0600268
    • (2006) J. Comb. Chem. , vol.8 , pp. 562-570
    • Lehman, A.1    Gholami, S.2    Hahn, M.3    Lam, K.S.4
  • 33
    • 84904421553 scopus 로고    scopus 로고
    • Conjugation of a reactive thiol at the nucleotide binding site for site-specific antibody functionalization
    • Alves, N. J., Mustafaoglu, N., and Bilgicer, B. (2014) Conjugation of a reactive thiol at the nucleotide binding site for site-specific antibody functionalization Bioconjugate Chem. 25, 1198-202 10.1021/bc500211d
    • (2014) Bioconjugate Chem. , vol.25 , pp. 1198-1202
    • Alves, N.J.1    Mustafaoglu, N.2    Bilgicer, B.3
  • 34
    • 84879530135 scopus 로고    scopus 로고
    • Oriented antibody immobilization by site-specific UV photocrosslinking of biotin at the conserved nucleotide binding site for enhanced antigen detection
    • Alves, N. J., Mustafaoglu, N., and Bilgicer, B. (2013) Oriented antibody immobilization by site-specific UV photocrosslinking of biotin at the conserved nucleotide binding site for enhanced antigen detection Biosens. Bioelectron. 49, 387-93 10.1016/j.bios.2013.05.052
    • (2013) Biosens. Bioelectron. , vol.49 , pp. 387-393
    • Alves, N.J.1    Mustafaoglu, N.2    Bilgicer, B.3
  • 35
    • 84865235085 scopus 로고    scopus 로고
    • Chemically programmed bispecific antibodies that recruit and activate T Cells
    • Cui, H. T., Thomas, J. D., Burke, T. R., and Rader, C. (2012) Chemically programmed bispecific antibodies that recruit and activate T Cells J. Biol. Chem. 287, 28206-28214 10.1074/jbc.M112.384594
    • (2012) J. Biol. Chem. , vol.287 , pp. 28206-28214
    • Cui, H.T.1    Thomas, J.D.2    Burke, T.R.3    Rader, C.4
  • 38
    • 84874300889 scopus 로고    scopus 로고
    • Location matters: site of conjugation modulates stability and pharmacokinetics of antibody drug conjugates
    • Strop, P., Liu, S. H., Dorywalska, M., Delaria, K., Dushin, R. G., Tran, T. T., Ho, W. H., Farias, S., Casas, M. G., and Abdiche, Y. et al. 2013, Location matters: site of conjugation modulates stability and pharmacokinetics of antibody drug conjugates Chem. Biol. 20, 161-7 10.1016/j.chembiol.2013.01.010
    • (2013) Chem. Biol. , vol.20 , pp. 161-167
    • Strop, P.1    Liu, S.H.2    Dorywalska, M.3    Delaria, K.4    Dushin, R.G.5    Tran, T.T.6    Ho, W.H.7    Farias, S.8    Casas, M.G.9    Abdiche, Y.10
  • 39
    • 84875446702 scopus 로고    scopus 로고
    • Brentuximab vedotin: an anti-CD30 antibody-drug conjugate
    • Bradley, A. M., Devine, M., and DeRemer, D. (2013) Brentuximab vedotin: an anti-CD30 antibody-drug conjugate Am. J. Health-Syst. Pharm. 70, 589-97 10.2146/ajhp110608
    • (2013) Am. J. Health-Syst. Pharm. , vol.70 , pp. 589-597
    • Bradley, A.M.1    Devine, M.2    Deremer, D.3
  • 40
    • 0019525292 scopus 로고
    • Minimization by Random Search Techniques
    • Solis, F. J. and Wets, R. J. B. (1981) Minimization by Random Search Techniques Math. Oper. Res. 6, 19-30 10.1287/moor.6.1.19
    • (1981) Math. Oper. Res. , vol.6 , pp. 19-30
    • Solis, F.J.1    Wets, R.J.B.2
  • 41
    • 79960029361 scopus 로고    scopus 로고
    • SwissDock, a protein-small molecule docking web service based on EADock DSS
    • Grosdidier, A., Zoete, V., and Michielin, O. (2011) SwissDock, a protein-small molecule docking web service based on EADock DSS Nucleic Acids Res. 39, W270-7 10.1093/nar/gkr366
    • (2011) Nucleic Acids Res. , vol.39 , pp. W270-W277
    • Grosdidier, A.1    Zoete, V.2    Michielin, O.3
  • 42
    • 79958242366 scopus 로고    scopus 로고
    • Fast docking using the CHARMM force field with EADock DSS
    • Grosdidier, A., Zoete, V., and Michielin, O. (2011) Fast docking using the CHARMM force field with EADock DSS J. Comput. Chem. 32, 2149-2159 10.1002/jcc.21797
    • (2011) J. Comput. Chem. , vol.32 , pp. 2149-2159
    • Grosdidier, A.1    Zoete, V.2    Michielin, O.3
  • 43
    • 0037571112 scopus 로고    scopus 로고
    • Merck molecular force field 0.1. Basis, form, scope, parameterization, and performance of MMFF94
    • Halgren, T. A. (1996) Merck molecular force field 0.1. Basis, form, scope, parameterization, and performance of MMFF94 J. Comput. Chem. 17, 490-519 10.1002/(SICI)1096-987X(199604)17:5/6<490::AID-JCC1>3.0.CO;2-P
    • (1996) J. Comput. Chem. , vol.17 , pp. 490-519
    • Halgren, T.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.