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Volumn 8, Issue 2, 2016, Pages 114-119

Recent advances in the construction of antibody-drug conjugates

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODY CONJUGATE; DRUG; MONOCLONAL ANTIBODY;

EID: 84955494300     PISSN: 17554330     EISSN: 17554349     Source Type: Journal    
DOI: 10.1038/nchem.2415     Document Type: Review
Times cited : (287)

References (50)
  • 1
    • 84937416363 scopus 로고
    • Address in pathology, on CHEMIOTHERAPY: Delivered before the seventeenth international congress of medicine
    • Ehrlich, P. Address in pathology, ON CHEMIOTHERAPY: Delivered before the seventeenth international congress of medicine. Brit. Med. J. 2, 353-359 (1913).
    • (1913) Brit. Med. J. , vol.2 , pp. 353-359
    • Ehrlich, P.1
  • 2
    • 84961023030 scopus 로고
    • Effet sur la leucémie 1210 de la souris d'une combinaison par diazotation d'A-méthoptérine et de γ-globulines de hamsters porteurs de cette leucémie par hétérogreffe
    • Mathé, G., Loc, T. B. & Bernard, J. Effet sur la leucémie 1210 de la souris d'une combinaison par diazotation d'A-méthoptérine et de γ-globulines de hamsters porteurs de cette leucémie par hétérogreffe. C.R. Hebd. Séances Acad. Sci. 246, 1626-1628 (1958).
    • (1958) C.R. Hebd. Séances Acad. Sci. , vol.246 , pp. 1626-1628
    • Mathé, G.1    Loc, T.B.2    Bernard, J.3
  • 3
    • 0015333917 scopus 로고
    • Antibody as carrier of chlorambucil
    • Ghose, T. & Nigam, S. P. Antibody as carrier of chlorambucil. Cancer 29, 1398-1400 (1972).
    • (1972) Cancer , vol.29 , pp. 1398-1400
    • Ghose, T.1    Nigam, S.P.2
  • 4
    • 0016831976 scopus 로고
    • Suppression of tumour growth in mice by a drug-antibody conjugate using a novel approach to linkage
    • Rowland, G. F., O'Neill, G. J. & Davies, D. A. L. Suppression of tumour growth in mice by a drug-antibody conjugate using a novel approach to linkage. Nature 255, 487-488 (1975).
    • (1975) Nature , vol.255 , pp. 487-488
    • Rowland, G.F.1    O'Neill, G.J.2    Davies, D.A.L.3
  • 5
    • 0020674198 scopus 로고
    • Localisation and toxicity study of a vindesine-anti-CEA conjugate in patients with advanced cancer
    • Ford, C. H. J. et al. Localisation and toxicity study of a vindesine-anti-CEA conjugate in patients with advanced cancer. Brit. J. Cancer 47, 35-42 (1983).
    • (1983) Brit. J. Cancer , vol.47 , pp. 35-42
    • Ford, C.H.J.1
  • 6
    • 0027218284 scopus 로고
    • Cure of xenografted human carcinomas by Br96-doxorubicin immunoconjugates
    • Trail, P. A. et al. Cure of xenografted human carcinomas by Br96-doxorubicin immunoconjugates. Science 261, 212-215 (1993).
    • (1993) Science , vol.261 , pp. 212-215
    • Trail, P.A.1
  • 7
    • 0028067743 scopus 로고
    • Antibody-targeted drugs for the therapy of cancer
    • Pietersz, G. A. & Krauer, K. Antibody-targeted drugs for the therapy of cancer. J. Drug Target. 2, 183-215 (1994).
    • (1994) J. Drug Target. , vol.2 , pp. 183-215
    • Pietersz, G.A.1    Krauer, K.2
  • 8
    • 0035883042 scopus 로고    scopus 로고
    • Multidrug-resistance phenotype and clinical responses to gemtuzumab ozogamicin
    • Linenberger, M. L. et al. Multidrug-resistance phenotype and clinical responses to gemtuzumab ozogamicin. Blood 98, 988-994 (2001).
    • (2001) Blood , vol.98 , pp. 988-994
    • Linenberger, M.L.1
  • 9
    • 78049515807 scopus 로고    scopus 로고
    • Brentuximab vedotin (SGN-35) for relapsed CD30-positive lymphomas
    • Younes, A. et al. Brentuximab vedotin (SGN-35) for relapsed CD30-positive lymphomas. N. Engl. J. Med. 363, 1812-1821 (2010).
    • (2010) N. Engl. J. Med. , vol.363 , pp. 1812-1821
    • Younes, A.1
  • 10
    • 84863688504 scopus 로고    scopus 로고
    • The discovery and development of brentuximab vedotin for use in relapsed Hodgkin lymphoma and systemic anaplastic large cell lymphoma
    • Senter, P. D. & Sievers, E. L. The discovery and development of brentuximab vedotin for use in relapsed Hodgkin lymphoma and systemic anaplastic large cell lymphoma. Nature Biotechnol. 30, 631-637 (2012).
    • (2012) Nature Biotechnol. , vol.30 , pp. 631-637
    • Senter, P.D.1    Sievers, E.L.2
  • 11
    • 84868520609 scopus 로고    scopus 로고
    • Trastuzumab emtansine for HER2-positive advanced breast cancer
    • Verma, S. et al. Trastuzumab emtansine for HER2-positive advanced breast cancer. N. Engl. J. Med. 367, 1783-1791 (2012).
    • (2012) N. Engl. J. Med. , vol.367 , pp. 1783-1791
    • Verma, S.1
  • 12
    • 80054092983 scopus 로고    scopus 로고
    • Trastuzumab emtansine: A unique antibody-drug conjugate in development for human epidermal growth factor receptor 2-positive cancer
    • Lo Russo, P. M., Weiss, D., Guardino, E., Girish, S. & Sliwkowski, M. X. Trastuzumab emtansine: a unique antibody-drug conjugate in development for human epidermal growth factor receptor 2-positive cancer. Clin. Cancer Res. 17, 6437-6447 (2011).
    • (2011) Clin. Cancer Res. , vol.17 , pp. 6437-6447
    • Lo Russo, P.M.1    Weiss, D.2    Guardino, E.3    Girish, S.4    Sliwkowski, M.X.5
  • 13
    • 84877310777 scopus 로고    scopus 로고
    • Maturing antibody-drug conjugate pipeline hits 30
    • Mullard, A. Maturing antibody-drug conjugate pipeline hits 30. Nature Rev. Drug Discov. 12, 329-332 (2013).
    • (2013) Nature Rev. Drug Discov. , vol.12 , pp. 329-332
    • Mullard, A.1
  • 14
    • 6044223544 scopus 로고    scopus 로고
    • Effects of drug loading on the antitumor activity of a monoclonal antibody drug conjugate
    • Hamblett, K. J. et al. Effects of drug loading on the antitumor activity of a monoclonal antibody drug conjugate. Clin. Cancer Res. 10, 7063-7070 (2004).
    • (2004) Clin. Cancer Res. , vol.10 , pp. 7063-7070
    • Hamblett, K.J.1
  • 15
    • 0032922077 scopus 로고    scopus 로고
    • Antineoplastic efficacy of doxorubicin enzymatically assembled on galactose residues of a monoclonal antibody specific for the carcinoembryonic antigen
    • Stan, A. C., Radu, D. L., Casares, S., Bona, C. A. & Brumeanu, T. D. Antineoplastic efficacy of doxorubicin enzymatically assembled on galactose residues of a monoclonal antibody specific for the carcinoembryonic antigen. Cancer Res. 59, 115-121 (1999).
    • (1999) Cancer Res. , vol.59 , pp. 115-121
    • Stan, A.C.1    Radu, D.L.2    Casares, S.3    Bona, C.A.4    Brumeanu, T.D.5
  • 16
    • 84874300889 scopus 로고    scopus 로고
    • Location matters: Site of conjugation modulates stability and pharmacokinetics of antibody drug conjugates
    • Strop, P. et al. Location matters: site of conjugation modulates stability and pharmacokinetics of antibody drug conjugates. Chem. Biol. 20, 161-167 (2013).
    • (2013) Chem. Biol. , vol.20 , pp. 161-167
    • Strop, P.1
  • 17
    • 0025140678 scopus 로고
    • Site-specific attachment to recombinant antibodies via introduced surface cysteine residues
    • Lyons, A. et al. Site-specific attachment to recombinant antibodies via introduced surface cysteine residues. Protein Eng. 3, 703-708 (1990).
    • (1990) Protein Eng. , vol.3 , pp. 703-708
    • Lyons, A.1
  • 18
    • 49449087300 scopus 로고    scopus 로고
    • Site-specific conjugation of a cytotoxic drug to an antibody improves the therapeutic index
    • Junutula, J. R. et al. Site-specific conjugation of a cytotoxic drug to an antibody improves the therapeutic index. Nature Biotechnol. 26, 925-932 (2008).
    • (2008) Nature Biotechnol. , vol.26 , pp. 925-932
    • Junutula, J.R.1
  • 19
    • 70349266046 scopus 로고    scopus 로고
    • Site specific protein labeling by enzymatic posttranslational modification
    • Sunbul, M. & Yin, J. Site specific protein labeling by enzymatic posttranslational modification. Org. Biomol. Chem. 7, 3361-3371 (2009).
    • (2009) Org. Biomol. Chem. , vol.7 , pp. 3361-3371
    • Sunbul, M.1    Yin, J.2
  • 20
    • 73149104141 scopus 로고    scopus 로고
    • An enhanced system for unnatural amino acid mutagenesis in E. Coli
    • Young, T. S., Ahmad, I., Yin, J. A. & Schultz, P. G. An enhanced system for unnatural amino acid mutagenesis in E. coli. J. Mol. Biol. 395, 361-374 (2010).
    • (2010) J. Mol. Biol. , vol.395 , pp. 361-374
    • Young, T.S.1    Ahmad, I.2    Yin, J.A.3    Schultz, P.G.4
  • 21
    • 84861034877 scopus 로고    scopus 로고
    • Site-specific chemical protein conjugation using genetically encoded aldehyde tags
    • Rabuka, D., Rush, J. S., de Hart, G. W., Wu, P. & Bertozzi, C. R. Site-specific chemical protein conjugation using genetically encoded aldehyde tags. Nature Protoc. 7, 1052-1067 (2012).
    • (2012) Nature Protoc. , vol.7 , pp. 1052-1067
    • Rabuka, D.1    Rush, J.S.2    De Hart, G.W.3    Wu, P.4    Bertozzi, C.R.5
  • 22
    • 84867040452 scopus 로고    scopus 로고
    • Synthesis of site-specific antibody-drug conjugates using unnatural amino acids
    • Axup, J. Y. et al. Synthesis of site-specific antibody-drug conjugates using unnatural amino acids. Proc. Natl Acad. Sci. USA 109, 16101-16106 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 16101-16106
    • Axup, J.Y.1
  • 23
    • 40649126110 scopus 로고    scopus 로고
    • Rapid identification of reactive cysteine residues for site-specific labeling of antibody-Fabs
    • Junutula, J. R. et al. Rapid identification of reactive cysteine residues for site-specific labeling of antibody-Fabs. J. Immunol. Methods 332, 41-52 (2008).
    • (2008) J. Immunol. Methods , vol.332 , pp. 41-52
    • Junutula, J.R.1
  • 24
    • 0026095012 scopus 로고
    • Carbohydrate-binding protein 35 (Mac-2), a laminin-binding lectin, forms functional dimers using cysteine 186
    • Woo, H. J., Lotz, M. M., Jung, J. U. & Mercurio, A. M. Carbohydrate-binding protein 35 (Mac-2), a laminin-binding lectin, forms functional dimers using cysteine 186. J. Biol. Chem. 266, 18419-18422 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 18419-18422
    • Woo, H.J.1    Lotz, M.M.2    Jung, J.U.3    Mercurio, A.M.4
  • 25
    • 0037383418 scopus 로고    scopus 로고
    • Homo-oligomerization of the porcine reproductive and respiratory syndrome virus nucleocapsid protein and the role of disulfide linkages
    • Wootton, S. K. & Yoo, D. Homo-oligomerization of the porcine reproductive and respiratory syndrome virus nucleocapsid protein and the role of disulfide linkages. J. Virol. 77, 4546-4557 (2003).
    • (2003) J. Virol. , vol.77 , pp. 4546-4557
    • Wootton, S.K.1    Yoo, D.2
  • 26
    • 0026338017 scopus 로고
    • Transglutaminases: Multifunctional cross-linking enzymes that stabilize tissues
    • Greenberg, C. S., Birckbichler, P. J. & Rice, R. H. Transglutaminases: multifunctional cross-linking enzymes that stabilize tissues. FASEB J. 5, 3071-3077 (1991).
    • (1991) FASEB J. , vol.5 , pp. 3071-3077
    • Greenberg, C.S.1    Birckbichler, P.J.2    Rice, R.H.3
  • 27
    • 0027223075 scopus 로고
    • Primary structure of microbial transglutaminase from Streptoverticillium sp. Strain s-8112
    • Kanaji, T. et al. Primary structure of microbial transglutaminase from Streptoverticillium sp. strain s-8112. J. Biol. Chem. 268, 11565-11572 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 11565-11572
    • Kanaji, T.1
  • 28
    • 0037114005 scopus 로고    scopus 로고
    • Crystal structure of microbial transglutaminase from Streptoverticillium mobaraense
    • Kashiwagi, T. et al. Crystal structure of microbial transglutaminase from Streptoverticillium mobaraense. J. Biol. Chem. 277, 44252-44260 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 44252-44260
    • Kashiwagi, T.1
  • 29
    • 78650297318 scopus 로고    scopus 로고
    • Site-specific and stoichiometric modification of antibodies by bacterial transglutaminase
    • Jeger, S. et al. Site-specific and stoichiometric modification of antibodies by bacterial transglutaminase. Angew. Chem. Int. Ed. 49, 9995-9997 (2010).
    • (2010) Angew. Chem. Int. Ed. , vol.49 , pp. 9995-9997
    • Jeger, S.1
  • 30
    • 62549121136 scopus 로고    scopus 로고
    • Site-specific chemical modification of recombinant proteins produced in mammalian cells by using the genetically encoded aldehyde tag
    • Wu, P. et al. Site-specific chemical modification of recombinant proteins produced in mammalian cells by using the genetically encoded aldehyde tag. Proc. Natl Acad. Sci. USA 106, 3000-3005 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 3000-3005
    • Wu, P.1
  • 31
    • 84904408813 scopus 로고    scopus 로고
    • Aldehyde tag coupled with HIPS chemistry enables the production of ADCs conjugated site-specifically to different antibody regions with distinct in vivo efficacy and PK outcomes
    • Drake, P. M. et al. Aldehyde tag coupled with HIPS chemistry enables the production of ADCs conjugated site-specifically to different antibody regions with distinct in vivo efficacy and PK outcomes. Bioconjugate Chem. 25, 1331-1341 (2014).
    • (2014) Bioconjugate Chem. , vol.25 , pp. 1331-1341
    • Drake, P.M.1
  • 32
    • 84894445908 scopus 로고    scopus 로고
    • Production of site-specific antibody-drug conjugates using optimized non-natural amino acids in a cell-free expression system
    • Zimmerman, E. S. et al. Production of site-specific antibody-drug conjugates using optimized non-natural amino acids in a cell-free expression system. Bioconjugate Chem. 25, 351-361 (2014).
    • (2014) Bioconjugate Chem. , vol.25 , pp. 351-361
    • Zimmerman, E.S.1
  • 33
    • 84872529363 scopus 로고    scopus 로고
    • Long-term tumor regression induced by an antibody-drug conjugate that targets 5T4, an oncofetal antigen expressed on tumor-initiating cells
    • Sapra, P. et al. Long-term tumor regression induced by an antibody-drug conjugate that targets 5T4, an oncofetal antigen expressed on tumor-initiating cells. Mol. Cancer Ther. 12, 38-47 (2013).
    • (2013) Mol. Cancer Ther. , vol.12 , pp. 38-47
    • Sapra, P.1
  • 34
    • 84893452692 scopus 로고    scopus 로고
    • A general approach to site-specific antibody drug conjugates
    • Tian, F. et al. A general approach to site-specific antibody drug conjugates. Proc. Natl Acad. Sci. USA 111, 1766-1771 (2014).
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. 1766-1771
    • Tian, F.1
  • 35
    • 25444507922 scopus 로고    scopus 로고
    • Reduction-alkylation strategies for the modification of specific monoclonal antibody disulfides
    • Sun, M. M. et al. Reduction-alkylation strategies for the modification of specific monoclonal antibody disulfides. Bioconjugate Chem. 16, 1282-1290 (2005).
    • (2005) Bioconjugate Chem. , vol.16 , pp. 1282-1290
    • Sun, M.M.1
  • 36
    • 10744222473 scopus 로고    scopus 로고
    • Development of potent monoclonal antibody auristatin conjugates for cancer therapy
    • Doronina, S. O. et al. Development of potent monoclonal antibody auristatin conjugates for cancer therapy. Nature Biotechnol. 21, 778-784 (2003).
    • (2003) Nature Biotechnol. , vol.21 , pp. 778-784
    • Doronina, S.O.1
  • 37
  • 38
    • 84863012529 scopus 로고    scopus 로고
    • Conjugation site modulates the in vivo stability and therapeutic activity of antibody-drug conjugates
    • Shen, B. Q. et al. Conjugation site modulates the in vivo stability and therapeutic activity of antibody-drug conjugates. Nature Biotechnol. 30, 184-189 (2012).
    • (2012) Nature Biotechnol. , vol.30 , pp. 184-189
    • Shen, B.Q.1
  • 39
    • 84921407368 scopus 로고    scopus 로고
    • Self-hydrolyzing maleimides improve the stability and pharmacological properties of antibody-drug conjugates
    • Lyon, R. P. et al. Self-hydrolyzing maleimides improve the stability and pharmacological properties of antibody-drug conjugates. Nature Biotechnol. 32, 1059-1062 (2014).
    • (2014) Nature Biotechnol. , vol.32 , pp. 1059-1062
    • Lyon, R.P.1
  • 40
    • 84902660348 scopus 로고    scopus 로고
    • Bridging disulfides for stable and defined antibody drug conjugates
    • Badescu, G. et al. Bridging disulfides for stable and defined antibody drug conjugates. Bioconjugate Chem. 25, 1124-1136 (2014).
    • (2014) Bioconjugate Chem. , vol.25 , pp. 1124-1136
    • Badescu, G.1
  • 41
    • 84934976018 scopus 로고    scopus 로고
    • Functional native disulfide bridging enables delivery of a potent, stable and targeted antibody-drug conjugate (ADC)
    • Nunes, J. P. M. et al. Functional native disulfide bridging enables delivery of a potent, stable and targeted antibody-drug conjugate (ADC). Chem. Commun. 51, 10624-10627 (2015).
    • (2015) Chem. Commun. , vol.51 , pp. 10624-10627
    • Nunes, J.P.M.1
  • 42
    • 84926284885 scopus 로고    scopus 로고
    • A plug-and-play approach to antibody-based therapeutics via a chemoselective dual click strategy
    • Maruani, A. et al. A plug-and-play approach to antibody-based therapeutics via a chemoselective dual click strategy. Nature Commun. 6, 7645 (2015).
    • (2015) Nature Commun. , vol.6 , pp. 7645
    • Maruani, A.1
  • 43
    • 84943801701 scopus 로고    scopus 로고
    • Site-selective multi-porphyrin attachment enables the formation of a next-generation antibody-based photodynamic therapeutic
    • Maruani, A. et al. Site-selective multi-porphyrin attachment enables the formation of a next-generation antibody-based photodynamic therapeutic. Chem. Commun. 51, 15304-15307 (2015).
    • (2015) Chem. Commun. , vol.51 , pp. 15304-15307
    • Maruani, A.1
  • 44
    • 84951196784 scopus 로고    scopus 로고
    • Next-generation disulfide stapling: Reduction and functional re-bridging all in one
    • Lee, M. T. W., Maruani, A., Baker, J., Caddick, S. & Chudasama, V. Next-generation disulfide stapling: Reduction and functional re-bridging all in one. Chem. Sci. 7, 799-802 (2016).
    • (2016) Chem. Sci. , vol.7 , pp. 799-802
    • Lee, M.T.W.1    Maruani, A.2    Baker, J.3    Caddick, S.4    Chudasama, V.5
  • 45
    • 0027194197 scopus 로고
    • Preparation and characterization of monoclonal antibody conjugates of the calicheamicins: A novel and potent family of antitumor antibiotics
    • Hinman, L. M. et al. Preparation and characterization of monoclonal antibody conjugates of the calicheamicins: a novel and potent family of antitumor antibiotics. Cancer Res. 53, 3336-3342 (1993).
    • (1993) Cancer Res. , vol.53 , pp. 3336-3342
    • Hinman, L.M.1
  • 46
    • 20144375952 scopus 로고    scopus 로고
    • An anti-MUC1 antibody-calicheamicin conjugate for treatment of solid tumors. Choice of linker and overcoming drug resistance
    • Hamann, P. R. et al. An anti-MUC1 antibody-calicheamicin conjugate for treatment of solid tumors. Choice of linker and overcoming drug resistance. Bioconjugate Chem. 16, 346-353 (2005).
    • (2005) Bioconjugate Chem. , vol.16 , pp. 346-353
    • Hamann, P.R.1
  • 47
    • 79951552251 scopus 로고    scopus 로고
    • Impact of methionine oxidation in human IgG1 Fc on serum half-life of monoclonal antibodies
    • Wang, W. et al. Impact of methionine oxidation in human IgG1 Fc on serum half-life of monoclonal antibodies. Mol. Immunol. 48, 860-866 (2011).
    • (2011) Mol. Immunol. , vol.48 , pp. 860-866
    • Wang, W.1
  • 48
    • 84896537748 scopus 로고    scopus 로고
    • Site-specific antibody-drug conjugation through glycoengineering
    • Zhou, Q. et al. Site-specific antibody-drug conjugation through glycoengineering. Bioconjugate Chem. 25, 510-520 (2014).
    • (2014) Bioconjugate Chem. , vol.25 , pp. 510-520
    • Zhou, Q.1
  • 49
    • 84903715027 scopus 로고    scopus 로고
    • Preparation of well-defined antibody-drug conjugates through glycan remodeling and strain-promoted azide-alkyne cycloadditions
    • Li, X., Fang, T. & Boons, G. J. Preparation of well-defined antibody-drug conjugates through glycan remodeling and strain-promoted azide-alkyne cycloadditions. Angew. Chem. Int. Ed. 53, 7179-7182 (2014).
    • (2014) Angew. Chem. Int. Ed. , vol.53 , pp. 7179-7182
    • Li, X.1    Fang, T.2    Boons, G.J.3
  • 50
    • 13544276336 scopus 로고    scopus 로고
    • Glycosylation of recombinant antibody therapeutics
    • Jefferis, R. Glycosylation of recombinant antibody therapeutics. Biotechnol. Prog. 21, 11-16 (2005).
    • (2005) Biotechnol. Prog. , vol.21 , pp. 11-16
    • Jefferis, R.1


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