A novel affibody-auristatin e conjugate with a potent and selective activity against HER2+ cell lines

Journal of Immunotherapy

Volumn 39, Issue 6, 2016, Pages 223-232

  Sochaj Gregorczyk, Alicja M ^a   Serwotka Suszczak, Anna M ^a   Otlewski, Jacek ^a  

^a UNIVERSITY OF WROC AW   (Poland)

Author keywords

Affibody molecule; Antibody drug conjugates; HER2 overexpression

Indexed keywords

ANTIBODY; AURISTATIN E; CYSTEINE; CYTOTOXIC AGENT; MALEIMIDE; UNCLASSIFIED DRUG; AMINOBENZOIC ACID DERIVATIVE; AURISTATIN; EPIDERMAL GROWTH FACTOR RECEPTOR 2; ERBB2 PROTEIN, HUMAN; IMMUNOTOXIN; MONOCLONAL ANTIBODY; OLIGOPEPTIDE;

ARTICLE; BREAST CANCER CELL LINE; CELL LINE; CONJUGATE; CYTOTOXICITY; DRUG CONJUGATION; HER2 CELL LINE; HUMAN; IC50; NONHUMAN; PRIORITY JOURNAL; ADENOCARCINOMA; ANIMAL; BREAST TUMOR; FEMALE; GENETICS; IMMUNOLOGY; IMMUNOTHERAPY; METABOLISM; MOUSE; PATHOLOGY; PROCEDURES; PROTEIN ENGINEERING; TUMOR CELL LINE;

ADENOCARCINOMA; AMINOBENZOATES; ANIMALS; ANTIBODIES, MONOCLONAL; BREAST NEOPLASMS; CELL LINE, TUMOR; CYTOTOXICITY, IMMUNOLOGIC; FEMALE; HUMANS; IMMUNOTHERAPY; IMMUNOTOXINS; MICE; OLIGOPEPTIDES; PROTEIN ENGINEERING; RECEPTOR, ERBB-2;

EID: 84970007003     PISSN: 15249557     EISSN: 15374513     Source Type: Journal    
DOI: 10.1097/CJI.0000000000000125     Document Type: Article

References (51)

1. Chari RVJ, Miller ML, Widdison WC. Antibody-drug conjugates: an emerging concept in cancer therapy. Angew Chem Int Ed Engl. 2014;53:3796-3827.
2. Panowski S, Bhakta S, Raab H, et al. Site-specific antibody drug conjugates for cancer therapy. MAbs. 2014;6:34-45.
3. Peddi PF, Hurvitz SA. Trastuzumab emtansine: the first targeted chemotherapy for treatment of breast cancer. Futur Oncol. 2013;9:319-326.
4. LoRusso PM, Weiss D, Guardino E, et al. Trastuzumab emtansine: a unique antibody-drug conjugate in development for human epidermal growth factor receptor 2-positive cancer. Clin Cancer Res. 2011;17:6437-6447.
5. Senter PD, Sievers EL. The discovery and development of brentuximab vedotin for use in relapsed Hodgkin lymphoma and systemic anaplastic large cell lymphoma. Nat Biotechnol. 2012;30:631-637.
6. Cortez-Retamozo V, Backmann N, Senter PD, et al. Efficient cancer therapy with a nanobody-based conjugate. Cancer Res. 2004;64:2853-2857.
7. De Meyer T, Muyldermans S, Depicker A. Nanobody-based products as research and diagnostic tools. Trends Biotechnol. 2014;32:263-270.
8. Nelson AL. Antibody fragments: hope and hype. MAbs. 2010;2:77-83.
9. Spiess C, Zhai Q, Carter PJ. Alternative molecular formats and therapeutic applications for bispecific antibodies. Mol Immunol. 2015;67:95-106.
10. Junutula JR, Bhakta S, Raab H, et al. Rapid identification of reactive cysteine residues for site-specific labeling of antibody- Fabs. J Immunol Methods. 2008;332:41-52.
11. Bryden F, Maruani A, Savoie H, et al. Regioselective and stoichiometrically controlled conjugation of photodynamic sensitizers to a HER2 targeting antibody fragment. Bioconjug Chem. 2014;25:611-617.
12. Nilsson B, Moks T, Jansson B, et al. A synthetic IgG-binding domain based on staphylococcal protein A. Protein Eng. 1987;1:107-113.
13. Nord K, Gunneriusson E, Ringdahl J, et al. Binding proteins selected from combinatorial libraries of an α-helical bacterial receptor domain. Nat Biotech. 1997;15:772-777.
14. Nord K, Nilsson J, Nilsson B, et al. A combinatorial library of an α-helical bacterial receptor domain. Protein Eng. 1995;8: 601-608.
15. Nygren PA. Alternative binding proteins: affibody binding proteins developed from a small three-helix bundle scaffold. FEBS J. 2008;275:2668-2676.
16. Slamon DJ, Clark GM, Wong SG, et al. Human breast cancer: correlation of relapse and survival with amplification of the HER-2/neu oncogene. Sci. 1987;235:177-182.
17. Feldwisch J, Tolmachev V, Lendel C, et al. Design of an optimized scaffold for affibody molecules. J Mol Biol. 2010; 398:232-247.
18. Eigenbrot C, Ultsch M, Dubnovitsky A, et al. Structural basis for high-affinity HER2 receptor binding by an engineered protein. Proc Natl Acad Sci U S A. 2010;107:15039-15044.
19. Ekerljung L, Lindborg M, Gedda L, et al. Dimeric HER2- specific affibody molecules inhibit proliferation of the SKBR-3 breast cancer cell line. Biochem Biophys Res Commun. 2008; 377:489-494.
20. 2 increases radiosensitivity in SKBR-3 cells. PLoS One. 2012;7:e49579.
21. Löfblom J, Feldwisch J, Tolmachev V, et al. Affibody molecules: engineered proteins for therapeutic, diagnostic and biotechnological applications. FEBS Lett. 2010;584:2670-2680.
22. Zakrzewska M, Krowarsch D, Wiedlocha A, et al. Highly stable mutants of human fibroblast growth factor-1 exhibit prolonged biological action. J Mol Biol. 2005;352:860-875.
23. Braisted AC, Wells JA. Minimizing a binding domain from protein A. Proc Natl Acad Sci U S A. 1996;93:5688-5692.
24. Trousil S, Hoppmann S, Nguyen QD, et al. Positron emission tomography imaging with 18F-labeled ZHER2:2891 affibody for detection of HER2 expression and pharmacodynamic response to HER2-modulating therapies. Clin Cancer Res. 2014;20: 1632-1643.
25. Francisco JA, Cerveny CG,Meyer DL, et al. cAC10-vcMMAE, an anti-CD30-monomethyl auristatin E conjugate with potent and selective antitumor activity. Blood. 2003;102:1458-1465.
26. Doronina SO, Toki BE, Torgov MY, et al. Development of potent monoclonal antibody auristatin conjugates for cancer therapy. Nat Biotechnol. 2003;21:778-784.
27. Sun MMC, Beam KS, Cerveny CG, et al. Reduction-alkylation strategies for the modification of specific monoclonal antibody disulfides. Bioconjug Chem. 2005;16:1282-1290.
28. Sochaj AM, Świderska KW, Otlewski J. Current methods for the synthesis of homogeneous antibody-drug conjugates. Biotechnol Adv. 2015;33:775-784.
29. Ahmad S, Gupta S, Kumar R, et al. Herceptin resistance database for understanding mechanism of resistance in breast cancer patients. Sci Rep. 2014;4:4483.
30. Holliday DL, Speirs V. Choosing the right cell line for breast cancer research. Breast Cancer Res. 2011;13:215.
31. Neve RM, Chin K, Fridlyand J, et al. A collection of breast cancer cell lines for the study of functionally distinct cell subtypes. Cancer Cell. 2006;10:515-527.
32. Casi G, Neri D. Antibody-drug conjugates and small molecule-drug conjugates: opportunities and challenges for the development of selective anticancer cytotoxic agents.JMed Chem. 2015;58:8751-8761.
33. Srinivasarao M, Galliford CV, Low PS. Principles in the design of ligand-targeted cancer therapeutics and imaging agents. Nat Rev Drug Discov. 2015;14:203-219.
34. Borsi L, Balza E, Bestagno M, et al. Selective targeting of tumoral vasculature: comparison of different formats of an antibody (L19) to the ED-B domain of fibronectin. Int J Cancer. 2002;102:75-85.
35. 64Cu-DOTA-trastuzumab PET imaging in patients with HER2-positive breast cancer. J Nucl Med. 2013;54:1869-1875.
36. 18F-FDG. J Nucl Med. 2012;53:939-946.
37. Orlova A, Jonsson A, Rosik D, et al. Site-specific radiometal labeling and improved biodistribution using ABY-027, a novel HER2-targeting affibody molecule-albumin-binding domain fusion protein. J Nucl Med. 2013;54:961-968.
38. Wang Y, Miao Z, Ren G, et al. A novel affibody bioconjugate for dual-modality imaging of ovarian cancer. Chem Commun. 2014;50:12832-12835.
39. Strand J, Nordeman P, Honarvar H, et al. Site-specific radioiodination of HER2-targeting affibody molecules using 4-Iodophenethylmaleimide decreases renal uptake of radioactivity. ChemistryOpen. 2015;4:174-182.
40. 111In-ABY-025 affibody molecule. J Nucl Med. 2014;55:730-735.
41. HER2:V2, a promising affibody-based targeting agent against HER2- expressing tumors: preclinical assessment. J Nucl Med. 2014; 55:1842-1848.
42. 177Lu-labeled HER2- specific affibody molecule. Cancer Res. 2007;67:2773-2782.
43. Zielinski R, Lyakhov I, Jacobs A, et al. Affitoxin-a novel recombinant, HER2-specific, anticancer agent for targeted therapy of HER2-positive tumors. J Immunother. 2009;32:817-825.
44. Zielinski R, Lyakhov I, Hassan M, et al. HER2-affitoxin: a potent therapeutic agent for the treatment of HER2-overexpressing tumors. Clin Cancer Res. 2011;17:5071-5081.
45. HER2:2891-ABD-PE38X8, including a targeting affibody molecule and a half-life extension domain. Int J Oncol. 2015;47: 601-609.
46. Shefet-Carasso L, Benhar I. Antibody-targeted drugs and drug resistance-challenges and solutions. Drug Resist Updat. 2015;18:36-46.
47. Hamblett KJ, Senter PD, Chace DF, et al. Effects of drug loading on the antitumor activity of a monoclonal antibody drug conjugate. Clin Cancer Res. 2004;10:7063-7070.
48. 111In-ABY-025, a second-generation affibody molecule with a fundamentally reengineered scaffold. J Nucl Med. 2010;51:1131-1138.
49. Schellenberger V, Wang CW, Geething NC, et al. A recombinant polypeptide extends the in vivo half-life of peptides and proteins in a tunable manner. Nat Biotechnol. 2009;27:1186-1190.
50. Schlapschy M, Binder U, Börger C, et al. PASylation: a biological alternative to PEGylation for extending the plasma half-life of pharmaceutically active proteins. Protein Eng Des Sel. 2013;26:489-501.
51. Alvarenga L, Zahid M, Tommaso A, et al. Engineering venom's toxin-neutralizing antibody fragments and its therapeutic potential. Toxins (Basel). 2014;6:2541-2567.