Biosimilars of Monoclonal Antibodies: A Practical Guide to Manufacturing, Preclinical and Clinical Development

Addressing a significant need by describing the science and process involved to develop biosimilars of monoclonal antibody (mAb) drugs, this book covers all aspects of biosimilar development: preclinical, clinical, regulatory, manufacturing.  Guides readers through the complex landscape involved with developing biosimilar versions of monoclonal antibody (mAb) drugs  Features flow charts, tables, and figures that clearly illustrate processes and makes the book comprehensible and accessible  Includes a review of FDA–approved mAb drugs as a quick reference to facts and useful information  Examines new technologies and strategies for improving biosimilar mAbs INDICE: Notes on Contributors .Preface .Chapter 1: The History of Therapeutic Monoclonal Antibodies Regis Sodoyer .1.1. Foreword .1.2. New markets for old antibodies, old markets for new antibodies .1.3. Antibody engineering: a new approach to the treatment of disease .1.4. Fully human antibodies, what else? .1.5. Antibody design .1.6. Antibody production .1.7. Recombinant antibodies: no limits .1.8. Acknowledgements .1.9. Abbreviations used in this chapter .References .Chapter 2: Structure, Classification and Naming of Therapeutic Monoclonal Antibodies Zhinan Xia .2.1. Antibody Structure .2.2. Classification of antibodies .2.3. IgG subtype .2.4. Nomenclature of therapeutic mAbs .2.5. List of therapeutic mAbs on market or in review in EU and US .2.6. Summary .References .Chapter 3: Mechanism of Action for Therapeutic Antibodies Yu Zhou and James D. Marks .3.1. Blockade of ligand–receptor interaction .3.2. Antibody binding to cell surface receptors .3.3. Engaging cytotoxic T cell through the use of bi–specific antibodies .3.4. Receptor down regulation by enhanced internalization and degradation .3.5. Targeted drug delivery .3.6. Summary .References .Chapter 4: Therapeutic Monoclonal Antibodies and Their Targets Maurizio Chiriva–Internati, et al .4.1. Introduction .4.2. Monoclonal antibody therapies for infectious diseases .4.3. Monoclonal antibody therapies for autoimmune diseases .4.4. Therapeutic monoclonal antibodies against neoplastic diseases .4.5. Conclusion .References .Chapter 5: Antibody Post–translational Modifications Roy Jefferis .5.1. Introduction .5.2. Overview of Co– & Post–translational Modifications .5.3. Glycosylation .5.4. Glycation .5.5. IgG–Fab Glycosylation .5.6. The Influence of Expression Platform on CTM/PTMs and Unintended Physic–chemical Changes .5.7. Human antibody isotypes other than IgG .5.8. Conclusion .References .Chapter 6: The Pharmacology, Pharmacokinetics, and Pharmacodynamics of Antibodies Ningning Xu, Meimei Liu and Margaret Liu .6.1. Introduction .6.2. Pharmacology of Anti–cancer mAbs .6.3. Antibody Pharmacokinetics (PK) .6.4. Pharmacodynamics (PD) .6.5. Conclusions .References .Chapter 7: Monoclonal Antibodies: Applications in Clinical Oncology Jeanene ( Gigi ) Robison .7.1. Introduction .7.2. Ado–trastuzumab emtansine (anti–HER2 antibody conjugated with emtansine, Kadcyla ) .7.3. Alemtuzumab (Campath® , Campath–1H) .7.4. Bevacizumab (Avastin) .7.5. Brentuximab vedotin (antiCD30 antibody, Adcetris®) .7.6. Cetuximab (anti–EGFR antibody, Erbitux®) .7.7. Denosumab (anti–RANKL antibody, XgevaTM; ProliaTM) .7.8. Eculizumab (anti–C5 antibody, Soliris®) .7.9. Ibritumomab tiuxetan (anti–CD20 antibody, Zevalin®) .7.10. Ipilimumab (anti–CTLA–4 antibody, Yervoy®) .7.11. Obinutuzumab (Gazyva®) .7.12. Ofatumumab (anti–CD20 antibody, Arzerra®) .7.13. Panitumumab (anti–EGFR antibody, Vectibix TM) .7.14. Pertuzumab (Perjeta®) .7.15. Ramucirumab (CYRAMZA® ) .7.16. Rituximab (anti–CD20 antibody, Rituxan®) .7.17. Tositumomab and Iodine I–131 Tositumab (anti–CD20 antibody, Bexxar®) .7.18. Trastuzumab (anti–HER2 antibody, Herceptin®) .References .Chapter 8: Development of Biosimilar Rituximab and Clinical Experience Reena Nair .8.1. Introduction .8.2. REDITUXTM Development Overview .8.3. Preclinical and Toxicology Studies .8.4. Clinical Evaluation .8.5. Conclusions .References .Chapter 9: Monoclonal Antibodies for Infectious Diseases Steven J. Projan .9.1. Into the future: prophylaxis & precision medicine .9.2. Immune therapy, a Nobel undertaking that went to the dogs .9.3. What s taking so long? .9.4. Staphylococcus aureus: still public enemy number one? .9.5. Pseudomonas aeruginosa: the bacterial cockroach .9.6. Immune evasion and degree of difficulty .9.7. Clostridium difficile: you can t win for losing .9.8. If two is enough is six too many? mAb combos .9.9. Prophylaxis or therapy? When you come to the fork in the road take it .9.10. Influenza and Plan B .9.11. Safety: Human enough for you? .9.12. Another precinct is heard from: immunomodulatory agents for the treatment of chronic infections .9.13. Are we there yet? Easy to use, fast turnaround, point of care diagnostics .9.14. Yeah but aren t these (biologic) drugs going to be expensive? .References .Chapter 10: Monoclonal Antibodies for Musculoskeletal, CNS, and other diseases Junming Yie and Tao Wu .10.1. Natalizumab (Tysabri®) .10.2. Eculizumab (Soliris®) .10.3. Ranibizumab (Lucentis®) .10.4. Denosumab (Prolia® and Xgeva®) .10.5. Antibody therapies for solid organ transplantation (Muromonab–CD3 (Orthoclone OKT3), Basiliximab (Simulect®), and Daclizumab (Zenapax®)) .10.6. Summary .References .Chapter 11: Manufacture of recombinant therapeutic proteins using Chinese Hamster Ovary cells in large–scale bioreactors history, methods and perspectives Florian M. Wurm and Maria De Jesus .11.1. Overview .11.2. Introduction .11.3. Process and cells: the quasispecies concept explains individualized development needs .11.4. Choices for manufacturing host cells for production and suitable selection systems .11.5. Methods for rapid generation of high–producing cell lines .11.6. Silencing stability of expression, facilitators for high level productivity .11.7. High–throughput bioprocess development .11.8. Disposable bioreactors .11.9. Non–clonal expression technologies for fast production and assessment of expression potential and quality .11.10. Conclusions .11.11. Conflict of interest statement .References .Chapter 12: Process Development Samuel D. Stimple and David W. Wood .12.1. Introduction .12.2. Protein A and Protein G Batch Affinity Chromatography .12.3. Alternatives to Protein A .12.4. Disposables and Continuous Downstream Processing .12.5. Conclusion .References .Chapter 13: Biosimilars and Biobetters: Impact on Biopharmaceutical Manufacturing and CMOs Ronald A. Rader .13.1. Overview .13.2. Introduction .13.3. The Biosimilar Pipeline .13.4. Developing Countries Will Continue to Prefer Cheaper Biogenerics .13.5. Biosimilar Candidates in the Pipeline .13.6. Biosimilar Development by Country/Region .13.7. Biosimilars Impact on Biopharmaceutical Markets and the Industry .13.8. Marketing Biosimilars Will Be a Challenge .13.9. Biosimilar Manufacturing Will Be State–of–the–Art .13.10. Biosimilars Will Increase Demand for Product Quality and Transparency .13.11. CMOs Benefit From Biosimilars .13.12. Conclusions .References .Chapter 14: Cell Line and Cell Culture Development for Biosimilar Antibody Drug Manufacturing Jianguo Yang, Ph.D .14.1. Overview .14.2. Mammalian Cell Line Development .14.3. Cell Culture Process Development .14.4. Future Trends .References .Chapter 15: Product Analysis of Biosimilar Antibodies Weidong Jiang, Scott Liu and Ziyang Zhong .15.1. Introduction .15.2. Identity .15.3. Purity and Impurities .15.4. Stability .15.5. Quantity – Concentration measurement .15.6. Biological activity Functional bioassays .15.7. Efficacy and Safety – Animal studies for antibody drug efficacy, PK/PD, and toxicity .References .Chapter 16: Bioanalytical Development Rafiq Islam .16.1. Introduction .16.2. Pharmacodynamics Characterization .16.3. Pharmacokinetic Assessment .16.4. Immunogenicity Assessment .16.5. Summary .References .Chapter 17: Preclinical and Clinical Development of Biosimilar Antibodies João Eurico Fonseca and João Gonçalves .17.1. Introduction .17.2. Quality and pre–clinical development of biosimilar monoclonal antibodies .17.3. Extrapolation of Indications .17.4. Clinical development of biosimilars of monoclonal antibodies .17.5. Published trials of candidate biosimilars of monoclonal antibodies .17.6. Ongoing trials of candidate biosimilars of monoclonal antibodies .17.7. Conclusion .References .Chapter 18: Regulatory Issues Clarinda Islam .18.1. Introduction .18.2. Existing Regulatory Pathways .18.3. Challenges .18.4. Conclusion .References .Chapter 19: Legal Considerations K. Lance Anderson, Jennifer R. Moore Meline, and Jonathan D. Ball .19.1. Introduction .19.2. Overview of the Biologics Price Competition and Innovation Act of 2009 ( BPCIA ) .19.3. Patent Litigation and The BPCIA .19.4. Conclusion .References .Chapter 20: ADCC Enhancement Technologies for Next Generation Therapeutic Antibodies Cheng Liu and Su Yan .20.1. Introduction .20.2. Activation of ADCC Functions .20.3. ADCC enhancement through glycol–engineering technologies .20.4. Major ADCC enhancement through glycol–engineering technologies .20.5. ADCC enhancement through Fc mutagenesis .20.6. Major ADCC enhancement Fc mutagenesis technologies .20.7. Summary .References .Chapter 21: Biosimilar Antibody Half–Life: Engineering for Optimal Performance K. John Morrow, Jr .21.1. Overview .21.2. Introduction .21.3. The IgG Molecule as a Therapeutic Entity .21.4. FcRn and Antibody half–life .21.5. Optimizing Antibody Fragments Half–Life .21.6. Albumin Fusions for Halflife Extension .21.7. Mice as Models for Human Disease .21.8. Half–Life Engineering: Present and Future .21.9. A bright future for biosimilars, biobetters and improved half–life modifications .References .Chapter 22: Technologies for Antibody Drug Conjugation Patrick G. Holder and David Rabuka .22.1. Introduction .22.2. The Importance of Therapeutic Index .22.3. ADC Construction: Building From the Protein Out .22.4. Conjugation Sites and Heterogeneity .22.5. Installation of Conjugation Sites .22.6. Bioconjugation Reactions .22.7. Linking Antibodies and Payloads .22.8. Summary .References .Index

• ISBN: 978-1-118-66231-1
• Editorial: Wiley–Blackwell
• Encuadernacion: Cartoné
• Páginas: 752
• Fecha Publicación: 02/01/2017
• Nº Volúmenes: 1
• Idioma: Inglés