{"product_id":"biosimilars-of-monoclonal-antibodies-9781118662311","title":"Biosimilars of Monoclonal Antibodies","description":"\u003cb\u003eBook Synopsis\u003c\/b\u003e\u003cbr\u003e\u003cp\u003eAddressing 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.\u003c\/p\u003e \u003cp\u003eGuides readers through the complex landscape involved with developing biosimilar versions of monoclonal antibody (mAb) drugs\u003cbr\u003eFeatures flow charts, tables, and figures that clearly illustrate processes and makes the book comprehensible and accessible\u003cbr\u003eIncludes a review of FDA-approved mAb drugs as a quick reference to facts and useful information\u003cbr\u003eExamines new technologies and strategies for improving biosimilar mAbs\u003c\/p\u003e\u003cbr\u003e\u003cbr\u003e\u003cb\u003eTable of Contents\u003c\/b\u003e\u003cbr\u003e\u003cp\u003eNotes on Contributors xxv\u003c\/p\u003e \u003cp\u003ePreface xli\u003c\/p\u003e \u003cp\u003e\u003cb\u003e1 The History of Therapeutic Monoclonal Antibodies 1\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eRegis Sodoyer\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e1.1 Summary 1\u003c\/p\u003e \u003cp\u003e1.2 Introduction 1\u003c\/p\u003e \u003cp\u003e1.3 New Markets for Old Antibodies, Old Markets for New Antibodies 2\u003c\/p\u003e \u003cp\u003e1.4 Antibody Engineering: A New Approach to the Treatment of Disease 5\u003c\/p\u003e \u003cp\u003e1.5 Fully Human Antibodies, What Else? 8\u003c\/p\u003e \u003cp\u003e1.6 Antibody Design 17\u003c\/p\u003e \u003cp\u003e1.7 Antibody Production 30\u003c\/p\u003e \u003cp\u003e1.8 Recombinant Antibodies: No Limits… 37\u003c\/p\u003e \u003cp\u003eAcknowledgments 37\u003c\/p\u003e \u003cp\u003eReferences 37\u003c\/p\u003e \u003cp\u003e\u003cb\u003e2 Structure, Classification, and Naming of Therapeutic Monoclonal Antibodies 63\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eZhinan Xia\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e2.1 Summary 63\u003c\/p\u003e \u003cp\u003e2.2 Introduction 64\u003c\/p\u003e \u003cp\u003e2.3 Antibody Structure 65\u003c\/p\u003e \u003cp\u003e2.4 Classification of Antibodies 71\u003c\/p\u003e \u003cp\u003e2.5 IgG Subtype 73\u003c\/p\u003e \u003cp\u003e2.6 Nomenclature of Therapeutic mAbs 73\u003c\/p\u003e \u003cp\u003e2.7 List of Therapeutic mAbs on Market or in Review in the European Union and the United States 82\u003c\/p\u003e \u003cp\u003eReferences 82\u003c\/p\u003e \u003cp\u003e\u003cb\u003e3 Mechanism of Action for Therapeutic Antibodies 85\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eYu Zhou and James D. Marks\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e3.1 Introduction 85\u003c\/p\u003e \u003cp\u003e3.2 Blockade of Ligand–Receptor Interaction 86\u003c\/p\u003e \u003cp\u003e3.3 Target Depletion via ADCC and CDC 94\u003c\/p\u003e \u003cp\u003e3.4 Engaging Cytotoxic T Cell Through the Use of Bispecific Abs 95\u003c\/p\u003e \u003cp\u003e3.5 Receptor Downregulation by Enhanced Internalization and Degradation 96\u003c\/p\u003e \u003cp\u003e3.6 Targeted Drug Delivery 96\u003c\/p\u003e \u003cp\u003e3.7 Summary 98\u003c\/p\u003e \u003cp\u003eReferences 98\u003c\/p\u003e \u003cp\u003e\u003cb\u003e4 Therapeutic Monoclonal Antibodies and Their Targets 113\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eJose A. Figueroa, Camilo Pena, Leonardo Mirandola, Adair Reidy, J. Drew Payne, Nattamol Hosiriluck, Natallia Suvorava, Rakhshanda Layeequr Rahman, Adrienne R. Whitlow, Rashmi Verma, Everardo Cobos, and Maurizio Chiriva-Internati\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e4.1 Summary 113\u003c\/p\u003e \u003cp\u003e4.2 Introduction 114\u003c\/p\u003e \u003cp\u003e4.3 Monoclonal Antibody Therapies for Infectious Diseases 117\u003c\/p\u003e \u003cp\u003e4.4 Monoclonal Antibody Therapies for Autoimmune Diseases 120\u003c\/p\u003e \u003cp\u003e4.5 Therapeutic Monoclonal Antibodies Against Neoplastic Diseases 127\u003c\/p\u003e \u003cp\u003e4.6 Conclusion 138\u003c\/p\u003e \u003cp\u003eReferences 140\u003c\/p\u003e \u003cp\u003e\u003cb\u003e5 Antibody Posttranslational Modifications 155\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eRoy Jefferis\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e5.1 Summary 155\u003c\/p\u003e \u003cp\u003e5.2 Introduction 155\u003c\/p\u003e \u003cp\u003e5.3 Overview of Co- and Posttranslational Modifications 157\u003c\/p\u003e \u003cp\u003e5.4 Glycosylation 162\u003c\/p\u003e \u003cp\u003e5.5 Glycation 172\u003c\/p\u003e \u003cp\u003e5.6 IgG-Fab Glycosylation 179\u003c\/p\u003e \u003cp\u003e5.7 The Influence of Expression Platform on CTM\/PTMs and Unintended Physicochemical Changes 181\u003c\/p\u003e \u003cp\u003e5.8 Human Antibody Isotypes Other than IgG 182\u003c\/p\u003e \u003cp\u003e5.9 Conclusion 182\u003c\/p\u003e \u003cp\u003eReferences 183\u003c\/p\u003e \u003cp\u003e\u003cb\u003e6 The Pharmacology, Pharmacokinetics, and Pharmacodynamics of Antibodies 201\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eNingning Xu, Meimei Liu, and Margaret Liu\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e6.1 Summary 201\u003c\/p\u003e \u003cp\u003e6.2 Introduction 201\u003c\/p\u003e \u003cp\u003e6.3 Pharmacology of Anticancer MAbs 202\u003c\/p\u003e \u003cp\u003e6.4 Antibody Pharmacokinetics 204\u003c\/p\u003e \u003cp\u003e6.5 Pharmacodynamics 208\u003c\/p\u003e \u003cp\u003e6.6 Conclusions 211\u003c\/p\u003e \u003cp\u003eReferences 211\u003c\/p\u003e \u003cp\u003e\u003cb\u003e7 Monoclonal Antibodies: Applications in Clinical Oncology 217\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eJeanene (“Gigi”) Robison\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e7.1 Summary 217\u003c\/p\u003e \u003cp\u003e7.2 Introduction 217\u003c\/p\u003e \u003cp\u003e7.3 Ado-trastuzumab Emtansine (Anti-HER2 Antibody Conjugated with Emtansine, Kadcyla®) 218\u003c\/p\u003e \u003cp\u003e7.4 Alemtuzumab (Campath®, Campath-1H) 220\u003c\/p\u003e \u003cp\u003e7.5 Bevacizumab (Avastin) 221\u003c\/p\u003e \u003cp\u003e7.6 Brentuximab Vedotin (Anti-CD30 Antibody, Adcetris®) 225\u003c\/p\u003e \u003cp\u003e7.7 Cetuximab (Anti-EGFR Antibody, Erbitux®) 227\u003c\/p\u003e \u003cp\u003e7.8 Denosumab (Anti-RANKL Antibody, Xgeva™; Prolia™) 230\u003c\/p\u003e \u003cp\u003e7.9 Eculizumab (Anti-C5 Antibody, Soliris®) 233\u003c\/p\u003e \u003cp\u003e7.10 Ibritumomab Tiuxetan (Anti-CD20 Antibody, Zevalin®) 235\u003c\/p\u003e \u003cp\u003e7.11 Ipilimumab (Anti-CTLA-4 Antibody, Yervoy®) 237\u003c\/p\u003e \u003cp\u003e7.12 Obinutuzumab (Gazyva®) 238\u003c\/p\u003e \u003cp\u003e7.13 Ofatumumab (Anti-CD20 Antibody, Arzerra®) 240\u003c\/p\u003e \u003cp\u003e7.14 Panitumumab (Anti-EGFR Antibody, Vectibix™) 242\u003c\/p\u003e \u003cp\u003e7.15 Pembrolizumab (Keytruda®) 244\u003c\/p\u003e \u003cp\u003e7.16 Pertuzumab (Perjeta®) 246\u003c\/p\u003e \u003cp\u003e7.17 Ramucirumab (Cyramza®) 248\u003c\/p\u003e \u003cp\u003e7.18 Rituximab (Anti-CD20 Antibody, Rituxan) 250\u003c\/p\u003e \u003cp\u003e7.19 Tositumomab and Iodine I-131 Tositumomab (Anti-CD20 Antibody, Bexxar®) 256\u003c\/p\u003e \u003cp\u003e7.20 Trastuzumab (Anti-HER2 Antibody, Herceptin®) 258\u003c\/p\u003e \u003cp\u003eReferences 262\u003c\/p\u003e \u003cp\u003e\u003cb\u003e8 Development of Biosimilar Rituximab and Clinical Experience 269\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eReena Nair\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e8.1 Summary 269\u003c\/p\u003e \u003cp\u003e8.2 Introduction 270\u003c\/p\u003e \u003cp\u003e8.3 Reditux Development Overview 271\u003c\/p\u003e \u003cp\u003e8.4 Preclinical and Toxicology Studies 276\u003c\/p\u003e \u003cp\u003e8.5 Clinical Evaluation 276\u003c\/p\u003e \u003cp\u003e8.6 Conclusions 280\u003c\/p\u003e \u003cp\u003eReferences 280\u003c\/p\u003e \u003cp\u003e\u003cb\u003e9 Monoclonal Antibodies for Infectious Diseases 283\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eSteven J. Projan\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e9.1 Summary 283\u003c\/p\u003e \u003cp\u003e9.2 Into the Future: Prophylaxis and Precision Medicine 283\u003c\/p\u003e \u003cp\u003e9.3 Immune Therapy: A Noble Undertaking that Went to the Dogs 284\u003c\/p\u003e \u003cp\u003e9.4 What’s Taking So Long? 285\u003c\/p\u003e \u003cp\u003e9.5 Staphylococcus aureus: Still Public Enemy Number One? 285\u003c\/p\u003e \u003cp\u003e9.6 Pseudomonas aeruginosa: The Bacterial Cockroach 286\u003c\/p\u003e \u003cp\u003e9.7 Immune Evasion and Degree of Difficulty 287\u003c\/p\u003e \u003cp\u003e9.8 Clostridium difficile: You Can’t Win for Losing 287\u003c\/p\u003e \u003cp\u003e9.9 If Two Is Enough, Is Six Too Many? mAb Combos 288\u003c\/p\u003e \u003cp\u003e9.10 Prophylaxis or Therapy? When You Come to a Fork in the Road, Take It 288\u003c\/p\u003e \u003cp\u003e9.11 Influenza and Plan “B” 288\u003c\/p\u003e \u003cp\u003e9.12 Safety: Human Enough for You? 288\u003c\/p\u003e \u003cp\u003e9.13 Another Precinct Is Heard from Immunomodulatory Agents for the Treatment of Chronic Infections 289\u003c\/p\u003e \u003cp\u003e9.14 Are We There Yet? Easy to Use, Fast Turnaround, Point-of-Care Diagnostics 289\u003c\/p\u003e \u003cp\u003e9.15 Yeah but Aren’t These (Biologic) Drugs Going to Be Expensive? 290\u003c\/p\u003e \u003cp\u003eReferences 290\u003c\/p\u003e \u003cp\u003e\u003cb\u003e10 Monoclonal Antibodies for Musculoskeletal, CNS, and Other Diseases 293\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eJunming Yie and Tao Wu\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e10.1 Summary 293\u003c\/p\u003e \u003cp\u003e10.2 Natalizumab (Tysabri®) 294\u003c\/p\u003e \u003cp\u003e10.3 Eculizumab (Soliris®) 297\u003c\/p\u003e \u003cp\u003e10.4 Ranibizumab (Lucentis®) 300\u003c\/p\u003e \u003cp\u003e10.5 Denosumab (Prolia® and Xgeva®) 304\u003c\/p\u003e \u003cp\u003e10.6 Antibody Therapies for Solid Organ Transplantation (Muromonab-CD3 (Orthoclone OKT3®), Basiliximab (Simulect®), and Daclizumab (Zenapax®)) 307\u003c\/p\u003e \u003cp\u003e10.7 Conclusion 314\u003c\/p\u003e \u003cp\u003eReferences 318\u003c\/p\u003e \u003cp\u003e\u003cb\u003e11 Manufacture of Recombinant Therapeutic Proteins Using Chinese Hamster Ovary Cells in Large-Scale Bioreactors: History, Methods, and Perspectives 327\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eFlorian M. Wurm and Maria de Jesus\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e11.1 Summary 327\u003c\/p\u003e \u003cp\u003e11.2 Introduction 329\u003c\/p\u003e \u003cp\u003e11.3 Process and Cells: The Quasi-species Concept Explains Individualized Development Needs 332\u003c\/p\u003e \u003cp\u003e11.4 Choices for Manufacturing: Host Cells for Production and Suitable Selection Systems 335\u003c\/p\u003e \u003cp\u003e11.5 Methods for Rapid Generation of High-Producing Cell Lines 337\u003c\/p\u003e \u003cp\u003e11.6 Silencing: Stability of Expression, Facilitators for High-Level Productivity 339\u003c\/p\u003e \u003cp\u003e11.7 High-Throughput Bioprocess Development 340\u003c\/p\u003e \u003cp\u003e11.8 Disposable Bioreactors 342\u003c\/p\u003e \u003cp\u003e11.9 Nonclonal Expression Technologies for Fast Production and Assessment of Expression Potential and Quality 343\u003c\/p\u003e \u003cp\u003e11.10 Conclusions 345\u003c\/p\u003e \u003cp\u003eConflict of Interest 346\u003c\/p\u003e \u003cp\u003eReferences 346\u003c\/p\u003e \u003cp\u003e\u003cb\u003e12 Process Development 355\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eSamuel D. Stimple and David W. Wood\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e12.1 Summary 355\u003c\/p\u003e \u003cp\u003e12.2 Introduction 355\u003c\/p\u003e \u003cp\u003e12.3 Protein A and Protein G Batch Affinity Chromatography 356\u003c\/p\u003e \u003cp\u003e12.4 Alternatives to Protein A 358\u003c\/p\u003e \u003cp\u003e12.5 Disposables and Continuous Downstream Processing 361\u003c\/p\u003e \u003cp\u003e12.6 Conclusion 373\u003c\/p\u003e \u003cp\u003eReferences 374\u003c\/p\u003e \u003cp\u003e\u003cb\u003e13 Biosimilars and Biobetters: Impact on Biopharmaceutical Manufacturing and CMOs 381\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eRonald A. Rader\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e13.1 Summary 381\u003c\/p\u003e \u003cp\u003e13.2 Introduction 382\u003c\/p\u003e \u003cp\u003e13.3 The Biosimilar Pipeline 383\u003c\/p\u003e \u003cp\u003e13.4 Developing Countries Will Continue to Prefer Cheaper Biogenerics 386\u003c\/p\u003e \u003cp\u003e13.5 Biosimilar Candidates in the Pipeline 387\u003c\/p\u003e \u003cp\u003e13.6 Biosimilar Development by Country\/Region 387\u003c\/p\u003e \u003cp\u003e13.7 Biosimilars Impact on Biopharmaceutical Markets and the Industry 389\u003c\/p\u003e \u003cp\u003e13.8 Marketing Biosimilars Will Be a Challenge 391\u003c\/p\u003e \u003cp\u003e13.9 Biosimilar Manufacturing Will Be State of the Art 391\u003c\/p\u003e \u003cp\u003e13.10 Biosimilars Will Increase Demand for Product Quality and Transparency 392\u003c\/p\u003e \u003cp\u003e13.11 CMOs Benefit from Biosimilars 393\u003c\/p\u003e \u003cp\u003e13.12 Conclusions 394\u003c\/p\u003e \u003cp\u003eReferences 395\u003c\/p\u003e \u003cp\u003e\u003cb\u003e14 Cell Line and Cell Culture Development for Biosimilar Antibody-Drug Manufacturing 397\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eJianguo Yang\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e14.1 Summary 397\u003c\/p\u003e \u003cp\u003e14.2 Mammalian Cell Line Development 398\u003c\/p\u003e \u003cp\u003e14.3 Cell Culture Process Development 406\u003c\/p\u003e \u003cp\u003e14.4 Future Trends 418\u003c\/p\u003e \u003cp\u003eReferences 419\u003c\/p\u003e \u003cp\u003e\u003cb\u003e15 Product Analysis of Biosimilar Antibodies 427\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eWeidong Jiang, Scott Liu, and Ziyang Zhong\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e15.1 Summary 427\u003c\/p\u003e \u003cp\u003e15.2 Introduction 428\u003c\/p\u003e \u003cp\u003e15.3 Identity 428\u003c\/p\u003e \u003cp\u003e15.4 Purity and Impurities 438\u003c\/p\u003e \u003cp\u003e15.5 Stability 445\u003c\/p\u003e \u003cp\u003e15.6 Quantity—Concentration Measurement 446\u003c\/p\u003e \u003cp\u003e15.7 Biological Activity—Functional Bioassays 446\u003c\/p\u003e \u003cp\u003e15.8 Efficacy and Safety: Animal Studies for Antibody-Drug Efficacy, PK\/PD, and Toxicity 450\u003c\/p\u003e \u003cp\u003eReferences 452\u003c\/p\u003e \u003cp\u003e\u003cb\u003e16 Bioanalytical Development 459\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eRafiq Islam\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e16.1 Summary 459\u003c\/p\u003e \u003cp\u003e16.2 Introduction 459\u003c\/p\u003e \u003cp\u003e16.3 Pharmacodynamics Characterization 460\u003c\/p\u003e \u003cp\u003e16.4 Pharmacokinetic Assessment 465\u003c\/p\u003e \u003cp\u003e16.5 Immunogenicity Assessment 472\u003c\/p\u003e \u003cp\u003e16.6 Conclusion 474\u003c\/p\u003e \u003cp\u003eReferences 475\u003c\/p\u003e \u003cp\u003e\u003cb\u003e17 Preclinical and Clinical Development of Biosimilar Antibodies 479\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eJoão Eurico Fonseca and João Gonçalves\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e17.1 Summary 479\u003c\/p\u003e \u003cp\u003e17.2 Introduction 480\u003c\/p\u003e \u003cp\u003e17.3 Quality and Preclinical Development of Biosimilar Monoclonal Antibodies 481\u003c\/p\u003e \u003cp\u003e17.4 Extrapolation of Indications 490\u003c\/p\u003e \u003cp\u003e17.5 Clinical Development of Biosimilars of Monoclonal Antibodies 492\u003c\/p\u003e \u003cp\u003e17.6 Ongoing Trials of Candidate Biosimilars of Monoclonal Antibodies 494\u003c\/p\u003e \u003cp\u003e17.7 Conclusion 498\u003c\/p\u003e \u003cp\u003eReferences 498\u003c\/p\u003e \u003cp\u003e\u003cb\u003e18 Regulatory Issues 505\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eClarinda Islam\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e18.1 Summary 505\u003c\/p\u003e \u003cp\u003e18.2 Introduction 505\u003c\/p\u003e \u003cp\u003e18.3 Existing Regulatory Pathways 506\u003c\/p\u003e \u003cp\u003e18.4 Challenges 512\u003c\/p\u003e \u003cp\u003e18.5 Conclusion 514\u003c\/p\u003e \u003cp\u003eReferences 514\u003c\/p\u003e \u003cp\u003e\u003cb\u003e19 Legal Considerations 517\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eK. Lance Anderson, Jennifer R. Moore Meline, and Jonathan D. Ball\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e19.1 Summary 517\u003c\/p\u003e \u003cp\u003e19.2 Overview of the Biologics Price Competition and Innovation Act of 2009 (“BPCIA”) 519\u003c\/p\u003e \u003cp\u003e19.3 Patent Litigation and the BPCIA 529\u003c\/p\u003e \u003cp\u003e19.4 Patenting Your Biosimilar 541\u003c\/p\u003e \u003cp\u003e19.5 Conclusion 543\u003c\/p\u003e \u003cp\u003eNotes 544\u003c\/p\u003e \u003cp\u003e\u003cb\u003e20 ADCC Enhancement Technologies for Next-Generation Therapeutic Antibodies 549\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eCheng Liu and Su Yan\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e20.1 Summary 549\u003c\/p\u003e \u003cp\u003e20.2 Introduction 549\u003c\/p\u003e \u003cp\u003e20.3 Activation of ADCC Functions 550\u003c\/p\u003e \u003cp\u003e20.4 ADCC Enhancement through Glycol-Engineering Technologies 552\u003c\/p\u003e \u003cp\u003e20.5 Major ADCC Enhancement through Glycol-Engineering Technologies 553\u003c\/p\u003e \u003cp\u003e20.6 ADCC Enhancement through Fc Mutagenesis 557\u003c\/p\u003e \u003cp\u003e20.7 Major ADCC Enhancement Fc Mutagenesis Technologies 557\u003c\/p\u003e \u003cp\u003e20.8 Conclusion 559\u003c\/p\u003e \u003cp\u003eReferences\u003c\/p\u003e \u003cp\u003e560\u003c\/p\u003e \u003cp\u003e\u003cb\u003e21 Antibody Half-Life: Engineering for Optimal Performance 565\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eK. John Morrow, Jr.\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e21.1 Summary 565\u003c\/p\u003e \u003cp\u003e21.2 Introduction 566\u003c\/p\u003e \u003cp\u003e21.3 The IgG Molecule as a Therapeutic Entity 568\u003c\/p\u003e \u003cp\u003e21.4 FcRn and Antibody Half-Life 569\u003c\/p\u003e \u003cp\u003e21.5 Optimizing Antibody Fragments’ Half-Life 572\u003c\/p\u003e \u003cp\u003e21.6 Albumin Fusions for Half-Life Extension 575\u003c\/p\u003e \u003cp\u003e21.7 Mice as Models for Human Disease 577\u003c\/p\u003e \u003cp\u003e21.8 Half-Life Engineering: Present and Future 578\u003c\/p\u003e \u003cp\u003e21.9 A Bright Future for Biosimilars, Biobetters, and Improved Half-Life Modifications 583\u003c\/p\u003e \u003cp\u003eReferences 585\u003c\/p\u003e \u003cp\u003e\u003cb\u003e22 Technologies for Antibody-Drug Conjugation 591\u003c\/b\u003e\u003cbr\u003e\u003ci\u003ePatrick G. Holder and David Rabuka\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e22.1 Summary 591\u003c\/p\u003e \u003cp\u003e22.3 The Importance of Therapeutic Index 592\u003c\/p\u003e \u003cp\u003e22.4 ADC Construction: Building from the Protein Out 593\u003c\/p\u003e \u003cp\u003e22.5 Conjugation Sites and Heterogeneity 596\u003c\/p\u003e \u003cp\u003e22.6 Installation of Conjugation Sites 597\u003c\/p\u003e \u003cp\u003e22.7 Bioconjugation Reactions 602\u003c\/p\u003e \u003cp\u003e22.8 Linking Antibodies and Payloads 613\u003c\/p\u003e \u003cp\u003e22.9 Conclusion 623\u003c\/p\u003e \u003cp\u003eReferences 623\u003c\/p\u003e \u003cp\u003eIndex 641\u003c\/p\u003e","brand":"John Wiley \u0026 Sons Inc","offers":[{"title":"Default Title","offer_id":49406902468951,"sku":"9781118662311","price":145.76,"currency_code":"GBP","in_stock":false}],"url":"https:\/\/bookcurl.com\/products\/biosimilars-of-monoclonal-antibodies-9781118662311","provider":"Book Curl","version":"1.0","type":"link"}