{"product_id":"protein-analysis-using-mass-spectrometry-isbn-9781118605196","title":"Protein Analysis using Mass Spectrometry","description":"\u003cp\u003e\u003cb\u003ePresents Practical Applications of Mass Spectrometry for Protein Analysis and Covers Their Impact on Accelerating Drug Discovery and Development\u003c\/b\u003e\u003c\/p\u003e \u003cul\u003e \u003cli\u003eCovers both qualitative and quantitative aspects of Mass Spectrometry protein analysis in drug discovery\u003c\/li\u003e \u003cli\u003ePrinciples, Instrumentation, Technologies topics include MS of peptides, proteins, and ADCs , instrumentation in protein analysis, nanospray technology in MS protein analysis, and automation in MS protein analysis\u003c\/li\u003e \u003cli\u003eDetails emerging areas from drug monitoring to patient care such as Identification and validation of biomarkers for cancer, targeted MS approaches for biomarker validation, biomarker discovery, and regulatory perspectives\u003c\/li\u003e \u003cli\u003eBrings together the most current advances in the mass spectrometry technology and related method in protein analysis\u003c\/li\u003e \u003c\/ul\u003e \u003cp\u003eList of Contributors xiii\u003c\/p\u003e \u003cp\u003eForeword xvii\u003c\/p\u003e \u003cp\u003ePreface xix\u003c\/p\u003e \u003cp\u003e\u003cb\u003e1 Contemporary Protein Analysis by Ion Mobility Mass Spectrometry 1\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eJohannes P.C. Vissers and James I. Langridge\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e1.1 Introduction 1\u003c\/p\u003e \u003cp\u003e1.2 Traveling-Wave Ion Mobility Mass Spectrometry 1\u003c\/p\u003e \u003cp\u003e1.3 IM–MS and LC–IM–MS Analysis of Simple and Complex Mixtures 2\u003c\/p\u003e \u003cp\u003e1.4 Outlook 7\u003c\/p\u003e \u003cp\u003eAcknowledgment 8\u003c\/p\u003e \u003cp\u003eReferences 8\u003c\/p\u003e \u003cp\u003e\u003cb\u003e2 High-Resolution Accurate Mass Orbitrap and Its Application in Protein Therapeutics Bioanalysis 11\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eHongxia Wang and Patrick Bennett\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e2.1 Introduction 11\u003c\/p\u003e \u003cp\u003e2.2 Triple Quadrupole Mass Spectrometer and Its Challenges 11\u003c\/p\u003e \u003cp\u003e2.3 High-Resolution Mass Spectrometers 12\u003c\/p\u003e \u003cp\u003e2.4 Quantitation Modes on Q Exactive Hybrid Quadrupole Orbitrap 13\u003c\/p\u003e \u003cp\u003e2.5 Protein Quantitation Approaches Using Q Exactive Hybrid Quadrupole Orbitrap 14\u003c\/p\u003e \u003cp\u003e2.6 Data Processing 16\u003c\/p\u003e \u003cp\u003e2.7 Other Factors That Impact LC–MS-based Quantitation 16\u003c\/p\u003e \u003cp\u003e2.8 Conclusion and Perspectives of LC–HRMS in Regulated Bioanalysis 18\u003c\/p\u003e \u003cp\u003eReferences 18\u003c\/p\u003e \u003cp\u003e\u003cb\u003e3 Current Methods for the Characterization of Posttranslational Modifications in Therapeutic Proteins Using Orbitrap Mass Spectrometry 21\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eZhiqi Hao, Qiuting Hong, Fan Zhang, Shiaw-Lin Wu, and Patrick Bennett\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e3.1 Introduction 21\u003c\/p\u003e \u003cp\u003e3.2 Characterization of PTMs Using Higher-Energy Collision Dissociation 23\u003c\/p\u003e \u003cp\u003e3.3 Application of Electron Transfer Dissociation to the Characterization of Labile PTMs 26\u003c\/p\u003e \u003cp\u003e3.4 Conclusion 31\u003c\/p\u003e \u003cp\u003eAcknowledgment 32\u003c\/p\u003e \u003cp\u003eReferences 32\u003c\/p\u003e \u003cp\u003e\u003cb\u003e4 Macro- to Micromolecular Quantitation of Proteins and Peptides by Mass Spectrometry 35\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eSuma Ramagiri, Brigitte Simons, and Laura Baker\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e4.1 Introduction 35\u003c\/p\u003e \u003cp\u003e4.2 Key Challenges of Peptide Bioanalysis 36\u003c\/p\u003e \u003cp\u003e4.3 Key Features of LC\/MS\/MS-Based Peptide Quantitation 38\u003c\/p\u003e \u003cp\u003e4.4 Advantages of the Diversity of Mass Spectrometry Systems 41\u003c\/p\u003e \u003cp\u003e4.5 Perspectives for the Future 41\u003c\/p\u003e \u003cp\u003eReferences 42\u003c\/p\u003e \u003cp\u003e\u003cb\u003e5 Peptide and Protein Bioanalysis Using Integrated Column-to-Source Technology for High-Flow Nanospray 45\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eShane R. Needham and Gary A. Valaskovic\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e5.1 Introduction – LC–MS Has Enabled the Field of Protein Biomarker Discovery 45\u003c\/p\u003e \u003cp\u003e5.2 Integration of Miniaturized LC with Nanospray ESI-MS Is a Key for Success 46\u003c\/p\u003e \u003cp\u003e5.3 Micro- and Nano-LC Are Well Suited for Quantitative Bioanalysis 47\u003c\/p\u003e \u003cp\u003e5.4 Demonstrating Packed-Emitter Columns Are Suitable for Bioanalysis 49\u003c\/p\u003e \u003cp\u003e5.5 Future Outlook 51\u003c\/p\u003e \u003cp\u003eReferences 52\u003c\/p\u003e \u003cp\u003e\u003cb\u003e6 Targeting the Right Protein Isoform: Mass Spectrometry-Based Proteomic Characterization of Alternative Splice Variants 55\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eJiang Wu\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e6.1 Introduction 55\u003c\/p\u003e \u003cp\u003e6.2 Alternative Splicing and Human Diseases 55\u003c\/p\u003e \u003cp\u003e6.3 Identification of Splice Variant Proteins 56\u003c\/p\u003e \u003cp\u003e6.4 Conclusion 64\u003c\/p\u003e \u003cp\u003eReferences 64\u003c\/p\u003e \u003cp\u003e\u003cb\u003e7 The Application of Immunoaffinity-Based Mass Spectrometry to Characterize Protein Biomarkers and Biotherapeutics 67\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eBradley L. Ackermann and Michael J. Berna\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e7.1 Introduction 67\u003c\/p\u003e \u003cp\u003e7.2 Overview of IA-MS Methods 69\u003c\/p\u003e \u003cp\u003e7.3 IA-MS Applications – Biomarkers 74\u003c\/p\u003e \u003cp\u003e7.3.1 Peptide Biomarkers 74\u003c\/p\u003e \u003cp\u003e7.4 IA-MS Applications – Biotherapeutics 81\u003c\/p\u003e \u003cp\u003e7.5 Future Direction 84\u003c\/p\u003e \u003cp\u003eReferences 85\u003c\/p\u003e \u003cp\u003e\u003cb\u003e8 Semiquantification and Isotyping of Antidrug Antibodies by Immunocapture-LC\/MS for Immunogenicity Assessment 91\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eJianing Zeng, Hao Jiang, and Linlin Luo\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e8.1 Introduction 91\u003c\/p\u003e \u003cp\u003e8.2 Multiplexing Direct Measurement of ADAs by Immunocapture-LC\/MS for Immunogenicity Screening, Titering, and Isotyping 93\u003c\/p\u003e \u003cp\u003e8.3 Indirect Measurement of ADAs by Quantifying ADA Binding Components 95\u003c\/p\u003e \u003cp\u003e8.4 Use of LC–MS to Assist in Method Development of Cell-Based Neutralizing Antibody Assays 96\u003c\/p\u003e \u003cp\u003e8.5 Conclusion and Future Perspectives 97\u003c\/p\u003e \u003cp\u003eReferences 97\u003c\/p\u003e \u003cp\u003e\u003cb\u003e9 Mass Spectrometry-Based Assay for High-Throughput and High-Sensitivity Biomarker Verification 99\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eXuejiang Guo and Keqi Tang\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e9.1 Background 99\u003c\/p\u003e \u003cp\u003e9.2 Sample Processing Strategies 100\u003c\/p\u003e \u003cp\u003e9.3 Advanced Electrospray Ionization Mass Spectrometry Instrumentation 102\u003c\/p\u003e \u003cp\u003e9.4 Conclusion 105\u003c\/p\u003e \u003cp\u003eReferences 105\u003c\/p\u003e \u003cp\u003e\u003cb\u003e10 Monitoring Quality of Critical Reagents Used in Ligand Binding Assays with Liquid Chromatography Mass Spectrometry (LC–MS) 107\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eBrian Geist, Adrienne Clements-Egan, and Tong-Yuan Yang\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e10.1 Introduction 107\u003c\/p\u003e \u003cp\u003e10.2 Case Study Examples 114\u003c\/p\u003e \u003cp\u003e10.3 Discussion 122\u003c\/p\u003e \u003cp\u003eAcknowledgment 126\u003c\/p\u003e \u003cp\u003eReferences 126\u003c\/p\u003e \u003cp\u003e\u003cb\u003e11 Application of Liquid Chromatography-High Resolution Mass Spectrometry in the Quantification of Intact Proteins in Biological Fluids 129\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eStanley (Weihua) Zhang, Jonathan Crowther, and Wenying Jian\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e11.1 Introduction 129\u003c\/p\u003e \u003cp\u003e11.2 Workflows for Quantification of Proteins Using Full-Scan LC-HRMS 131\u003c\/p\u003e \u003cp\u003e11.3 Internal Standard Strategy 133\u003c\/p\u003e \u003cp\u003e11.4 Calibration and Quality Control (QC) Sample Strategy 135\u003c\/p\u003e \u003cp\u003e11.5 Common Issues in Quantification of Proteins Using LC-HRMS 135\u003c\/p\u003e \u003cp\u003e11.6 Examples of LC-HRMS-Based Intact Protein Quantification 137\u003c\/p\u003e \u003cp\u003e11.7 Conclusion and Future Perspectives 138\u003c\/p\u003e \u003cp\u003eAcknowledgment 140\u003c\/p\u003e \u003cp\u003eReferences 140\u003c\/p\u003e \u003cp\u003e\u003cb\u003e12 LC–MS\/MS Bioanalytical Method Development Strategy for Therapeutic Monoclonal Antibodies in Preclinical Studies 145\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eHongyan Li, Timothy Heath, and Christopher A. James\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e12.1 Introduction: LC-MS\/MS Bioanalysis of Therapeutic Monoclonal Antibodies 145\u003c\/p\u003e \u003cp\u003e12.2 Highlights of Recent Method Development Strategies 146\u003c\/p\u003e \u003cp\u003e12.3 Case Studies of Preclinical Applications of LC–MS\/MS for Monoclonal Antibody Bioanalysis 154\u003c\/p\u003e \u003cp\u003e12.4 Conclusion and Future Perspectives 156\u003c\/p\u003e \u003cp\u003eReferences 158\u003c\/p\u003e \u003cp\u003e\u003cb\u003e13 Generic Peptide Strategies for LC–MS\/MS Bioanalysis of Human Monoclonal Antibody Drugs and Drug Candidates 161\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eMichael T. Furlong\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e13.1 Introduction 161\u003c\/p\u003e \u003cp\u003e13.2 A Universal Peptide LC–MS\/MS Assay for Bioanalysis of a Diversity of Human Monoclonal Antibodies and Fc Fusion Proteins in Animal Studies 161\u003c\/p\u003e \u003cp\u003e13.3 An Improved “Dual” Universal Peptide LC–MS\/MS Assay for Bioanalysis of Human mAb Drug Candidates in Animal Studies 165\u003c\/p\u003e \u003cp\u003e13.4 Extending the Universal Peptide Assay Concept to Human mAb Bioanalysis in Human Studies 170\u003c\/p\u003e \u003cp\u003e13.5 Internal Standard Options for Generic Peptide LC–MS\/MS Assays 173\u003c\/p\u003e \u003cp\u003e13.6 Sample Preparation Strategies for Generic Peptide LC–MS\/MS Assays 175\u003c\/p\u003e \u003cp\u003e13.7 Limitations of Generic Peptide LC–MS\/MS Assays 177\u003c\/p\u003e \u003cp\u003e13.8 Conclusion 178\u003c\/p\u003e \u003cp\u003eAcknowledgments 178\u003c\/p\u003e \u003cp\u003eReferences 178\u003c\/p\u003e \u003cp\u003e\u003cb\u003e14 Mass Spectrometry-Based Methodologies for Pharmacokinetic Characterization of Antibody Drug Conjugate Candidates During Drug Development 183\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eYongjun Xue, Priya Sriraman, Matthew V. Myers, Xiaomin Wang, Jian Chen, Brian Melo, Martha Vallejo, Stephen E. Maxwell, and Sekhar Surapaneni\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e14.1 Introduction 183\u003c\/p\u003e \u003cp\u003e14.2 Mechanism of Action 183\u003c\/p\u003e \u003cp\u003e14.3 Mass Spectrometry Measurement for DAR Distribution of Circulating ADCs 186\u003c\/p\u003e \u003cp\u003e14.4 Total Antibody Quantitation by Ligand Binding or LC–MS\/MS 189\u003c\/p\u003e \u003cp\u003e14.5 Total Conjugated Drug Quantitation by Ligand Binding or LC–MS\/MS 193\u003c\/p\u003e \u003cp\u003e14.6 Catabolite Quantitation by LC–MS\/MS 196\u003c\/p\u003e \u003cp\u003e14.7 Preclinical and Clinical Pharmacokinetic Support 197\u003c\/p\u003e \u003cp\u003e14.8 Conclusion and Future Perspectives 198\u003c\/p\u003e \u003cp\u003eReferences 198\u003c\/p\u003e \u003cp\u003e\u003cb\u003e15 Sample Preparation Strategies for LC–MS Bioanalysis of Proteins 203\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eLong Yuan and Qin C. Ji\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e15.1 Introduction 203\u003c\/p\u003e \u003cp\u003e15.2 Sample Preparation Strategies to Improve Assay Sensitivity 205\u003c\/p\u003e \u003cp\u003e15.3 Sample Preparation Strategies to Differentiate Free, Total, and ADA-Bound Proteins 213\u003c\/p\u003e \u003cp\u003e15.4 Sample Preparation Strategies to Overcome Interference from Antidrug Antibodies or Soluble Target 214\u003c\/p\u003e \u003cp\u003e15.5 Protein Digestion Strategies 214\u003c\/p\u003e \u003cp\u003e15.6. Conclusion 215\u003c\/p\u003e \u003cp\u003eAcknowledgment 216\u003c\/p\u003e \u003cp\u003eReferences 216\u003c\/p\u003e \u003cp\u003e\u003cb\u003e16 Characterization of Protein Therapeutics by Mass Spectrometry 221\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eWei Wu, Hangtian Song, Thomas Slaney, Richard Ludwig, Li Tao, and Tapan Das\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e16.1 Introduction 221\u003c\/p\u003e \u003cp\u003e16.2 Variants Associated with Cysteine\/Disulfide Bonds in Protein Therapeutics 221\u003c\/p\u003e \u003cp\u003e16.3 N–C-Terminal Variants 225\u003c\/p\u003e \u003cp\u003e16.4 Glycation 226\u003c\/p\u003e \u003cp\u003e16.5 Oxidation 226\u003c\/p\u003e \u003cp\u003e16.6 Discoloration 228\u003c\/p\u003e \u003cp\u003e16.7 Sequence Variants 230\u003c\/p\u003e \u003cp\u003e16.8 Glycosylation 232\u003c\/p\u003e \u003cp\u003e16.9 Conclusion 240\u003c\/p\u003e \u003cp\u003eReferences 240\u003c\/p\u003e \u003cp\u003eIndex 251\u003c\/p\u003e \u003cp\u003e\u003cb\u003eDr. Mike S. Lee\u003c\/b\u003e is a biotechnology entrepreneur and Founder and President of Milestone Development Services. He actively participates in the development of new technologies and their integration into industrial settings.  Dr. Lee is a founder of the Annual Symposium on Clinical and Pharmaceutical Solutions through Analysis (CPSA). These unique events, held in the US, China and Brazil, highlight industry-related applications and feature sessions promoting discussion on real-world experiences with the latest analytical technology and industry initiatives. Dr. Lee is the author or co-author of over 50 scientific papers and patents. He received his BS degree in Chemistry at the University of Maryland in 1982. In 1985 and 1987, he completed his MS and PhD, respectively, in Analytical Chemistry from the University of Florida under the direction of Professor Richard A. Yost.\u003c\/p\u003e \u003cp\u003e\u003cb\u003eDr. Qin C. Ji\u003c\/b\u003e is a Research Fellow in the Department of Bioanalytical Sciences at Bristol-Myers Squibb, Princeton, New Jersey. His current job responsibilities include regulated bioanalytical support (with LC-MS\/MS and ligand binding assays) for the development of biologic, new modality, and small molecule drugs in preclinical and clinical stages. He has authored and co-authored more than 60 peer reviewed articles and book chapters.  Prior to his current position, he held scientific and management positions at Abbott and Covance. Dr. Ji obtained his Ph.D. from Michigan State University and has completed Postdoctoral training at Mayo Clinic. He was awarded two President Awards and was an Associate Research Fellow in the prestigious Volwiler scientific society at Abbott Laboratories. He was also awarded a Chemistry Leadership Award at Bristol-Myers Squibb.\u003c\/p\u003e \u003cp\u003e\u003cb\u003ePresents Practical Applications of Mass Spectrometry for Protein Analysis and Covers Their Impact on Accelerating Drug Discovery and Development\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eProtein biotherapeutics has become a large portion of drug candidates and newly developed drugs aimed at conquering unmet medical needs. In recent years protein biotherapeutics have become an essential part of medical treatments for cancers and autoimmune diseases. \u003ci\u003eProtein Analysis using Mass Spectrometry: Accelerating Protein Biotherapeutics from Lab to Patient\u003c\/i\u003e describes the practical applications of mass spectrometry for protein analysis as well as their impact on accelerating drug discovery and development.\u003c\/p\u003e \u003cp\u003eAnalytical sciences used to develop technologies and methodologies to probe unknown systems quantitatively and qualitatively are one of essential components for delivering effective protein biotherapeutics. As protein molecules continue to be linked to diseases there is an increased opportunity for developing protein biotherapeutics to treat these diseases. The book brings together the most current advances in mass spectrometry technologies and related methods in order to accomplish this.\u003c\/p\u003e \u003cp\u003eDoctors and nurses, lab managers, lab technicians, and pharmaceutical researches from academia and industry as well as researchers and developers will find this reference a useful tool in their research.\u003c\/p\u003e","brand":"Wiley","offers":[{"title":"Default Title","offer_id":47989879537893,"sku":"NP9781118605196","price":196.95,"currency_code":"USD","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/1842\/7735\/files\/9781118605196.jpg?v=1761785769","url":"https:\/\/k12savings.com\/es\/products\/protein-analysis-using-mass-spectrometry-isbn-9781118605196","provider":"K12savings","version":"1.0","type":"link"}