TY  - BOOK
AU  - Wood,Clive
TI  - Antibody drug discovery
T2  - Molecular medicine and medicinal chemistry
SN  - 9781848166288
AV  - RS201.A56 A58 2012
U1  - 615.37 22
PY  - 2012///]
CY  - London
PB  - Imperial College Press
KW  - Antibody-drug conjugates
KW  - Drug development
KW  - Immunoglobulins
KW  - Antibodies
KW  - Drug Discovery
N1  - pharmacy bookfair2016; Includes bibliographical references and index; Contributors --  Foreword John McCafferty --  Preface Clive R.Wood --  Chapter 1 Humanization of Antibodies Olivier Léger and José W. Saldanha --  1.1 Introduction --  1.1.1 First step: chimerization --  1.2 CDR Grafting: Standard Technology --  1.2.1 Choice of CDR region to graft --  1.2.2 Choice of human framework acceptor regions --  1.2.2.1 Fixed frameworks --  1.2.2.2 Best fit --  1.2.2.3 Consensus --  1.2.2.4 Germline --  1.2.3 Backmutations --  1.3 Affinity versus Stability --  1.4 Alternative Approaches --  1.4.1 Veneering or resurfacing --  1.4.2 Grafting of abbreviated CDRs containing specificity-determining residues 1.4.3 Superhumanization1.4.4 Human string content optimization --  1.4.5 Framework shuffling and human framework adaptation --  1.4.6 Combinatorial library approaches --  1.4.6.1 Guided selection --  1.4.6.2 Framework libraries --  1.4.7 HumaneeringTM technology --  1.5 Concluding Remarks --  References --  Chapter 2 Selection and Screening of Antibody Phage Display Libraries David R. Buckler, Darren Schofield, Daniel J. Sexton, David Lowe and Tristan J. Vaughan --  2.1 Introduction --  2.2 Antibody Gene Rearrangement and Variable Region Sequence Diversity 2.2.1 Antibody architecture and germline gene segment recombination2.2.2 Variable region sequence diversity and structure guiding library design --  2.2.3 Amplification of variable region sequence repertoires --  2.2.4 Antibody sequence databases --  2.3 Antibody Display Libraries in Ff Bacteriophage --  2.3.1 Phage biology and early use as a display system --  2.3.2 Variation of display format and control of display level --  2.3.2.1 Coat protein display position --  2.3.2.2 Display format, scFv vs. Fab --  2.3.2.3 Signal peptide and vector design --  2.3.2.4 Control of functional display level and valency 2.3.2.5 Maximizing library size2.3.2.6 Assessment of diversity --  2.3.3 Representative large non-immune libraries --  2.4 Library Selection --  2.4.1 Antigen immobilization --  2.4.2 Overview of phage display selection --  2.4.3 Advantages and successes of phage display --  2.4.3.1 Species cross-reactivity --  2.4.3.2 Homolog binders --  2.4.3.3 Rare epitopes --  2.4.3.4 Exquisite specificity --  2.4.3.5 Cell surface antigens --  2.4.3.6 Toxins --  2.4.3.7 High-throughput generation of reagents for proteomics --  2.4.4 Advances in selection technology --  2.5 Library Screening --  2.5.1 Primary screening methods 2.5.2 Secondary screening methods2.5.3 High-throughput antibody purification --  2.6 Future Applications of Antibody Phage Display --  2.6.1 Antibody phage display in the proteomics arena --  2.6.2 Quality protein reagents --  2.6.3 Affinity maturation of antibody outputs --  2.6.4 Antibody format and production --  2.7 Conclusions --  References --  Chapter 3 Affinity Maturation Approaches for Antibody Lead Optimization David Lowe, Trevor Wilkinson and Tristan J. Vaughan --  3.1 Introduction --  3.2 Measuring the Affinity of Antibody-Antigen Complexes --  3.2.1 Improving antibody affinity and potency
UR  - http://repository.fue.edu.eg/xmlui/handle/123456789/1826
ER  -