Engineered antibodies

Engineered antibodies now represent over 30% of biopharmaceuticals in clinical trials, as highlighted by recent approvals from the US Food and Drug Administration. Recombinant antibodies have been reduced in size, rebuilt into multivalent molecules and fused with, for example radionuclides, toxins,...

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Bibliographic Details
Published inNature medicine Vol. 9; no. 1; pp. 129 - 134
Main Authors Hudson, Peter J, Souriau, Christelle
Format Journal Article
LanguageEnglish
Published United States Nature Publishing Group 01.01.2003
Subjects
Animals
Antibodies - immunology
Antibodies - metabolism
Antibodies, Bispecific - immunology
Antibodies, Bispecific - metabolism
Antibody Affinity
Antibody Specificity
Antigens
Binding Sites, Antibody
Cancer therapies
Clinical trials
Design
Enzymes
FDA approval
Humans
Immunoglobulin Fragments - immunology
Immunoglobulin Fragments - metabolism
Immunotherapy
Mice
Mice, Transgenic
Models, Immunological
Monoclonal antibodies
Peptide Library
Pharmacokinetics
Protein Binding
Protein Engineering
Reagents
Recombinant Proteins - immunology
Recombinant Proteins - metabolism
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Summary:Engineered antibodies now represent over 30% of biopharmaceuticals in clinical trials, as highlighted by recent approvals from the US Food and Drug Administration. Recombinant antibodies have been reduced in size, rebuilt into multivalent molecules and fused with, for example radionuclides, toxins, enzymes, liposomes and viruses. The emergence of recombinant technologies has revolutionized the selection, humanization and production of antibodies, superseding hybridoma technology and allowing the design of antibody-based reagents of any specificity and for very diverse purposes.
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ISSN:1078-8956
1546-170X
DOI:10.1038/nm0103-129