Abstract
Identification of the smallest antibody fragment still capable of binding to antigen has progressed from full antibody molecules to Fab and recombinant single chain Fv fragments. Now, a further reduction to single domain binding proteins based upon immunoglobulin VH and VH-like domains offers exciting prospects in the development of novel immunotherapeutics and immunodiagnostics. Minimisation of the antigen-binding fragment to such small single-domain proteins offers the advantages of enhanced stability, and possibly access to a class of antigenic epitopes not generally recognised by conventional antibodies.
Keywords: Immunoglobulin VH Domains, Fv fragments, Recombinant single chain, Natural VH Domains, Camelidae, Camelisation
Current Pharmaceutical Biotechnology
Title: Immunoglobulin VH Domains and Beyond Design and Selection of Single-Domain Binding and Targeting Reagents
Volume: 1 Issue: 3
Author(s): S. D. Nuttall, R. A. Iring and P. J. Hudson
Affiliation:
Keywords: Immunoglobulin VH Domains, Fv fragments, Recombinant single chain, Natural VH Domains, Camelidae, Camelisation
Abstract: Identification of the smallest antibody fragment still capable of binding to antigen has progressed from full antibody molecules to Fab and recombinant single chain Fv fragments. Now, a further reduction to single domain binding proteins based upon immunoglobulin VH and VH-like domains offers exciting prospects in the development of novel immunotherapeutics and immunodiagnostics. Minimisation of the antigen-binding fragment to such small single-domain proteins offers the advantages of enhanced stability, and possibly access to a class of antigenic epitopes not generally recognised by conventional antibodies.
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Cite this article as:
Nuttall D. S., Iring A. R. and Hudson J. P., Immunoglobulin VH Domains and Beyond Design and Selection of Single-Domain Binding and Targeting Reagents, Current Pharmaceutical Biotechnology 2000; 1 (3) . https://dx.doi.org/10.2174/1389201003378906
DOI https://dx.doi.org/10.2174/1389201003378906 |
Print ISSN 1389-2010 |
Publisher Name Bentham Science Publisher |
Online ISSN 1873-4316 |
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