Molecular Engineering of a Single-Chain FV Antibody Fragment to Femtomolar Affinity
Boder, Eric Thomas
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https://hdl.handle.net/2142/82463
Description
Title
Molecular Engineering of a Single-Chain FV Antibody Fragment to Femtomolar Affinity
Author(s)
Boder, Eric Thomas
Issue Date
1999
Doctoral Committee Chair(s)
Wittrup, K. Dane
Department of Study
Chemical Engineering
Discipline
Chemical Engineering
Degree Granting Institution
University of Illinois at Urbana-Champaign
Degree Name
Ph.D.
Degree Level
Dissertation
Keyword(s)
Biology, Molecular
Language
eng
Abstract
Mutants of anti-fluorescein scFv antibody 4-4-20 improved more than 1000-fold with respect to ligand dissociation kinetics and equilibrium binding affinity have been isolated from mutagenized libraries displayed on yeast and screened by flow cytometry. Analysis of the nature of mutations conferring binding improvements suggests a potentially general strategy for engineering scFv antibodies for high affinity binding to target ligands. The results of these studies clearly demonstrate the robustness of the yeast surface display system for quantitatively optimizing recognition parameters of biological macromolecules.
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