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University of Illinois at Urbana-Champaign
Molecular Engineering of a Single-Chain FV Antibody Fragment to Femtomolar Affinity
Abstract
dc:descriptionMutants 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.
Degree
thesis:*- Name thesis:degree_name
- Ph.D.
- Level thesis:degree_level
- Dissertation
- Discipline thesis:degree_discipline
- Chemical Engineering
- Grantor
- University of Illinois at Urbana-Champaign
- Year dc:date
- 2015
Author and committee
dc:creator, dc:contributor.*- Author dc:creator
-
- Boder, Eric Thomas
- Contributors dc:contributor
-
- Wittrup, K. Dane
Subjects
dc:subject × 1Rights
- Language dc:language
- eng
Identifiers
dc:identifier.*- Identifier
- (MiAaPQ)AAI9921662
- OAI identifier oai:identifier
- oai:www.ideals.illinois.edu:2142/82463