Journal
PROTEIN ENGINEERING DESIGN & SELECTION
Volume 17, Issue 4, Pages 293-304Publisher
OXFORD UNIV PRESS
DOI: 10.1093/protein/gzh038
Keywords
affinity; carcinoembryonic antigen; directed evolution; scFv; tumor targeting
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An scFv has been engineered to bind carcinoembryonic antigen (CEA) with a dissociation half-time >4 days at 37degreesC. Two mutations responsible for this affinity increase were isolated by screening yeast surface-displayed mutant libraries by flow cytometry. Soluble expression of the mutant scFv in a yeast secretion system was increased 100-fold by screening mutant libraries for improved yeast surface display level. This scFv will be useful as a limiting case for evaluating the significance of affinity in tumor targeting to noninternalizing antigens.
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