Abstract
Abstract Engineered single antibody domains are small (sizes about 12–14 kDa i.e. about 10-fold smaller than the size of a typical full-size antibody) and can access targets and epitopes that are not accessible by larger molecules. We have constructed two large (size 2×1010) VH-based libraries of high diversity (Chen et al, JMB, 2008, and submitted) from which several high affinity domain antibodies against HIV and cancer-related proteins were identified and characterized with potential use as therapeutics (Chen et al, PNAS, 2008, and unpublished). We have also engineered human antibody constant domains (CH2) as scaffolds which are highly stable, soluble, and express at high levels (Rui et al, JBC, 2009, and unpublished). Based on these new scaffolds several libraries have been constructed, and binders were selected and characterized (Xiao et al, BBRC, 2009; Bang et al, unpublished). Further engineering to confer additional functions (nanoantibodies) is in progress. Citation Information: Mol Cancer Ther 2009;8(12 Suppl):C188.
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