Journal
FEBS LETTERS
Volume 578, Issue 3, Pages 257-261Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2004.11.011
Keywords
CD22; single chain Fv; diabody; dimer; stability
Funding
- NCI NIH HHS [N01-CO-12400] Funding Source: Medline
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By varying linker length and domain orientation three multivalent derivatives of a monovalent anti-CD22 single-chain fragment variable (scFv) antibody were generated. Shortening the linker of the V-H-V-L oriented scFv to 5 or 0 residues resulted in the formation of diabodies or a mixture of tetramers and trimers, respectively. Unexpectedly, a V-L-0-V-H scFv assembled to homogenous dimers, remained substantially more stable than the V-H-5-V-L diabody when incubated in human serum at 37 degreesC, and retained its dimeric state when concentrated up to 4 mg/ml. These properties suggest the V-L-0-V-H scFv could become an attractive vehicle for the selective delivery of multiple effector molecules to CD22(+) tumor cells. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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