| Literature DB >> 15589829 |
Michaela A E Arndt1, Jürgen Krauss, Susanna M Rybak.
Abstract
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 degrees C, 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.Entities:
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Year: 2004 PMID： 15589829 DOI： 10.1016/j.febslet.2004.11.011
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124