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Science 20 May 1988:
Vol. 240. no. 4855, pp. 1034 - 1036
DOI: 10.1126/science.3368787
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Articles

Science, Vol 240, Issue 4855, 1034-1036
Copyright © 1988 by American Association for the Advancement of Science

articles

Inhibition of self-binding antibodies (autobodies) by a VH-derived peptide

CY Kang, TK Brunck, T Kieber-Emmons, JE Blalock, and H Kohler

IDEC Pharmaceuticals Corporation, La Jolla, CA 92037.

The self-binding properties of a dominant idiotypic antibody (T15) and a minor idiotypic antibody (M603), both specific for phosphorylcholine, were examined as models of self-binding antibodies (autobodies). Observed differences in the self-binding affinity of T15 and M603 relate to variable sequence differences in their respective heavy and light chains. A molecular recognition theory based on the translation of coding and noncoding DNA strands was used to identify complementary amino acid sequences responsible for self-binding. The second hypervariable region of the heavy chain domain, extending into the third framework region, was predicted as the primary self-binding locus. Among peptides synthesized with different variable heavy and light chain regions, a 24-residue peptide spanning the second hypervariable and third framework regions of the heavy chain of T15 was nearly as effective as phosphorycholine in inhibiting the self-binding complexes.


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