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Studies on the Combining Sites of the Protein Antigen Silk Fibroin

III. INHIBITION OF THE SILK FIBROIN-ANTIFIBROIN SYSTEM BY PEPTIDES DERIVED FROM THE ANTIGEN

From The Rockefeller Institute, New York City, New York

Abstract

1. The octapeptide Gly(Gly₃,Ala₃)Tyr was the most effective inhibitor of the fibroin-rabbit antifibroin precipitin reaction among the peptides tested that ranged in size from tetra- to octapeptides (40% inhibition at 5–18 µm/ml).

2. The tetrapeptides were considerably less effective than Gly(Gly₃,Ala₃)Tyr although one of them, Gly(Gly,Ala)Tyr (20% inhibition at 18–20 µm/ml) has the same qualitative amino acid composition as the most effective octapeptide inhibitor.

3. The dodecapeptide fraction was the most active of the peptides compared, giving 50% inhibition at 5–8 µm/ml.

4. Removal of carboxyl-terminal tyrosine from the active octapeptides resulted in a halving of their effectiveness as inhibitors.

5. The results indicate that, although tyrosine appears to account for a disproportionate part of the binding of peptide to antibody, a sizable segment (at least 8 to 12 residues) of the glycyl, alanyl chain is involved in specific combination.

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