Abstract
Two peptides rich in hydrophobic amino acids have been isolated from venom sacs of the European hornet, Vespa crabro. One peptide (P-2) is structurally and functionally related to the tetradecapeptide mastoparan and has been named mastoparan C. Leu-Asn-Leu-Lys-Ala-Leu-Leu-Ala-Val-Ala-Lys-Lys-Ile-LeuNH2. The other (P-1) is a tridecapeptide with a new sequence: Phe-Leu-Pro-Leu-Ile-Leu-Arg-Lys-Ile-Val-Thr-Ala-LeuNH2 which we have named crabrolin. The peptide releases histamine from rat peritoneal mast cells with a threshold of approximately 2.5 micrograms/ml (congruent to 8 microM). Crabrolin also facilitates the action of purified phospholipase A2 from different sources, but it is not quite as active as mastoparan. It is clearly less active than mastoparan in lysing erythrocytes, and it does not release amylase from dispersed guinea pig pancreatic acini. Given its unique sequence, the principal effect of crabrolin may be neither mast cell degranulation nor phospholipase facilitation, but a yet undiscovered action.
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