Crabrolin

Crabrolin
	Existing structural data: s. UniProt
Mass / length primary structure	13 amino acids
Identifier
External IDs	UniProt : P01518 ;
Occurrence
Parent taxon	Hornets

Crabrolin is an antimicrobial polypeptide found in the poison of hornets (Vespa) , which consists of 13 amino acids . The substance was first isolated in 1984 by Antonio Argiolas and John J. Pisano and its structure was described.

The amino sequence is: FLPLILRKIVTAL-NH ₂ (the last leucine is leucine amide)

Crabrolin has an antimicrobial effect , especially against gram-negative bacteria . It also shows hemolytic activity.

Individual evidence

↑ A. Argiolas, JJ Pisano: Isolation and characterization of two new peptides, mastoparan C and crabrolin, from the venom of the European hornet, Vespa crabro. In: Journal of Biological Chemistry. 259, Washington 1984, pp. 10106-10111. PMID 6206053 ; PDF (free full text access)
↑ Krishnakumari, V. and Nagaraj, R. (1997): Antimicrobial and hemolytic activities of crabrolin, a 13-residue peptide from the venom of the European hornet, Vespa crabro, and its analogs. In: J Pept Res . 50 (2); 88-93; PMID 9273892 ; doi : 10.1111 / j.1399-3011.1997.tb01173.x

[1] A. Argiolas, JJ Pisano: Isolation and characterization of two new peptides, mastoparan C and crabrolin, from the venom of the European hornet, Vespa crabro. In: Journal of Biological Chemistry. 259, Washington 1984, pp. 10106-10111. PMID 6206053 ; PDF (free full text access)

[2] Krishnakumari, V. and Nagaraj, R. (1997): Antimicrobial and hemolytic activities of crabrolin, a 13-residue peptide from the venom of the European hornet, Vespa crabro, and its analogs. In: J Pept Res . 50 (2); 88-93; PMID 9273892 ; doi : 10.1111 / j.1399-3011.1997.tb01173.x