Melittin

Literature References: Strongly basic polypeptide, the principal component of the venom of the honey bee, Apis mellifica (mellifera), comprising 40-50% of the dried venom. A "direct" hemolysin, one of the hemolytic principles present in the venom, the other being "indirect" acting phospholipase A. Sepn and isoln: Neumann et al., Naturwissenschaften 39, 286 (1952); Neumann, Haberman, Arch. Exp. Pathol. Pharmakol. 222, 367 (1954); Habermann, Reiz, Biochem. Z. 341, 451 (1965). Melittin is the first polypeptide whose biological effects can be understood on the basis of its primary structure. Elucidation of structure and correlation with activity: E. Habermann, J. Jentsch, Z. Physiol. Chem. 348, 37 (1967). Conformation studies: R. Bazzo et al., Eur. J. Biochem. 173, 139 (1988). About 10% of the melittin is thought to be formylated at the N-terminus: Kreil, Kreil-Kiss, Biochem. Biophys. Res. Commun. 27, 275 (1967). Isoln and structure of Na-formyl melittin: Lübke et al., Experientia 27, 765 (1971). Synthesis of melittin and related peptides: Lübke, Schröder, Peptides, H. C. Beyerman, A. van der Linde, W. M. van den Brink, Eds. (North-Holland Publishing Company, Amsterdam, 1967) pp 271-279; Dorman, Markley, J. Med. Chem. 14, 5 (1970); Schröder et al., Experientia 27, 764 (1971). Solid phase synthesis and purification: M. T. Tosteson et al., Biochemistry 26, 6627 (1987). Review of biochemistry and pharmacology: Habermann, Science 177, 314 (1972).