Sequenzanalyse des Melittins aus den tryptischen und peptischen Spaltstücken

Abstract

Melittin, the toxic main peptide from bee venom, possesses the following primary structure, resulting from analysis of the tryptic and peptic fragments and from partial Edman degradation of the intact peptide: Gly-Ile-Gly-Ala-Val-Leu-Lys-Val-Leu-Thr-Thr-Gly-Leu-Pro-Ala-Leu-Ile-Ser-Trp-Ue-Lys-Arg-Lys-Arg-Gln-Gln-NH2. Some hydrolysis products, originating in, small amounts, argue for further peptides accompanying some melittin fractions; they are substituted at the N-terminus by a still unknown residue and/or differ from melittin by some amino acid residues. The construction principle of the melittin molecule is to be seen in the extremely unequal distribution of preponderantly hydrophobic, neutral (pos. 1-20) and hydrophilic, mostly basic (21-26) amino acyls. The pharmacological and biochemical effects of melittin depend on its tenside character which again results from its primary structure. Thus, melittin is the first peptide whose biological effects can be understood on the basis of its primary structure.