Purification and chemical characterization of melittin and acetylated derivatives.
Melittin, the main basic and hydrophobic peptide of bee venom, displays marked detergent-like properties. At high peptide concentration, and depending on salt and pH, it forms a tetramer. This is prevented by using urea. A purification procedure in presence of 4.0 M urea was developed to prepare melittin in its monomeric form, free of other venom constituents such as N alpha-formyl melittin, degradation products of peptides and phospholipase A2. NH2-residues on the melittin molecule were modified by reaction with acetic anhydride to alter the asymmetrical charge distribution supposed to confer detergent-like properties to the molecule. This gave rise to di- and mono acetyl derivatives which could be used, once isolated, to study further the melittin structure-activity relationship.
D000818:Animals; D001514:Bee Venoms / Q000302:isolation & purification*; D001516:Bees; D003902:Detergents; D008555:Melitten / Q000031:analogs & derivatives / Q000302:isolation & purification*; D008968:Molecular Conformation; D009842:Oligopeptides / Q000302:isolation & purification; D013329:Structure-Activity Relationship
D001514:Bee Venoms; D003902:Detergents; D009842:Oligopeptides; D008555:Melitten