Purification and chemical characterization of melittin and acetylated derivatives.

Journal Article (Journal Article)

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.

Full Text

Duke Authors

Cited Authors

  • Maulet, Y; Mathey-Prevot, B; Kaiser, G; Rüegg, UT; Fulpius, BW

Published Date

  • October 21, 1980

Published In

Volume / Issue

  • 625 / 2

Start / End Page

  • 274 - 280

PubMed ID

  • 7437462

International Standard Serial Number (ISSN)

  • 0006-3002

Digital Object Identifier (DOI)

  • 10.1016/0005-2795(80)90291-3


  • eng

Conference Location

  • Netherlands