Bioscience Reports

, Volume 27, Issue 4–5, pp 189–223 | Cite as

Melittin: a Membrane-active Peptide with Diverse Functions

  • H. Raghuraman
  • Amitabha Chattopadhyay
Review Article


Melittin is the principal toxic component in the venom of the European honey bee Apis mellifera and is a cationic, hemolytic peptide. It is a small linear peptide composed of 26 amino acid residues in which the amino-terminal region is predominantly hydrophobic whereas the carboxy-terminal region is hydrophilic due to the presence of a stretch of positively charged amino acids. This amphiphilic property of melittin has resulted in melittin being used as a suitable model peptide for monitoring lipid–protein interactions in membranes. In this review, the solution and membrane properties of melittin are highlighted, with an emphasis on melittin–membrane interaction using biophysical approaches. The recent applications of melittin in various cellular processes are discussed.


Melittin Hemolysis Tryptophan fluorescence Lipid–protein interactions Melittin orientation Aggregation and pores 























Red edge excitation shift



Work in A.C.’s laboratory was supported by the Council of Scientific and Industrial Research, and Department of Science and Technology, Government of India. H.R. thanks the Council of Scientific and Industrial Research for the award of Research Associateship. Some of the work described in this review article was carried out by former and present members of A.C.’s group whose contribution is gratefully acknowledged. We thank members of our laboratory for critically reading the manuscript.


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© Springer Science+Business Media, LLC 2006

Authors and Affiliations

  1. 1.Centre for Cellular and Molecular BiologyHyderabadIndia

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