Journal
BIOSCIENCE REPORTS
Volume 27, Issue 4-5, Pages 189-223Publisher
PORTLAND PRESS LTD
DOI: 10.1007/s10540-006-9030-z
Keywords
melittin; hemolysis; tryptophan fluorescence; lipid-protein interactions; melittin orientation; aggregation and pores
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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.
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