Raghuraman, H. ; Chattopadhyay, Amitabha (2007) Melittin: a membrane-active peptide with diverse functions Bioscience Reports, 27 (4-5). pp. 189-223. ISSN 0144-8463
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Official URL: http://www.springerlink.com/content/980826550rh77h...
Related URL: http://dx.doi.org/10.1007/s10540-006-9030-z
Abstract
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.
Item Type: | Article |
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Source: | Copyright of this article belongs to Portland Press Limited. |
Keywords: | Melittin; Hemolysis; Tryptophan Fluorescence; Lipid-Protein Interactions; Melittin Orientation; Aggregation and Pores |
ID Code: | 7067 |
Deposited On: | 25 Oct 2010 12:42 |
Last Modified: | 16 May 2016 17:19 |
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