Literature DB >> 17139559

Melittin: a membrane-active peptide with diverse functions.

H Raghuraman1, Amitabha Chattopadhyay.   

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.

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Year:  2007        PMID: 17139559     DOI: 10.1007/s10540-006-9030-z

Source DB:  PubMed          Journal:  Biosci Rep        ISSN: 0144-8463            Impact factor:   3.840


  144 in total

1.  The dynamics of melittin-induced membrane permeability.

Authors:  Gašper Kokot; Mojca Mally; Saša Svetina
Journal:  Eur Biophys J       Date:  2012-03-24       Impact factor: 1.733

2.  Melittin-lipid bilayer interactions and the role of cholesterol.

Authors:  Per Wessman; Adam A Strömstedt; Martin Malmsten; Katarina Edwards
Journal:  Biophys J       Date:  2008-07-25       Impact factor: 4.033

3.  The micelle-associated 3D structures of Boc-Y(SO3)-Nle-G-W-Nle-D-2-phenylethylester (JMV-180) and CCK-8(s) share conformational elements of a calculated CCK1 receptor-bound model.

Authors:  Mohanraja Kumar; Joseph R Reeve; Weidong Hu; Laurence J Miller; David A Keire
Journal:  J Med Chem       Date:  2008-06-10       Impact factor: 7.446

4.  Melittin modulates keratinocyte function through P2 receptor-dependent ADAM activation.

Authors:  Anselm Sommer; Anja Fries; Isabell Cornelsen; Nancy Speck; Friedrich Koch-Nolte; Gerald Gimpl; Jörg Andrä; Sucharit Bhakdi; Karina Reiss
Journal:  J Biol Chem       Date:  2012-05-21       Impact factor: 5.157

5.  Interaction of 18-residue peptides derived from amphipathic helical segments of globular proteins with model membranes.

Authors:  Chandrasekaran Sivakamasundari; Ramakrishnan Nagaraj
Journal:  J Biosci       Date:  2009-06       Impact factor: 1.826

6.  On the mechanism of pore formation by melittin.

Authors:  Geert van den Bogaart; Jeanette Velásquez Guzmán; Jacek T Mika; Bert Poolman
Journal:  J Biol Chem       Date:  2008-09-25       Impact factor: 5.157

7.  The structure of a melittin-stabilized pore.

Authors:  John M Leveritt; Almudena Pino-Angeles; Themis Lazaridis
Journal:  Biophys J       Date:  2015-05-19       Impact factor: 4.033

8.  Structural basis for the geometry-driven localization of a small protein.

Authors:  Richard L Gill; Jean-Philippe Castaing; Jen Hsin; Irene S Tan; Xingsheng Wang; Kerwyn Casey Huang; Fang Tian; Kumaran S Ramamurthi
Journal:  Proc Natl Acad Sci U S A       Date:  2015-03-30       Impact factor: 11.205

9.  Antitumour action on human glioblastoma A1235 cells through cooperation of bee venom and cisplatin.

Authors:  Goran Gajski; Tamara Čimbora-Zovko; Sanjica Rak; Maja Osmak; Vera Garaj-Vrhovac
Journal:  Cytotechnology       Date:  2015-04-28       Impact factor: 2.058

10.  Analysis of cytotoxicity of melittin on adherent culture of human endothelial cells reveals advantage of fluorescence microscopy over flow cytometry and haemocytometer assay.

Authors:  Katarina Černe; Andreja Erman; Peter Veranič
Journal:  Protoplasma       Date:  2013-02-28       Impact factor: 3.356

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