AA sequence: GIGAVLKVLTTGLPALISWIKRKRQQ-NH2
Length (aa): 26
Formula: C131H229N39O31
Molecular Weight: 2846,56 Da
Appearance: white lyophilized solid
Solubility: water or saline buffer
CAS number: 20449-79-0
Source: synthetic
Purity rate: > 95 %
Melittin
Highly pure synthetic Melittin
Melittin is a major constituent of the bee venom of Apis mellifera. The N-terminal part of Melittin is hydrophobic and the C-terminal part is hydrophilic. Melittin accumulates in cell membrane which leads to various effects. It can be used to study lipid-protein interactions in membranes. Melittin has demonstrated interesting properties in pre-clinical studies as antimicrobial substance, as drug against rheumatoid arthritis, arteriosclerosis, cancer or as drug delivery system. Smartox Biotechnology offers highly pure synthetic Melittin.
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- Apamin: SK channel blocker from bee venom
Three Valuable Peptides from Bee and Wasp Venoms for Therapeutic and biotechnological Use: Melittin, Apamin and Mastoparan.
Moreno M. and Giralt E. (2015) Three Valuable Peptides from Bee and Wasp Venoms for Therapeutic and biotechnological Use: Melittin, Apamin and Mastoparan. Toxins. PubMed link
While knowledge of the composition and mode of action of bee and wasp venoms dates back 50 years, the therapeutic value of these toxins remains relatively unexploded. The properties of these venoms are now being studied with the aim to design and develop new therapeutic drugs. Far from evaluating the extensive number of monographs, journals and books related to bee and wasp venoms and the therapeutic effect of these toxins in numerous diseases, the following review focuses on the three most characterized peptides, namely melittin, apamin, and mastoparan. Here, we update information related to these compounds from the perspective of applied science and discuss their potential therapeutic and biotechnological applications in biomedicine.
Conformational States of Melittin at a Bilayer Interface.
Andersson M. et al. (2013) Conformational States of Melittin at a Bilayer Interface. Biophysical J. PubMed link
The distribution of peptide conformations in the membrane interface is central to partitioning energetics. Molecular-dynamics simulations enable characterization of in-membrane structural dynamics. Here, we describe melittin partitioning into dioleoylphosphatidylcholine lipids using CHARMM and OPLS force fields. Although the OPLS simulation failed to reproduce experimental results, the CHARMM simulation reported was consistent with experiments. The CHARMM simulation showed melittin to be represented by a narrow distribution of folding states in the membrane interface.
Melittin: a membrane-active peptide with diverse functions
Raghuraman H., Chattopadhyay A. (2007) Melittin: a membrane-active peptide with diverse functions. Biosci Rep. PubMed link
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 melittinbeing used as a suitable model peptide for monitoring lipid-protein interactions in membranes. In this review, the solution and membrane properties ofmelittin are highlighted, with an emphasis on melittin-membrane interaction using biophysical approaches. The recent applications of melittin in various cellular processes are discussed.
The actions of melittin on membranes
Dempsey CE (1990) The actions of melittin on membranes. Biochim Biophys Acta. PubMed link
The molecular mechanisms underlying the various effects of melittin on membranes have not been completely defined and much of the evidence described indicates that different molecular mechanisms may underlie different actions of the peptide. Ideas about the formation of transbilayer aggregates of melittin under the influence of a transbilayer potential, and for bilayer structural perturbation arising from the location of the peptide helix within the head group region of the membrane have been made based on the crystal structure of the peptide, the kinetics and concentration dependence of melittins membrane actions, together with simple ideas about the conformational properties of amphipathic helical peptides and their interactions with membranes…