Melittin is the principal active component of apitoxin (bee venom) and is a powerful stimulator of phospholipase A2. Melittin is a peptide consisting of 26 amino acids with the sequence GIGAVLKVLTTGLPALISWIKRKRQQ.
[edit] Biological effects
Melittin inhibits protein kinase C, Ca2+/calmodulin-dependent protein kinase II, myosin light chain kinase and Na+/K+-ATPase (synaptosomal membrane) and is a cell membrane lytic factor. Melittin is a small peptide with no disulphide bridge; the N-terminal part of the molecule is predominantly hydrophobic and the C-terminal part is hydrophilic and strongly basic.
Extensive work with melittin has shown that the venom has multiple effects, probably, as a result of its interaction with negatively changed phospholipids. It inhibits well known transport pumps such as the Na+-K+-ATPase and the H+-K+-ATPase. Melittin increases the permeability of cell membranes to ions, particularly Na+ and indirectly Ca2+, because of the Na+-Ca2+-exchange. This effect results in marked morphological and functional changes, particularly in excitable tissues such as cardiac myocytes. In some other tissues, e.g., cornea, not only Na+ but Cl- permeability is also increased by melittin. Similar effects to melittin on H+-K+-ATPase have been found with the synthetic amphipathic polypeptide Trp-3.[2]
Melittin also exhibits potent anti-microbial activity. For example, melittin has been shown to exert "profound inhibitory effects" on Borrelia burgdorferi, the bacteria that causes lyme disease.[3] Melittin has also been shown to kill the yeast Candida albicans[4] and to suppress Mycoplasma hominis and Chlamydia trachomatis infections.[5][6][7]
At Washington University School of Medicine in St. Louis, very small nanite "nanobee" devices are being developed to carefully deliver melittin, which is known to disrupt cellular walls and thus destroy cells, to tumor cells in animals.[8]
[edit] Melittin in Art
Melittin (2009) by
Julian Voss-Andreae. The pictured melittin sculpture is part of a series called "The Building Blocks of Life".
Artist and scientist Julian Voss-Andreae has created a sculpture based on the structure of melittin, which he mentions in a talk about his work.[9]
[edit] References
- ^ Melitten - Compound Summary, PubChem.
- ^ Yang S, Carrasquer G (January 1997). "Effect of melittin on ion transport across cell membranes". Zhongguo Yao Li Xue Bao 18 (1): 3-5. PMID 10072885.
- ^ Lubke, LL; Garon, CF (1997). "The antimicrobial agent melittin exhibits powerful in vitro inhibitory effects on the Lyme disease spirochete". Clinical infectious diseases : an official publication of the Infectious Diseases Society of America 25 Suppl 1: S48–51. doi:10.1086/516165. PMID 9233664.
- ^ Klotz, SA; Gaur, NK; Rauceo, J; Lake, DF; Park, Y; Hahm, KS; Lipke, PN (2004). "Inhibition of adherence and killing of Candida albicans with a 23-Mer peptide (Fn/23) with dual antifungal properties". Antimicrobial agents and chemotherapy 48 (11): 4337–41. doi:10.1128/AAC.48.11.4337-4341.2004. PMC 525394. PMID 15504862. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=525394.
- ^ Lazarev, VN; Shkarupeta, MM; Titova, GA; Kostrjukova, ES; Akopian, TA; Govorun, VM (2005). "Effect of induced expression of an antimicrobial peptide melittin on Chlamydia trachomatis and Mycoplasma hominis infections in vivo". Biochemical and biophysical research communications 338 (2): 946–50. doi:10.1016/j.bbrc.2005.10.028. PMID 16246304.
- ^ Lazarev, VN; Stipkovits, L; Biro, J; Miklodi, D; Shkarupeta, MM; Titova, GA; Akopian, TA; Govorun, VM (2004). "Induced expression of the antimicrobial peptide melittin inhibits experimental infection by Mycoplasma gallisepticum in chickens". Microbes and infection / Institut Pasteur 6 (6): 536–41. doi:10.1016/j.micinf.2004.02.006. PMID 15158186.
- ^ Lazarev, VN; Parfenova, TM; Gularyan, SK; Misyurina, OY; Akopian, TA; Govorun, VM (2002). "Induced expression of melittin, an antimicrobial peptide, inhibits infection by Chlamydia trachomatis and Mycoplasma hominis in a HeLa cell line". International journal of antimicrobial agents 19 (2): 133–7. PMID 11850166.
- ^ "The Buzz: Targeting Cancer With Bee Venom". Wall Street Journal. September 28, 2009. http://online.wsj.com/article/SB10001424052970203803904574433382922095534.html?mod=WSJ_hpp_MIDDLENexttoWhatsNewsThird.
- ^ Julian Voss-Andreae (March 27, 2011) (in English). Julian Voss-Andreae: Quantum Sculptures. London, UK: ISIS. http://vimeo.com/24156278.
[edit] External links
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