This is an old revision of this page, as edited by Jdevola (talk | contribs) at 13:28, 15 February 2011 (clarify link). The present address (URL) is a permanent link to this revision, which may differ significantly from the current revision.
Revision as of 13:28, 15 February 2011 by Jdevola (talk | contribs) (clarify link)(diff) ← Previous revision | Latest revision (diff) | Newer revision → (diff)Identifiers | |
---|---|
CAS Number | |
3D model (JSmol) | |
ECHA InfoCard | 100.157.496 |
MeSH | Melitten |
PubChem CID | |
CompTox Dashboard (EPA) | |
SMILES
| |
Properties | |
Chemical formula | C131H229N39O31 |
Molar mass | 2846.46266 |
Except where otherwise noted, data are given for materials in their standard state (at 25 °C , 100 kPa). Infobox references |
Melittin is the principal active component of bee venom (apitoxin), and is a powerful stimulator of phospholipase A2. Melittin is a peptide consisting of 26 amino acids with the sequence GIGAVLKVLTTGLPALISWIKRKRQQ.
Therapeutic Use
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 (Lubke & Garon, 1997). Melittin has also been shown to kill the yeast Candida albicans and to suppress Mycoplasma hominis and Chlamydia trachomatis infections.
At Washington University School of Medicine in St. Louis, very small nanite "nanobee" devices are being used to carefully deliver melittin, which is known to disrupt cellular walls and thus destroy cells, to tumor cells.
References
- Melitten - Compound Summary, PubChem.
- Klotz SA, Gaur NK, Rauceo J, Lake DF, Park Y, Hahm KS, Lipke PN. "Inhibition of adherence and killing of Candida albicans with a 23-Mer peptide (Fn/23) with dual antifungal properties." Antimicrobial Agents and Chemotherapy. 2004 Nov;48(11):4337-41. PMID 15504862. Accessed November 11, 2007.
- Lazarev VN, Shkarupeta MM, Titova GA, Kostrjukova ES, Akopian TA, Govorun VM. "Effect of induced expression of an antimicrobial peptide melittin on Chlamydia trachomatis and Mycoplasma hominis infections in vivo." Biochemical and Biophysical Research Commununications. 2005 Dec 16;338(2):946-50. PMID 16246304
- Lazarev VN, Stipkovits L, Biro J, Miklodi D, Shkarupeta MM, Titova GA, Akopian TA, Govorun VM. "Induced expression of the antimicrobial peptide melittin inhibits experimental infection by Mycoplasma gallisepticum in chickens." Microbes and Infection. 2004 May;6(6):536-41. PMID 15158186
- Lazarev VN, Parfenova TM, Gularyan SK, Misyurina OY, Akopian TA, Govorun VM. "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. 2002 Feb;19(2):133-7. PMID 11850166
- Targeting Cancer With Bee Venom""
External links
- Melitten at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
This pharmacology-related article is a stub. You can help Misplaced Pages by expanding it. |
Protein: cell membrane proteins (other than Cell surface receptor, enzymes, and cytoskeleton) | |
---|---|
Arrestin | |
Membrane-spanning 4A | |
Myelin | |
Pulmonary surfactant | |
Tetraspanin | |
Other/ungrouped | |
see also other cell membrane protein disorders |
Pore-forming toxins (TC 1C) | |
---|---|
Antimicrobial cationic peptides | |
Other, human | |
Other, nonhuman |