User:Kaguya-Taketori/蜂毒肽
蜂毒肽 | |||||||||
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![]() 蜂毒肽 | |||||||||
鑑定 | |||||||||
標誌 | 蜂毒肽 | ||||||||
Pfam | PF01372(旧版) | ||||||||
InterPro | IPR002116 | ||||||||
SCOP | 2mlt / SUPFAM | ||||||||
TCDB | 1.C.18 | ||||||||
OPM家族 | 160 | ||||||||
OPM蛋白 | 2mlt | ||||||||
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Kaguya-Taketori/蜂毒肽[1] | |
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识别 | |
CAS号 | 20449-79-0 ![]() |
PubChem | 16133648 |
ChemSpider | 17290230 |
SMILES |
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InChI |
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InChIKey | VDXZNPDIRNWWCW-JFTDCZMZBB |
ChEBI | 6736 |
MeSH | Melitten |
性质 | |
化学式 | C131H229N39O31 |
摩尔质量 | 2846.46266 g·mol⁻¹ |
若非注明,所有数据均出自标准状态(25 ℃,100 kPa)下。 |
蜂毒肽(Melittin)係蜂毒中的主要有效成分。它能夠對Phospholipase A2產生強烈的刺激作用。蜂毒肽是由26個氨基酸構成的多肽,其序列爲「GIGAVLKVLTTGLPALISWIKRKRQQ」。
生物效應
[编辑]蜂毒肽能抑制蛋白激酶C、鈣離子(Ca2+)/鈣調蛋白依賴性蛋白激酶II、肌球蛋白輕鏈激酶,以及突觸膜上的鈉鉀泵的活性。它還能夠使細胞膜裂解。蜂毒肽是一種沒有二硫鍵的小分子肽。蜂毒肽分子的N端主要體現疏水性,而該分子的C端則主要體現親水性,而且具有強鹼性。
Extensive work with melittin has shown that the venom has multiple effects, probably, as a result of its interaction with negatively charged 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]
Potential therapeutic applications
[编辑]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] In February 2013, it was reported that nanoparticles carrying melittin were effective in destroying HIV by eroding the double-layer viral envelope surrounding the virus. Possible applications include a vaginal gel that would target HIV intrusion prior to infection and as an intravenous treatment of extant HIV infections.[9]
It has been suggested that the regulation of S100B by melittin has potential for the treatment of epilepsy.[10]
References
[编辑]- ^ Melitten - Compound Summary, PubChem.
- ^ Yang S, Carrasquer G. Effect of melittin on ion transport across cell membranes. Zhongguo Yao Li Xue Bao. January 1997, 18 (1): 3–5. PMID 10072885.
- ^ Lubke LL, Garon CF. The antimicrobial agent melittin exhibits powerful in vitro inhibitory effects on the Lyme disease spirochete. Clin. Infect. Dis. July 1997, 25 (Suppl 1): S48–51. PMID 9233664. doi:10.1086/516165.
- ^ 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. Antimicrob. Agents Chemother. November 2004, 48 (11): 4337–41. PMC 525394
. PMID 15504862. doi:10.1128/AAC.48.11.4337-4341.2004.
- ^ 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. Biochem. Biophys. Res. Commun. December 2005, 338 (2): 946–50. PMID 16246304. doi:10.1016/j.bbrc.2005.10.028.
- ^ 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 Infect. May 2004, 6 (6): 536–41. PMID 15158186. doi:10.1016/j.micinf.2004.02.006.
- ^ 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. Int. J. Antimicrob. Agents. February 2002, 19 (2): 133–7. PMID 11850166. doi:10.1016/S0924-8579(01)00479-4.
- ^ The Buzz: Targeting Cancer With Bee Venom. Wall Street Journal. September 28, 2009.
- ^ Hood JL, Jallouk AP, Campbell N, Ratner L, Wickline SA. Cytolytic nanoparticles attenuate HIV-1 infectivity. Antiviral therapy. 2013, 18 (1): 95–103. PMID 22954649. doi:10.3851/IMP2346. 简明摘要 – Washington University in St. Louis (March 7, 2013).
- ^ Verma N, Karmakar M, Singh KP, Smita S. Structural and Dynamic Insights into S100B Protein Activity Inhibition by Melittin for the Treatment of Epilepsy. International journal of Computer Application. February 2013,. NSAAILS (1): 55–60. ISSN 0975-8887.
External links
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