Melittin (trifluoroacetate salt)
目录号 : GC49546
The principal cytotoxic component of bee venom
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
- View current batch:
- Purity: >95.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
Melittin is a small protein that is the principal cytotoxic component of venom of the honey bee, A. mellifera.1 Structurally, melittin consists of two α-helical segments forming a bent rod, with hydrophilic residues on the convex side and hydrophobic sites on the concave side.1,2 This allows melittin molecules to assemble as tetramers on membrane surfaces and form pores, resulting in cell death. Bee venom is also known to stimulate phospholipase A2 (PLA2) activity, and this may be linked to melittin-mediated pore production as well as the presence of low molecular weight PLA2 enzymes in the venom.2,3 Melittin also has antimicrobial properties, which, combined with its cytolytic properties, extends its potential for therapeutic applications.3
1.Terwilliger, T.C., and Eisenberg, D.The structure of melittin. II. Interpretation of the structureThe Journal of Biological Chemisty257(11)6016-6022(1982) 2.Kourie, J.I., and Shorthouse, A.A.Properties of cytotoxic peptide-formed ion channelsAmerican Journal of Physiology.Cell Physiology278C1063-C1087(2000) 3.Moreno, M., and Giralt, E.Three valuable peptides from bee and wasp venoms for therapeutic and biotechnological use: Melittin, apamin and mastoparanToxins71126-1150(2015)
| Cas No. | N/A | SDF | Download SDF |
| Canonical SMILES | NC([C@H](CCC(N)=O)NC([C@H](CCC(N)=O)NC([C@H](CCCNC(N)=N)NC([C@H](CCCCN)NC([C@H](CCCNC(N)=N)NC([C@H](CCCCN)NC([C@@]([C@H](CC)C)([H])NC([C@@H](NC([C@H](CO)NC([C@@]([C@H](CC)C)([H])NC([C@H](CC(C)C)NC([C@@H](NC([C@@H]1CCCN1C([C@H](CC(C)C)NC(CNC([C@@]([C@@H](C)O)([H])NC([C@@]([C@@H](C)O)([H])NC([C@H](CC(C)C)NC([C@H](C(C)C)NC([C@H](CCCCN)NC([C@H](CC(C)C)NC([C@H](C(C)C)NC([C@@H](NC(CNC([C@@]([C@H](CC)C)([H])NC(CN[H])=O)=O)=O)C)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)C)=O)=O)=O)=O)CC2=CNC3=C2C=CC=C3)=O)=O)=O)=O)=O)=O)=O)=O.OC(C(F)(F)F)=O | ||
| 分子式 | C131H229N39O31 • XCF3COOH | 分子量 | 2846.5 |
| 溶解度 | DMF: 25 mg/ml,DMSO: 25 mg/ml,PBS (pH 7.2): 3 mg/ml | 储存条件 | -20°C |
| General tips | 请根据产品在不同溶剂中的溶解度选择合适的溶剂配制储备液；一旦配成溶液，请分装保存，避免反复冻融造成的产品失效。 储备液的保存方式和期限：-80°C 储存时，请在 6 个月内使用，-20°C 储存时，请在 1 个月内使用。 为了提高溶解度，请将管子加热至37℃，然后在超声波浴中震荡一段时间。 |
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| Shipping Condition | 评估样品解决方案：配备蓝冰进行发货。所有其他可用尺寸：配备RT，或根据请求配备蓝冰。 | ||
| 制备储备液 | |||
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1 mg | 5 mg | 10 mg |
| 1 mM | 0.3513 mL | 1.7565 mL | 3.5131 mL |
| 5 mM | 0.0703 mL | 0.3513 mL | 0.7026 mL |
| 10 mM | 0.0351 mL | 0.1757 mL | 0.3513 mL |
| 第一步：请输入基本实验信息（考虑到实验过程中的损耗，建议多配一只动物的药量） | ||||||||||
| 给药剂量 | mg/kg |  |
动物平均体重 | g | |
每只动物给药体积 | ul | |
动物数量 | 只 |
| 第二步：请输入动物体内配方组成（配方适用于不溶于水的药物；不同批次药物配方比例不同，请联系GLPBIO为您提供正确的澄清溶液配方） | ||||||||||
| % DMSO % % Tween 80 % saline | ||||||||||
| 计算重置 | ||||||||||
计算结果:
工作液浓度： mg/ml；
DMSO母液配制方法： mg 药物溶于 μL DMSO溶液（母液浓度 mg/mL，
体内配方配制方法：取 μL DMSO母液，加入 μL PEG300，混匀澄清后加入μL Tween 80，混匀澄清后加入 μL saline，混匀澄清。
1. 首先保证母液是澄清的；
2.
一定要按照顺序依次将溶剂加入，进行下一步操作之前必须保证上一步操作得到的是澄清的溶液，可采用涡旋、超声或水浴加热等物理方法助溶。
3. 以上所有助溶剂都可在 GlpBio 网站选购。
Perchlorate-induced formation of the alpha-helical structure of mastoparan
J Biochem 1994 Oct;116(4):910-5.PMID:7883768DOI:10.1093/oxfordjournals.jbchem.a124615.
Mastoparan, a basic tetradecapeptide from wasp venom, has been considered to be unfolded under aqueous conditions. On the basis of the far-UV circular dichroism spectrum, we found that sodium perchlorate at molar concentrations stabilizes an alpha-helical structure of mastoparan. To understand the mechanism of the perchlorate-induced stabilization of the alpha-helical structure, we synthesized a dimeric form of mastoparan derivative, which was linked at the C terminal by a disulfide bond. The linkage decreased the concentration of perchlorate required to stabilize the alpha-helical structure by 30-fold. With the dimeric mastoparan derivative, we measured the effects of several salts such as sodium trichloroacetate, sodium trifluoroacetate, and sodium chloride. The concentration of salts required to induce the conformational transition varied and the order of effectiveness of different salts was consistent with the electroselectivity series of anions toward anion-exchange resins, indicating that the anion binding to the positively charged amino groups is responsible for the transition. These results suggest that the salt-induced formation of the alpha-helical state of mastoparan can be explained by a mechanism similar to that proposed for the salt-induced conformational transition of Melittin.
Acyl transfer from membrane lipids to peptides is a generic process
J Mol Biol 2013 Nov 15;425(22):4379-87.PMID:23871685DOI:10.1016/j.jmb.2013.07.013.
The generality of acyl transfer from phospholipids to membrane-active peptides has been probed using liquid chromatography-mass spectrometry analysis of peptide-lipid mixtures. The peptides examined include Melittin, magainin II, PGLa, LAK1, LAK3 and penetratin. Peptides were added to liposomes with membrane lipid compositions ranging from pure phosphatidylcholine (PC) to mixtures of PC with phosphatidylethanolamine, phosphatidylserine or phosphatidylglycerol. Experiments were typically conducted at pH7.4 at modest salt concentrations (90 mM NaCl). In favorable cases, lipidated peptides were further characterized by tandem mass spectrometry methods to determine the sites of acylation. Melittin and magainin II were the most reactive peptides, with significant acyl transfer detected under all conditions and membrane compositions. Both peptides were lipidated at the N-terminus by transfer from PC, phosphatidylethanolamine, phosphatidylserine or phosphatidylglycerol, as well as at internal sites: lysine for Melittin; serine and lysine for magainin II. Acyl transfer could be detected within 3h of Melittin addition to negatively charged membranes. The other peptides were less reactive, but for each peptide, acylation was found to occur in at least one of the conditions examined. The data demonstrate that acyl transfer is a generic process for peptides bound to membranes composed of diacylglycerophospholipids. Phospholipid membranes cannot therefore be considered as chemically inert toward peptides and by extension proteins.