Magainin 2
(Synonyms: 蛙皮素 2; Magainin II) 目录号 : GC30830
Magainin2是在非洲爪蟾皮肤中发现的抗微生物多肽。
Cas No.:108433-95-0
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
- View current batch:
- Purity: >99.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
Cell experiment: | Escherichia coli cells are incubated with magainin 2 (50 μg /mL). The cultures are acquired after incubation for 0, 2, 4, 6, and 8 h, respectively, and spread onto LB agar plates, and then the colony-forming units are counted after incubation for 24 h at 37°C. The percentage survival is determined relative to the control treatment[1]. |
References: [1]. Lee W, et al. Magainin 2 induces bacterial cell death showing apoptotic properties. Curr Microbiol. 2014 Dec;69(6):794-801. | |
Magainin 2 is an antimicrobial peptide discovered in the skin of Xenopus laevis.
Magainin 2 exhibits bactericidal effects and induces morphological changes in Escherichia coli regarding early apoptosis. Magainin 2 induces the expression of a bacterial protein with affinity for the caspase substrate and effects the expression of RecA as a caspase-like protein[1]. Magainin 2 kill bacteria by permeabilizing the cell membranes without exhibiting significant toxicity against mammalian cells. The main target of the peptide is considered to be the lipid matrix of the membranes. Application of 10 μg /mL magainin 2 to Paramecium caudatum, a protozoan, in pond water caused an osmotic swelling of the cell and a subsequent cell burst, suggesting that the peptide could perturb membrane functions responsible for osmotic balance[2]. Magainin 2 permeabilizes bacterial and mammalian membranes in significantly different ways. The peptide forms pores with a diameter of about 2.8 nm (less than 6.6 nm) in B. megaterium, and translocates into the cytosol. In contrast, the peptide significantly perturbes the membrane of CHO-K1 cells, permitting the entry of a large molecule (larger than 23 nm) into the cytosol, accompanied by membrane budding and lipid flip-flop, mainly accumulating in mitochondria and nuclei[3].
[1]. Lee W, et al. Magainin 2 induces bacterial cell death showing apoptotic properties. Curr Microbiol. 2014 Dec;69(6):794-801. [2]. Matsuzaki K, et al. Magainins as paradigm for the mode of action of pore forming polypeptides. Biochim Biophys Acta. 1998 Nov 10;1376(3):391-400. [3]. Imura Y, et al. Magainin 2 in action: distinct modes of membrane permeabilization in living bacterial and mammalian cells. Biophys J. 2008 Dec 15;95(12):5757-65.
| Cas No. | 108433-95-0 | SDF | |
| 别名 | 蛙皮素 2; Magainin II | ||
| Canonical SMILES | Gly-Ile-Gly-Lys-Phe-Leu-His-Ser-Ala-Lys-Lys-Phe-Gly-Lys-Ala-Phe-Val-Gly-Glu-Ile-Met-Asn-Ser | ||
| 分子式 | C114H180N30O29S | 分子量 | 2466.9 |
| 溶解度 | H2O : 50 mg/mL (20.27 mM; Need ultrasonic) | 储存条件 | -20°C, protect from light |
| 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 | 0.4054 mL | 2.0268 mL | 4.0537 mL |
| 5 mM | 0.0811 mL | 0.4054 mL | 0.8107 mL |
| 10 mM | 0.0405 mL | 0.2027 mL | 0.4054 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。
Magainin 2 and PGLa in bacterial membrane mimics III: Membrane fusion and disruption
We previously speculated that the synergistically enhanced antimicrobial activity of Magainin 2 and PGLa is related to membrane adhesion, fusion, and further membrane remodeling. Here we combined computer simulations with time-resolved in vitro fluorescence microscopy, cryoelectron microscopy, and small-angle X-ray scattering to interrogate such morphological and topological changes of vesicles at nanoscopic and microscopic length scales in real time. Coarse-grained simulations revealed formation of an elongated and bent fusion zone between vesicles in the presence of equimolar peptide mixtures. Vesicle adhesion and fusion were observed to occur within a few seconds by cryoelectron microscopy and corroborated by small-angle X-ray scattering measurements. The latter experiments indicated continued and time-extended structural remodeling for individual peptides or chemically linked peptide heterodimers but with different kinetics. Fluorescence microscopy further captured peptide-dependent adhesion, fusion, and occasional bursting of giant unilamellar vesicles a few seconds after peptide addition. The synergistic interactions between the peptides shorten the time response of vesicles and enhance membrane fusogenic and disruption properties of the equimolar mixture compared with the individual peptides.
Magainin 2 and PGLa in bacterial membrane mimics IV: Membrane curvature and partitioning
We previously reported that the synergistically enhanced antimicrobial activity of magainin 2 (MG2a) and PGLa is related to membrane adhesion and fusion. Here, we demonstrate that equimolar mixtures of MG2a and L18W-PGLa induce positive monolayer curvature stress and sense, at the same time, positive mean and Gaussian bilayer curvatures already at low amounts of bound peptide. The combination of both abilities-membrane curvature sensing and inducing-is most likely the base for the synergistically enhanced peptide activity. In addition, our coarse-grained simulations suggest that fusion stalks are promoted by decreasing the free-energy barrier for their formation rather than by stabilizing their shape. We also interrogated peptide partitioning as a function of lipid and peptide concentration using tryptophan fluorescence spectroscopy and peptide-induced leakage of dyes from lipid vesicles. In agreement with a previous report, we find increased membrane partitioning of L18W-PGLa in the presence of MG2a. However, this effect does not prevail to lipid concentrations higher than 1 mM, above which all peptides associate with the lipid bilayers. This implies that synergistic effects of MG2a and L18W-PGLa in previously reported experiments with lipid concentrations >1 mM are due to peptide-induced membrane remodeling and not their specific membrane partitioning.
A magainin-2 like bacteriocin BpSl14 with anticancer action from fish gut Bacillus safensis SDG14
Bacteriocins are gaining utmost importance in antimicrobial and chemotherapy due to their diverse structure and activity. This study centres on magainin-2 like bacteriocin with anticancer action, produced by Bacillus safensis strain SDG14 isolated from gut of marine fish Sardinella longiceps. The purified bacteriocin designated as BpSl14 was thermostable and pH tolerant. The molecular weight of BpS114 was estimated to be 6061.2 Da using MALDI-ToF MS. The partial primary sequence was elucidated by peptide mass fingerprinting using MALDI MS/MS. The tertiary structure of the partial sequence was similar to that of two magainin-2 α-helices joined together by extended indolicidin. The BpSl14 protein inhibited the cells of lung carcinoma, one of the deadliest cancers. Docking studies conducted with DR5 and TGF-β, two of the most prominent apoptotic receptors in adenocarcinoma, also proved the anti-apoptotic action of BpSl14.
Interaction between Antimicrobial Peptide Magainin 2 and Nonlipid Components in the Bacterial Outer Envelope
Antimicrobial peptides (AMPs) offer advantages over conventional antibiotics; for example, bacteria develop more resistance to small-molecule antibiotics than to AMPs. The interaction of the AMPs with the lipopolysaccharide (LPS) layer of the Gram-negative bacteria cell envelope is not well understood. A MARTINI model was constructed of a Gram-negative bacterial outer membrane interacting with the AMP Magainin 2. In a 20 μs molecular dynamics (MD) simulation, the AMP diffused to the LPS layer of the cell envelope and remained there, suggesting interactions between the Magainin 2 and the LPS layer, causing the AMP to concentrate at that position. The free energy profile for the insertion of the Magainin 2 into the membrane was also calculated using umbrella sampling, which showed that the AMP positioned such that the cationic side chains of the AMP coordinated to the negatively charged phosphate groups of the LPS layer. These simulations indicate that the AMP Magainin 2 partition into the LPS layer of a bacterial membrane.
Anti-Pythium insidiosum activity of MSI-78, LL-37, and magainin-2 antimicrobial peptides
We investigated the anti-Pythium insidiosum activity of the antimicrobial peptides (AMPs) MSI-78, LL-37, and magainin-2. To detect the minimum inhibitory concentration (MIC), fourteen clinical strains were incubated with the AMPs following the CLSI M38-A2 protocol. All three AMPs showed antimicrobial activity with an MIC range of 20-80 mg/L against all strains. We concluded that the evaluated AMPs have great potential as anti-Pythium insidiosum agents, and their activity deserves to be more explored in further research. Antimicrobial peptides were tested against Pythium insidiosum, a microorganism that causes a difficult-to-treat disease in animals and humans. These peptides have been shown to be able to kill P. insidiosum and may be candidates for use in the treatment of this infection.