Alamethicin F50
(Synonyms: 丙甲菌素F50) 目录号 : GC42763
A peptaibol antibiotic
Cas No.:56165-93-6
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
- View current batch:
- Purity: >98.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
Alamethicin F50 is a peptaibol isolated from Trichoderma. It is a polymer of 20 amino acids that includes modified and non-proteinogenic amino acids. Alamethicin F50 is a mixture of 13 different peptides, with the most abundant designated as alamethicin F50/5. Alamethicin F50 forms voltage-dependent ion channels in lipid membranes and acts as a lytic agent. It induces lysis of leukocytes (IC50 = 54 and 80 μM for rat mast cells and mouse spleen lymphocytes, respectively) and exhibits antibacterial activity against a panel of 8 mollicutes (MICs = 1.56-12.5 μM).
| Cas No. | 56165-93-6 | SDF | |
| 别名 | 丙甲菌素F50 | ||
| 分子式 | C92H151N23O24 | 分子量 | 1963.3 |
| 溶解度 | DMF: Soluble,DMSO: Soluble,Ethanol: Soluble,Methanol: Soluble | 储存条件 | Store at -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 | 0.5093 mL | 2.5467 mL | 5.0935 mL |
| 5 mM | 0.1019 mL | 0.5093 mL | 1.0187 mL |
| 10 mM | 0.0509 mL | 0.2547 mL | 0.5093 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。
Enhancing the Antimicrobial Activity of Alamethicin F50/5 by Incorporating N-terminal Hydrophobic Triazole Substituents
Chemistry 2017 Dec 19;23(71):17964-17972.PMID:28922505DOI:10.1002/chem.201703569.
A simple and efficient strategy is proposed to significantly improve the antibacterial activity of peptaibols and other antimicrobial peptides by N-terminal capping with 1,2,3-triazole bearing various hydrophobic substituents on C-4. Such N-terminal insertions on Alamethicin F50/5 could enhance its antimicrobial activity on Gram-positive bacteria without modification of its overall three-dimensional structure. Although the native peptide and its analogues shared comparable helical contents, the crystal structure of one of the most active derivative showed a local slight distortion of the N-terminal extremity, which was also observed in solution using NMR spectroscopy. Importantly, fluorescence studies showed that the N-capped derivatives had increased affinity for liposomes, which may indicate they interacted more strongly with the bacterial membrane than Alamethicin F50/5.
Conformational analysis of TOAC-labelled Alamethicin F50/5 analogues
Chem Biodivers 2007 Jun;4(6):1256-68.PMID:17589864DOI:10.1002/cbdv.200790108.
In the preceding paper in this issue, we reported the total syntheses in solution of a set of four TOAC-containing analogues of the [L-Glu(OMe)(7,18,19)] F50/5 component of alamethicin, the prototype of peptaibol antibiotics forming channels in the biological membranes. In this article, we have expanded this work to the examination of their preferred conformation in solution by use of a combination of CD, FT-IR absorption, and NMR spectroscopies. The results are strongly in favor of the view that replacement of the Aib residues at positions 1, 8, and 16 with TOAC (both are members of the helicogenic sub-class of C(alpha)-tetrasubstituted alpha-amino acids) does not significantly affect the overwhelmingly populated alpha-helical 3D structure of alamethicin. The X-ray diffraction crystal structure of the N(alpha)-protected, C-terminal, hexapeptide amide segment Z-L-Pro-L-Val-(Aib)(2)-[L-Glu(OMe)](2)-Fol lends further support to our conformational conclusions.
Total synthesis in solution of Alamethicin F50/5 by an easily tunable segment condensation approach
Biopolymers 2004;76(6):485-93.PMID:15499566DOI:10.1002/bip.20161.
A total synthesis in solution of the 19-mer peptide component F50/5 of alamethicin, the most extensively investigated among the channel-former peptaibol antibiotics, is reported. Three peptide segments (A, B, C) were prepared and assembled, followed by incorporation of the acetylated N-terminal amino acid. The synthetic modules B and C are characterized by three Glu(OMe) residues (at positions 7, 18, and 19) that, after completion of the synthesis, were reacted with ammonia to provide Alamethicin F50/5. By use of this general strategy, we also prepared the [Gln7, Glu(OMe)18,19] Alamethicin F50/5 analogue. The purity and conformation of the final products were assessed by chromatographic, spectrometric, and spectroscopic techniques. This tunable segment condensation approach will pave the way for an easy synthesis of alamethicin analogues bearing amino acid residues with desired side-chain probes even at the N-terminus and in internal positions of the sequence.
Pore-forming properties of Alamethicin F50/5 inserted in a biological membrane
Chem Biodivers 2007 Jun;4(6):1338-46.PMID:17589885DOI:10.1002/cbdv.200790114.
The pore-forming properties of native and synthetic alamethicins were investigated in photoreceptor rod outer segments (OS) isolated from frog retina, and recorded in whole-cell configuration. The peptaibols were applied (and removed) to (from) the OS within less than 50 ms by means of a computer-controlled micro-perfusion system. Once blocked with light, the main OS endogenous conductance, the OS membrane resistance was >1 GOmega, allowing low-noise and high-resolution recordings. Currents of ca. 700 pA were recorded in symmetric K(+) (100 mM) and Ca(2+) (1 mM), upon applying 1 microM of Alamethicin F50/5 or its [L-Glu(OMe)(7,18,19)] analogue to the OS membrane (clamped at -20 mV). In the latter peptide, the Gln residues at positions 7, 18, and 19 were substituted with side-chain esterified Glu residues. For both peptides, the current activated exponentially, with a delay from peptide application, and exponentially returned to zero without any delay, upon removing the peptide from the external solution. The delay as well as the activation (tau(a)) and deactivation (tau(d)) time constants of the current produced by the modified alamethicin were much slower, and the current noise was much larger, with respect to the corresponding values for Alamethicin F50/5. Therefore, the above three Gln residues are not a key factor for pore formation, but the [L-Glu(OMe)(7,18,19)] analogue produces larger pores with a lower probability of formation.
Solution synthesis, conformational analysis, and antimicrobial activity of three Alamethicin F50/5 analogs bearing a trifluoroacetyl label
Chem Biodivers 2014 Aug;11(8):1163-91.PMID:25146762DOI:10.1002/cbdv.201300394.
We prepared, by solution-phase methods, and fully characterized three analogs of the membrane-active peptaibiotic Alamethicin F50/5, bearing a single trifluoroacetyl (Tfa) label at the N-terminus, at position 9 (central region) or at position 19 (C-terminus), and with the three Gln at positions 7, 18, and 19 replaced by Glu(OMe) residues. To add the Tfa label at position 9 or 19, a γ-trifluoroacetylated α,γ-diaminobutyric acid (Dab) residue was incorporated as a replacement for the original Val(9) or Glu(OMe)(19) amino acid. We performed a detailed conformational analysis of the three analogs (using FT-IR absorption, CD, 2D-NMR, and X-ray diffraction), which clearly showed that Tfa labeling does not introduce any dramatic backbone modification in the predominantly α-helical structure of the parent peptaibiotic. The results of an initial solid-state (19)F-NMR study on one of the analogs favor the conclusion that the Tfa group is a very promising reporter for the analysis of peptaibioticmembrane interactions. Finally, we found that the antimicrobial activities of the three newly synthesized analogs depend on the position of the Tfa label in the peptide sequence.