Cecropin B
(Synonyms: 天蚕丝抗菌肽) 目录号 : GC32991
An antimicrobial peptide
Cas No.:80451-05-4
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
Animal experiment: | Mice[1]Thirty ICR mice are enrolled in the study, and the Pseudomonas aeruginosa infection model is reproduced by excision of the full layer of dorsal skin with an area of 1 cm x 1 cm. Then they are randomly divided into C (control, n=10, with wet compress of isotonic saline at 3 postinjury hour (PIH)) , M (with hydropathic compress of 100 g/L mafenide at 3 PIH), A (with wet compress of 1 000 mg/L Cecropin B at 3 PIH) groups. The changes in body temperature and hemogram in each group are determined before and 4 days after injury[2]. |
References: [1]. Zhou X et al. Cecropin B Represses CYP3A29 Expression through Activation of the TLR2/4-NF-κB/PXR Signaling Pathway. Sci Rep. 2016 Jun 14 | |
Cecropin B is an antimicrobial peptide.1 It is active against the Gram-positive bacteria S. aureus, B. subtilis, Sporosarcina, and Curtobacterium (MICs = 0.89, 0.98, 0.88, and 0.97 ?M, respectively) and the Gram-negative bacteria E. coli, S. pullorum, and P. aeruginosa (MICs = 0.5, 0.78, and 0.98, respectively). Cecropin B also induces membrane permeabilization in, and is active against the plant pathogenic fungi R. solani (MIC = 9.8 ?M).2
1.Wang, X., Zhu, M., Yang, G., et al.Expression of cecropin B in Pichia pastoris and its bioactivity in vitroExp. Ther. Med.2(4)655-660(2011) 2.Oard, S., Rush, M.C., and Oard, J.H.Characterization of antimicrobial peptides against a US strain of the rice pathogen Rhizoctonia solaniJ. Appl. Microbiol.97(1)169-180(2004)
| Cas No. | 80451-05-4 | SDF | |
| 别名 | 天蚕丝抗菌肽 | ||
| Canonical SMILES | Lys-Trp-Lys-Val-Phe-Lys-Lys-Ile-Glu-Lys-Met-Gly-Arg-Asn-Ile-Arg-Asn-Gly-Ile-Val-Lys-Ala-Gly-Pro-Ala-Ile-Ala-Val-Leu-Gly-Glu-Ala-Lys-Ala-Leu-NH2 | ||
| 分子式 | C176H302N52O41S | 分子量 | 3834.67 |
| 溶解度 | Water : 20 mg/mL (5.22 mM) | 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 | 0.2608 mL | 1.3039 mL | 2.6078 mL |
| 5 mM | 0.0522 mL | 0.2608 mL | 0.5216 mL |
| 10 mM | 0.0261 mL | 0.1304 mL | 0.2608 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。
Cecropin B Represses CYP3A29 Expression through Activation of the TLR2/4-NF-κB/PXR Signaling Pathway
Sci Rep 2016 Jun 14;6:27876.PMID:27296244DOI:10.1038/srep27876.
Cecropins are peptide antibiotics used as drugs and feed additives. Cecropin B can inhibit the expression of CYP3A29, but the underlying mechanisms remain unclear. The present study was designed to determine the mechanisms responsible for the effects of Cecropin B on CYP3A29 expression, focusing on the Toll-like receptors (TLRs) and NF-κB pathways. Our results indicated that the CYP3A29 expression was inhibited by Cecropin B, which was regulated by pregnane X receptor (PXR) in a time- and dose-dependent manner. Cecropin B-induced NF-κB activation played a pivotal role in the suppression of CYP3A29 through disrupting the association of the PXR/retinoid X receptor alpha (RXR-α) complex with DNA sequences. NF-κB p65 directly interacted with the DNA-binding domain of PXR, suppressed its expression, and inhibited its transactivation, leading to the downregulation of the PXR-regulated CYP3A29 expression. Furthermore, Cecropin B activated pig liver cells by interacting with TLRs 2 and 4, which modulated NF-κB-mediated signaling pathways. In conclusion, Cecropin B inhibited the expression of CYP3A29 in a TLR/NF-κB/PXR-dependent manner, which should be considered in future development of cecropins and other antimicrobial peptides.
Hyaluronan-cecropin B interactions studied by ultrasound velocimetry and isothermal titration calorimetry
Int J Biol Macromol 2023 Feb 1;227:786-794.PMID:36549616DOI:10.1016/j.ijbiomac.2022.12.144.
Interactions between hyaluronan and the antimicrobial peptide Cecropin B were studied in water and PBS using high-resolution ultrasonic spectroscopy and isothermal titration calorimetry. Although each technique is fundamentally different, they both gave identical results. It was found that the molecular weight of hyaluronan plays an important role in the interactions - in particular, the transition between the rod conformation and the random coil conformation. In water, interactions were saturated in a molar charge ratio of 1.5 and not 1.0 as expected. The later saturation of the interaction probably occurred either for steric reasons or due to the interaction between functional groups in the cecropin structure, which allowed complete dissociation of the antimicrobial peptide. In PBS, in contrast to water, no interactions were observed, irrespective of the molecular weight of hyaluronan. Thus, at a sufficiently high ionic strength, the interactions were suppressed.
Label-free liquid crystal biosensor for Cecropin B detection
Talanta 2018 Aug 15;186:60-64.PMID:29784409DOI:10.1016/j.talanta.2018.04.004.
A label-free liquid crystal (LC) biosensor based on orientation changes of LC molecules was reported for the detection of Cecropin B. The homeotropic-to-tilted alignment transition of LC molecules, induced by the specific binding event between Cecropin B and anti-cecropin B antibody immobilized via glutaraldehyde, could result in obvious change of the optical appearance from a dark to a bright response and as a result, the detection limit of Cecropin B was as low as 50 ng/mL. The average gray-scale intensities (GIs) of optical appearances were calculated to quantitatively analyse Cecropin B concentrations. This study offers a simple, highly sensitive and specific, lable-free method for Cecropin B detection.
A novel cecropin B-derived peptide with antibacterial and potential anti-inflammatory properties
PeerJ 2018 Jul 25;6:e5369.PMID:30065898DOI:10.7717/peerj.5369.
Cecropins, originally found in insects, are a group of cationic antimicrobial peptides. Most cecropins have an amphipathic N-terminal segment and a largely hydrophobic C-terminal segment, and normally form a helix-hinge-helix structure. In this study, we developed the novel 32-residue cecropin-like peptide cecropin DH by deleting the hinge region (Alanine-Glycine-Proline) of Cecropin B isolated from Chinese oak silk moth, Antheraea pernyi. Cecropin DH possesses effective antibacterial activity, particularly against Gram-negative bacteria, with very low cytotoxicity against mammalian cells. Interactions between cecropin DH and the highly anionic lipopolysaccharide (LPS) component of the Gram-negative bacterial outer membrane indicate that it is capable of dissociating LPS micelles and disrupting LPS aggregates into smaller assemblies, which may play a vital role in its antimicrobial activity. Using LPS-stimulated mouse macrophage RAW264.7 cells, we found that cecropin DH exerted higher potential anti-inflammatory activity than Cecropin B, as demonstrated by the inhibition of pro-inflammatory cytokines nitric oxide production and secretion of tumor necrosis factor-α. In conclusion, cecropin DH has potential as a therapeutic agent for both antibacterial and anti-inflammatory applications.
Expression of Antimicrobial Peptide (AMP), Cecropin B, in a Fused Form to SUMO Tag With or Without Three-Glycine Linker in Escherichia coli and Evaluation of Bacteriolytic Activity of the Purified AMP
Probiotics Antimicrob Proteins 2021 Dec;13(6):1780-1789.PMID:34018140DOI:10.1007/s12602-021-09797-1.
Current antibiotics have limited action mode, which makes it difficult for the antibiotics dealing with the emergence of bacteria resisting the existing antibiotics. As a need for new bacteriolytic agents alternative to the antibiotics, AMPs have long been considered substitutes for the antibiotics. Cecropin B was expressed in a fusion form to six-histidine and SUMO tags in Escherichia coli. Six-histidine tag attached to SUMO was for purification of SUMO-cecropin B fusion proteins and removal of the SUMO tag from Cecropin B. Chimeric gene was constructed into pKSEC1 vector that was designed to be functional in both Escherichia coli and chloroplast. To maximize translation of the fusion protein, sequences were codon-optimized. Four different constructs were tested for the level of expression and solubility, and the construct with a linker, 6xHisSUMO3xGly-cecropin B, showed the highest expression. In addition, cleavage of the SUMO tag by SUMOase in the three fusion constructs which have no linker sequence (3xGly, three glycines) was not as efficient as the construct with the linker between SUMO and Cecropin B. The cleaved Cecropin B showed bacteriolytic activity against Bacillus subtilis at a concentration of 0.0625 μg/μL, while Cecropin B fused to SUMO had no activity at a higher concentration, 0.125 μg/μL. As an expression system for AMPs in prokaryotic hosts, the use of tag proteins and appropriate codon-optimization strategy can be employed and further genetic modification of the fusion construct should help the complete removal of the tag proteins from the AMP in the final step of purification.