Bactenecin (Bactenecin, bovine)
(Synonyms: 抗菌肽; Bactenecin, bovine) 目录号 : GC32308
Bactenecin (Bactenecin, bovine) (Bactenecin (Bactenecin, bovine), bovine) 是一种从牛嗜中性粒细胞中分离出来的有效的 12-aa 环状抗菌肽。
Cas No.:116229-36-8
Sample solution is provided at 25 µL, 10mM.
;)
,-1-7$$$37316672.jpg');)
;)
;)
$$$36806353.jpg');)
;33(7)%EF%BC%9A546-561$$$37156877.jpg');)
;)
;)
;)
%201124-1138.$$$35908550.jpg');)
%20766-780.$$$37100057.jpg');)
%20418-432.$$$36893736.jpg');)
%EF%BC%9A-240-255.$$$35108512.jpg');)
533-545$$$36543525.jpg');)
%201-13.$$$36600053.jpg');)
;)
Quality Control & SDS
- View current batch:
- Purity: >98.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
|
Cell experiment: |
Rat neuronal cells (5000 cells/well) are incubated for 24 hr with bactenecin (0.3, 0.6, 1.25, 2.5, 5, 10, 20, 40 μg/mL) or the control peptide. Cytotoxicity is assayed in 96-well tissue culture plates using a commercially available kit. The method is based on cellular reduction of tetrazolium salt into intensely coloured formazan derivates.[2]. |
|
References: [1]. Gallis B, et al. Antimicrobial activity of synthetic bactenecin. Biotechnol Ther. 1989-1990;1(4):335-46. |
|
Bactenecin is a cyclic antimicrobial peptide isolated from bovine neutrophils with potent activity against Bacterial and Fungal species.
Bactenecin inhibits the growth of Escherichia coli and Staphylococcus aureus at the same concentration. Bactenecin inhibits the growth of other medically important bacteria and yeast, and it kills the fungus Trichophyton rubrum. Acetylation and amidation of the amino- and carboxy-termini of bactenecin do not change its potency, while replacement of its two cysteine residues with serine decreases the potency[1]. Bactenecin, a dodecapeptide, is strongly cytotoxic to rat embryonic neurons, fetal rat astrocytes and human glioblastoma cells. This neurotoxicity is unique to bactenecin, as a panel of antibacterial peptides from vertebrates and invertebrates, like defensins corticostatin, indolicidin, cecropin P1, tachyplesin I, the magainins, or apidaecins did not impair neuronal viability[2].
[1]. Gallis B, et al. Antimicrobial activity of synthetic bactenecin. Biotechnol Ther. 1989-1990;1(4):335-46. [2]. Radermacher SW, et al. Bactenecin, a leukocytic antimicrobial peptide, is cytotoxic to neuronal and glial cells. J Neurosci Res. 1993 Dec 15;36(6):657-62.
| Cas No. | 116229-36-8 | SDF | |
| 别名 | 抗菌肽; Bactenecin, bovine | ||
| Canonical SMILES | Arg-Leu-Cys-Arg-Ile-Val-Val-Ile-Arg-Val-Cys-Arg (Disulfide bridge: Cys3-Cys11) | ||
| 分子式 | C63H118N24O13S2 | 分子量 | 1483.89 |
| 溶解度 | Soluble in DMSO | 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。 |
||
| 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 | |||
 |
1 mg | 5 mg | 10 mg |
| 1 mM | 0.6739 mL | 3.3695 mL | 6.739 mL |
| 5 mM | 0.1348 mL | 0.6739 mL | 1.3478 mL |
| 10 mM | 0.0674 mL | 0.337 mL | 0.6739 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。
In vitro and in vivo properties of the bovine antimicrobial peptide, Bactenecin 5
PLoS One 2019 Jan 9;14(1):e0210508.PMID:30625198DOI:10.1371/journal.pone.0210508.
Antimicrobial peptides (AMP), part of the innate immune system, are well studied for their ability to kill pathogenic microorganisms. However, many also possess important immunomodulatory effects, and this area has potential for the development of novel therapies to supplement traditional methods such as the use of antibiotics. Here, we characterise the microbicidal and immunomodulatory potential of the proline-rich bovine AMP, Bactenecin 5 (Bac5). We demonstrate broad antimicrobial activity, including against some mycobacterial species, which are important pathogens of fish, cattle and humans. Bac5 is able to activate macrophage-like THP-1 cells and can synergistically trigger the upregulation of tnf-伪 when co-stimulated with M. marinum. Furthermore, Bac5 sensitises A549 epithelial cells to stimulation with TNF-伪. For the first time, we characterise the activity of Bac5 in vivo, and show it to be a potent chemokine for macrophages in the zebrafish (Danio rerio) embryo model of infection. Bac5 also supports the early recruitment of neutrophils in the presence of M. marinum. In the absence of host adaptive immunity, exogenous injected Bac5 is able to slow, although not prevent, infection of zebrafish with M. marinum.
Structural identification of DnaK binding sites within bovine and sheep Bactenecin Bac7
Protein Pept Lett 2014 Apr;21(4):407-12.PMID:24164259DOI:10.2174/09298665113206660111.
Bacterial resistance against common antibiotics is an increasing health problem. New pharmaceuticals for the treatment of infections caused by resistant pathogens are needed. Small proline-rich antimicrobial peptides (PrAMPs) from insects are known to bind intracellularly to the conventional substrate binding cleft of the E. coli Hsp70 chaperone DnaK. Furthermore, bactenecins from mammals, members of the cathelicidin family, also contain potential DnaK binding sites. Crystal structures of bovine and sheep Bac7 in complex with the DnaK substrate binding domain show that the peptides bind in the forward binding mode with a leucine positioned in the central hydrophobic pocket. In most structures, proline and arginine residues preceding leucine occupy the hydrophobic DnaK binding sites -1 and -2. Within bovine Bac7, four potential DnaK binding sites were identified.
Synthetic analogues of bovine Bactenecin dodecapeptide reduce herpes simplex virus type 2 infectivity in mice
Antiviral Res 2013 Nov;100(2):455-9.PMID:24012999DOI:10.1016/j.antiviral.2013.08.019.
We have evaluated the potential of four synthetic peptides (denoted HH-2, 1002, 1006, 1018) with a distant relationship to the host defense peptide bovine Bactenecin dodecapeptide for their ability to prevent genital infections with herpes simplex virus type 2 (HSV-2) in mice. All four peptides showed antiviral properties in vitro and reduced HSV-2 infection of Vero cells in a dose-dependent manner. Detailed analysis showed that the peptides were able to interfere with both viral attachment and entry, but not with replication post-entry, and were effective antivirals also when HSV-2 was introduced in human semen. Two of the peptides proved especially effective in reducing HSV-2 infection also in vivo. When admixed with virus prior to inoculation, both HH-2 and 1018 reduced viral replication and disease development in a genital model of HSV-2 infection in mice, and also when using very high infectious doses of HSV-2. These data show that peptides HH-2 and 1018 have antiviral properties and can be used to prevent genital herpes infection in mice.
Interaction of the cyclic antimicrobial cationic peptide Bactenecin with the outer and cytoplasmic membrane
J Biol Chem 1999 Jan 1;274(1):29-35.PMID:9867806DOI:10.1074/jbc.274.1.29.
Bactenecin, a 12-amino acid cationic antimicrobial peptide from bovine neutrophils, has two cysteine residues, which form one disulfide bond, making it a cyclic molecule. To study the importance of the disulfide bond, a linear derivative Bac2S was made and the reduced form (linear Bactenecin) was also included in this study. Circular dichroism spectroscopy showed that Bactenecin existed as a type I beta-turn structure regardless of its environment, while the reduced form and linear Bactenecin adopted different conformations according to the lipophilicity of the environment. Bactenecin was more active against the Gram-negative wild type bacteria Escherichia coli, Pseudomonas aeruginosa, and Salmonella typhimurium than its linear derivative and reduced form, while all three peptides were equally active against the outer membrane barrier-defective mutants of the first two bacteria. Only the two linear peptides showed activity against the Gram-positive bacteria Staphylococcus epidermidis and Enterococcus facaelis. Bactenecin interacted well with the outer membrane and its higher affinity for E. coli UB1005 lipopolysaccharide and improved ability to permeabilize the outer membrane seemed to account for its better antimicrobial activity against Gram-negative bacteria. The interaction of Bactenecin with the cytoplasmic membrane was determined by its ability to dissipate the membrane potential by using the fluorescence probe 3, 3-dipropylthiacarbocyanine and an outer membrane barrier-defective mutant E. coli DC2. It was shown that the linear derivative and reduced form were able to dissipate the membrane potential at much lower concentrations than Bactenecin despite the similar minimal inhibitory concentrations of all three against this barrier-defective mutant.
Antimicrobial activity of synthetic Bactenecin
Biotechnol Ther 1989;1(4):335-46.PMID:2562655doi
Bactenecin is an antimicrobial peptide isolated from bovine neutrophils. Bactenecin was synthesized by solid-phase peptide synthesis and renatured to a fully disulfide bonded form. The peptide inhibits the growth of Escherichia coli and Staphylococcus aureus at the same concentration reported for the peptide purified from bovine neutrophils. Bactenecin inhibits the growth of other medically important bacteria and yeast, and it kills the fungus Trichophyton rubrum. Acetylation and amidation of the amino- and carboxy-termini of Bactenecin do not change its potency, while replacement of its two cysteine residues with serine decreases the potency.