Apidaecin IB
目录号 : GC32315
ApidaecinIB是一种昆虫抗菌肽，抑制大肠杆菌(E.coliML35,O18K1H7andATCC25922)三种菌株的最小浓度均为8μM。
Cas No.:123276-94-8
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
Apidaecin IB is a insect antimicrobial peptide, with minimum inhibitory concentration (MIC) values of 8 μM for E. coli (ML35, O18K1H7 and ATCC 25922).
Apidaecin IB is an insect antimicrobial peptide, with minimum inhibitory concentration (MIC) values of 8 μM for E. coli (ML35, O18K1H7 and ATCC 25922), 64 μM for K. pneumoniae 22, 8-16 μM for S. enteritidis (D5, PD1) and 4-8 μM for S. typhimurium ATCC 14028[1].
[1]. Gobbo M, et al. Substitution of the arginine/leucine residues in apidaecin Ib with peptoid residues: effect on antimicrobial activity, cellular uptake, and proteolytic degradation. J Med Chem. 2009 Aug 27;52(16):5197-206.
| Cas No. | 123276-94-8 | SDF | |
| Canonical SMILES | Gly-Asn-Asn-Arg-Pro-Val-Tyr-Ile-Pro-Gln-Pro-Arg-Pro-Pro-His-Pro-Arg-Leu | ||
| 分子式 | C95H150N32O23 | 分子量 | 2108.41 |
| 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 | 0.4743 mL | 2.3715 mL | 4.7429 mL |
| 5 mM | 0.0949 mL | 0.4743 mL | 0.9486 mL |
| 10 mM | 0.0474 mL | 0.2371 mL | 0.4743 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。
Substitution of the arginine/leucine residues in Apidaecin IB with peptoid residues: effect on antimicrobial activity, cellular uptake, and proteolytic degradation
J Med Chem 2009 Aug 27;52(16):5197-206.PMID:20560644DOI:10.1021/jm900396a.
Several aspects of the mechanism of action of Pro-rich antimicrobial peptides, together with their low toxicity in mammalian cells, make them good candidates for the development of new antibiotic agents. We investigated the effect induced in the insect antimicrobial peptide Apidaecin IB by the replacement of a single arginine/leucine residue with a N-substituted glycine. The resulting peptoid-peptide hybrids are more resistant to proteolysis and devoid of any significant cytotoxic activity, but moving the [NArg]residue from the N- to the C-terminal end of the molecule progressively reduces the antibacterial activity. Cell uptake experiments in E. coli cells suggest that the loss of antibacterial activity of [NArg(17)]apidaecin is a consequence of its inability to translocate into bacterial cells. Conversely, apidaecin and its peptoid-peptide hybrids are able to cross the plasma membrane in eukaryotic cells and to diffuse in the cytosol, although their translocating ability is far less effective than that of other known cell permeant peptides.
Porphyrin-apidaecin conjugate as a new broad spectrum antibacterial agent
ACS Med Chem Lett 2010 Feb 1;1(1):35-8.PMID:24900172DOI:10.1021/ml900021y.
The conjugation of the cationic antimicrobial peptide, Apidaecin IB, to the anionic photosensitizer, 5(4'-carboxyphenyl)-10,15,20-triphenylporphyrin (cTPP), afforded a new antibacterial agent effective, under light activation, against both Gram-positive and Gram-negative bacteria. At low concentrations (1.5-15 渭M) the conjugate was able to reduce the survival of Escherichia coli cells by 3-4 log10, and most notably, it resulted photoactive also against hard-to-treat Pseudomonas aeruginosa, although at higher concentration (60 渭M). Under similar conditions, the photosensitizer alone was only photoactive against Staphylococcus aureus while the unconjugated peptide was inactive against all the bacterial strains tested. This study shows the possibility of obtaining new broad-spectrum apidaecin-photosensitizer conjugates with potent antibacterial activity.
iTRAQ-coupled 2-D LC-MS/MS analysis of cytoplasmic protein profile in Escherichia coli incubated with Apidaecin IB
J Proteomics 2011 Dec 21;75(2):511-6.PMID:21889622DOI:10.1016/j.jprot.2011.08.015.
Apidaecins refer to a series of proline-rich, 18- to 20-residue antimicrobial peptides produced by insects. Accumulating evidence that proline-rich antimicrobial peptides are not-toxic to human and animal cells makes them potential candidates for the development of novel antibiotic drugs. However, the mechanism of action was not fully understood. In this study, antibacterial mechanism of apidaecins was investigated. iTRAQ-coupled 2-D LC-MS/MS technique was utilized to identify altered cytoplasmic proteins of Escherichia coli incubated with one isoform of apidaecins--apidaecin IB. The production of the chaperonin GroEL and its cofactor GroES, which together form the only essential chaperone system in E. coli cytoplasm under all growth conditions, was decreased in cells incubated with Apidaecin IB. The decreasing of the GroEL-GroES chaperone team was further found to be involved in a new antibacterial mechanism of apidaecins. Our findings therefore provide important new insights into the antibacterial mechanism of apidaecins and perhaps, by extension, for other proline-rich antimicrobial peptides.
iTRAQ-coupled 2-D LC-MS/MS analysis of membrane protein profile in Escherichia coli incubated with Apidaecin IB
PLoS One 2011;6(6):e20442.PMID:21673808DOI:10.1371/journal.pone.0020442.
Apidaecins are a series of proline-rich, 18- to 20-residue antimicrobial peptides produced by insects. They are predominantly active against the gram-negative bacteria. Previous studies mainly focused on the identification of their internal macromolecular targets, few addressed on the action of apidaecins on the molecules, especially proteins, of bacterial cell membrane. In this study, iTRAQ-coupled 2-D LC-MS/MS technique was utilized to identify altered membrane proteins of Escherichia coli cells incubated with one isoform of apidaecins--apidaecin IB. Cell division protease ftsH, an essential regulator in maintenance of membrane lipid homeostasis, was found to be overproduced in cells incubated with Apidaecin IB. Its over-expression intensified the degradation of cytoplasmic protein UDP-3-O-acyl-N- acetylglucosamine deacetylase, which catalyzes the first committed step in the biosynthesis of the lipid A moiety of LPS, and thus leaded to the further unbalanced biosynthesis of LPS and phospholipids. Our findings suggested a new antibacterial mechanism of apidaecins and perhaps, by extension, for other proline-rich antimicrobial peptides.
Antimicrobial peptides: synthesis and antibacterial activity of linear and cyclic drosocin and apidaecin 1b analogues
J Med Chem 2002 Sep 26;45(20):4494-504.PMID:12238928DOI:10.1021/jm020861d.
Drosocin and Apidaecin IB are two insect antimicrobial peptides showing a significant sequence homology and a common mechanism of action, which includes stereoselective elements but is devoid of any pore-forming activity. A substantial difference between the two peptides is the presence in the drosocin sequence of an O-glycosylated threonine residue, which is important for its antimicrobial activity. Through the synthesis of a series of differently glycosylated drosocin analogues, we have shown that the antimicrobial activity against several Gram-negative bacteria appears to be modulated by the sugar moiety (Gal vs GalNAc) and the type of glycosidic linkage (alpha-O-, beta-O-, or alpha-C-). The insertion of a glycosylated threonine residue in the Apidaecin IB sequence improves the sequence homology with drosocin but reduces the antimicrobial activity. To gain information on the possible bioactive conformation of these peptides, we synthesized an unglycosylated cyclic analogue of drosocin, containing an intrachain disulfide bond, and the head-to-tail cyclic analogues of drosocin and apidaecin, as well as their corresponding cyclic dimers. Only the large cyclic dimer of apidaecin partially retained the antimicrobial activity, suggesting that a bending of the peptide chain, in particular in the middle of the molecule, is not a structural element characteristic of the bioactive conformation of drosocin and apidaecin. Experiments aimed at testing the effect of selected drosocin and apidaecin peptides on biological membranes showed that some peptides display a moderate hemolytic activity and that a dissociation between antibacterial activity and cytotoxicity to eukaryotic cells can be achieved in differently glycosylated peptide analogues.