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Indolicidin Sale

目录号 : GC32207

An antimicrobial peptide

Indolicidin Chemical Structure

Cas No.:140896-21-5

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500μg
¥1,428.00
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1mg
¥2,321.00
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5mg
¥6,962.00
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Sample solution is provided at 25 µL, 10mM.

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实验参考方法

Cell experiment:

The time course and dose dependence of indolicidin bactericidal activity are determined using Escherichia coli ML35 and Staphylococcus aureus 502A as test organisms. The assays are performed in 10 mM sodium phosphate buffer, pH 7.4, at 37°C. A 50 μg sample of indolicidin is dissolved in 50 pl of 0.1 M pyridine acetate, pH 6.5, and incubated with 5 μg of chymotrypsin for 15 h at 37°C. Digestion of the sample is confirmed by the disappearance of the indolicidin band on acid-urea PAGE. Following lyophilization, untreated and digested samples are tested for antibacterial activity in a agar diffusion assay against Escherichia coli using concentrations of peptide ranging from 10 to 300 μg/mL[1].

References:

[1]. Selsted ME, et al. Indolicidin, a novel bactericidal tridecapeptide amide from neutrophils. J Biol Chem. 1992 Mar 5;267(7):4292-5.
[2]. Falla TJ, et al. Mode of action of the antimicrobial peptide indolicidin. J Biol Chem. 1996 Aug 9;271(32):19298-303.

产品描述

Indolicidin is an antimicrobial peptide.1 It is active against multidrug-resistant isolates of enteroaggregative E. coli (MDR-EAEC; MICs = 32 ?M for all). Indolicidin is also active against S. cerevisiae, T. beigelii, and C. albicans (MICs = 5-10, 2.5-5, and 5-10 ?M, respectively) and reduces viral replication of HIV-1 in MT-2 cells when used at concentrations ranging from 67 to 100 ?g/ml.2,3 In vivo, indolicidin increases survival of MDR-EAEC-infected G. mellonella larvae.1

1.Vergis, J., Malik, S.S., Pathak, R., et al.Antimicrobial efficacy of indolicidin against multi-drug resistant enteroaggregative Escherichia coli in a Galleria mellonella modelFront. Microbiol.102723(2019) 2.Lee, D.G., Kim, H.K., Kim, S.A., et al.Fungicidal effect of indolicidin and its interaction with phospholipid membranesBiochem. Biophys. Res. Commun.305(2)305-310(2003) 3.Robinson, W.E., Jr., McDougall, B., Tran, D., et al.Anti-HIV-1 activity of indolicidin, an antimicrobial peptide from neutrophilsJ. Leukoc. Biol.63(1)94-100(1998)

Chemical Properties

Cas No. 140896-21-5 SDF
Canonical SMILES Ile-Leu-Pro-Trp-Lys-Trp-Pro-Trp-Trp-Pro-Trp-Arg-Arg-NH2
分子式 C100H132N26O13 分子量 1906.28
溶解度 Soluble in DMSO 储存条件 -20°C, protect from light
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1 mM 0.5246 mL 2.6229 mL 5.2458 mL
5 mM 0.1049 mL 0.5246 mL 1.0492 mL
10 mM 0.0525 mL 0.2623 mL 0.5246 mL
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Research Update

Indolicidin revisited: biological activity, potential applications and perspectives of an antimicrobial peptide not yet fully explored

World J Microbiol Biotechnol 2022 Jan 12;38(3):39.PMID:35018535DOI:10.1007/s11274-022-03227-2.

The emergence of multidrug-resistant bacteria, viruses and tumors is a serious threat to public health. Among natural peptides, Indolicidin, a 13-residue peptide belonging to the cathelicidin family, deserves special attention. Indolicidin has a broad spectrum of biological activity and is active against a wide range of targets, such as bacteria (Gram+ and Gram-), fungi and viruses. Here, we review the most important features of the biological activity, potential applications and perspectives of Indolicidin and its analogs. Although not yet approved for commercialization, this peptide has great potential to be applied in different areas, including the medical, biomedical, food industry and other unexplored areas. To achieve this goal, a multidisciplinary team of researchers must work together to fine tune peptides that overall lead to novel analogs and formulations to combat existing and possibly future diseases.

Indolicidin analogs with broad-spectrum antimicrobial activity and low hemolytic activity

Peptides 2020 Oct;132:170356.PMID:32593681DOI:10.1016/j.peptides.2020.170356.

To create a broad-spectrum peptide biocide, we synthesized 45 analogs of antimicrobial peptide Indolicidin (H-Ile-Leu-Pro-Trp-Lys-Trp-Pro-Trp-Trp-Pro-Trp-Arg-Arg-NH2). Among them the peptides H-Ile-Leu-Pro-(2-Me)Phe-Lys-(2-Me)Phe-Pro-(2-Me)Phe-(2-Me)Phe-Pro-(2-Me)Phe-Arg-Arg-NH2 and HN2-(CH2)10-Ile-Leu-Pro-D-Phe-Lys-D-Phe-Pro-D-Phe-D-Phe-Pro-D-Phe-Arg-Arg-NH2 have the broadest spectrum of antimicrobial activity and the lowest hemolytic activity. They are active against all 11 tested strains of Gram-positive bacteria, Gram-negative bacteria and fungi with MIC50 from 0.9 to 6.1 渭g/ml (0.5 to 3.2 渭M), being up to 3 times more active than Indolicidin, and are at least 1.8 times less hemolytically active than Indolicidin (reached the detection limit). These peptides are patented and could be used for further drug development as antimicrobials.

Influence of the Polysaccharide Capsule on the Bactericidal Activity of Indolicidin on S treptococcus pneumoniae

Front Microbiol 2022 May 13;13:898815.PMID:35633685DOI:10.3389/fmicb.2022.898815.

Streptococcus pneumoniae is a pathogen responsible for high morbidity and mortality worldwide. The polysaccharide capsule confers protection against phagocytosis and influences many aspects of pneumococcal pathogenesis. The capsular polysaccharides (CPS) are highly immunogenic and exhibit great structural variability, with more than 100 serotypes described so far. Antimicrobial peptides (AMPs) are an important part of the innate defense mechanisms against many pathogens. Indolicidin is a cationic AMP produced by bovine neutrophils, with bactericidal effects against several bacteria. CPS has been shown to interfere with the ability of AMPs to kill pneumococci, but the effects of capsule variability on susceptibility to Indolicidin have not been explored. The present work determined the effects of capsule on resistance to Indolicidin in vitro. Using a bactericidal plate assay, we observed that different pneumococcal serotypes exhibited variable resistance to Indolicidin, which correlated with the capsule net charge. Interestingly, the effect of capsule expression on resistance to Indolicidin was dependent on the serotype; bacteria with lower zeta potential were more resistant to Indolicidin when capsule was present, while those with less negative surface charge were more resistant in the absence of capsule. The addition of purified CPS partially rescued the bacteria from the bactericidal effects of Indolicidin, while the addition of anticapsular antibodies accentuated the peptide's bactericidal action, suggesting a possible new protective mechanism induced by polysaccharide-based pneumococcal vaccines.

Correction of Acute Parodontitis with Indolicidin Analogues

Bull Exp Biol Med 2019 May;167(1):47-49.PMID:31177448DOI:10.1007/s10517-019-04457-5.

We studied the influence of synthetic Indolicidin analogues on the development of acute periodontitis. The corrective effect was found in Indolicidin analogues Nos. 7 and 8; it manifested in a decrease in the edema of gingival epithelium and lamina propria, a decrease in the relative area of inflammatory infiltrates, and a significant increase in the relative area of normal connective tissue. These changes were revealed as soon as on day 14 and were most pronounced in 21 days after the removal of the ligature. Indolicidin analogues Nos. 7 and 8 demonstrated similar effectiveness on the model of acute periodontitis.

Indolicidin action on membrane permeability: carrier mechanism versus pore formation

Biochim Biophys Acta 2011 Jan;1808(1):91-7.PMID:20851098DOI:10.1016/j.bbamem.2010.09.005.

Indolicidin, a 13-residue cationic peptide with extremely high tryptophan content, exhibits broad-spectrum antimicrobial as well as hemolytic activity. To gain insight into the mechanism of Indolicidin action on membrane permeability, liposome leakage induced by this peptide was studied by using various probes with vesicles of different lipid compositions. In liposomes containing negatively charged lipids, Indolicidin induced rather unselective permeabilization. By contrast, the peptide appeared to be selective in provoking leakage of neutral, egg phosphatidylcholine (PC) liposomes: it effectively induced the release of negatively charged fluorescent dyes, carboxyfluorescein (CF), calcein and sulforhodamine B, but was unable to induce the leakage of a neutral compound, glucose, and that of positively charged doxorubicin. Moreover, organic anions, such as fatty acids, were found to suppress the indolicidin-induced CF leakage of egg PC liposomes. Based on these results, we concluded that Indolicidin facilitates the dye release from uncharged lipid vesicles not by formation of membrane pores as it is generally accepted for the majority of antimicrobial peptides but rather via translocation of dye molecules across the membrane in the form of dye-peptide complexes, i.e. Indolicidin operates as an organic anion carrier. This conclusion was supported by observing the formation of complexes between Indolicidin and pyrenebutyrate in solution. The Indolicidin analog having only one arginine was ineffective in pyrenebutyrate binding and CF transport. The mode of action proposed here for Indolicidin can be related to that previously postulated for oligoarginine derivatives which are able to carry organic anions across liposomal and bulk phase membranes [Sakai N. & Matile S. J. Am. Chem. Soc. 2003, 125:14348-14356]. The newly identified mechanism of peptide ionophoric activity in uncharged lipid membranes may be involved in hemolytic action of Indolicidin via induction of plasma membrane permeability for important anionic metabolites which disturbs regulation of osmotic balance ultimately leading to erythrocyte membrane rupture.