Feglymycin
目录号 : GC43659A peptide with antibacterial and antiviral activities
Cas No.:209335-49-9
Sample solution is provided at 25 µL, 10mM.
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- Purity: >95.00%
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Feglymycin is a 13-amino acid peptide originally isolated from Streptomyces that has antibacterial and antiviral activities. It is active against Gram-positive bacteria (MICs = 32-64 µg/ml) and inhibits HIV viral replication in H9 cells (IC50 = ~5 µM). Feglymycin is also active against clinical isolates of HIV-1 from clades A-D, A/E, and G (EC50s = 0.5-6.7 µM). It interacts with gp120 and inhibits HIV-1 NL4.3 binding to human soluble CD4 (EC50 = 4.4 µM) and to CD4+ SupT1 T cells by 74.5% when used at a concentration of 10.5 µM. Feglymycin inhibits the E. coli peptidoglycan biosynthesis enzymes MurA and MurC (Kis = 3.4 and 0.3 µM, respectively) in a noncompetitive manner.
Cas No. | 209335-49-9 | SDF | |
分子式 | C95H97N13O30 | 分子量 | 1900.9 |
溶解度 | DMF: soluble,DMSO: soluble,Ethanol: soluble,Methanol: soluble | 储存条件 | Store at -20°C |
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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。 |
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1 mg | 5 mg | 10 mg | |
1 mM | 0.5261 mL | 2.6303 mL | 5.2607 mL |
5 mM | 0.1052 mL | 0.5261 mL | 1.0521 mL |
10 mM | 0.0526 mL | 0.263 mL | 0.5261 mL |
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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。
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Feglymycin, a unique natural bacterial antibiotic peptide, inhibits HIV entry by targeting the viral envelope protein gp120
Virology 2012 Nov 25;433(2):308-19.PMID:22959895DOI:10.1016/j.virol.2012.08.007.
Feglymycin (FGM), a natural Streptomyces-derived 13mer peptide, consistently inhibits HIV replication in the lower μM range. FGM also inhibits HIV cell-to-cell transfer between HIV-infected T cells and uninfected CD4(+) T cells and the DC-SIGN-mediated viral transfer to CD4(+) T cells. FGM potently interacts with gp120 (X4 and R5) as determined by SPR analysis and shown to act as a gp120/CD4 binding inhibitor. Alanine-scan analysis showed an important role for l-aspartic acid at position 13 for its anti-HIV activity. In vitro generated FGM-resistant HIV-1 IIIB virus (HIV-1 IIIB(FGMres)) showed two unique mutations in gp120 at positions I153L and K457I. HIV-1 IIIB(FGMres) virus was equally susceptible to other viral binding/adsorption inhibitors with the exception of dextran sulfate (9-fold resistance) and cyclotriazadisulfonamide (>15-fold), two well-described compounds that interfere with HIV entry. In conclusion, FGM is a unique prototype lead peptide with potential for further development of more potent anti-HIV derivatives.
Feglymycin, a novel inhibitor of the replication of the human immunodeficiency virus. Fermentation, isolation and structure elucidation
J Antibiot (Tokyo) 1999 Apr;52(4):374-82.PMID:10395273DOI:10.7164/antibiotics.52.374.
The novel peptide Feglymycin has been isolated from cultures of Streptomyces sp. DSM 11171 by solid phase extraction, size exclusion chromatography and repeated reversed-phase chromatography. The molecular weight was found to be 1900.90 g/mol and the molecular formula is C95H97Nl3O30. Feglymycin contains 13 amino acids of which four are 3-hydroxyphenylglycine and five are 3,5-dihydroxyphenylglycine residues. The structure of the linear peptide has been determined by 1H and 13C NMR spectroscopy. The sequence was confirmed by the observed mass spectroscopic fragmentation pattern. As well as having weak antibacterial activity, Feglymycin inhibits the replication of the human immunodeficiency virus (HIV) in vitro.
Biosynthesis of the Peptide Antibiotic Feglymycin by a Linear Nonribosomal Peptide Synthetase Mechanism
Chembiochem 2015 Dec;16(18):2610-4.PMID:26515424DOI:10.1002/cbic.201500432.
Feglymycin, a peptide antibiotic produced by Streptomyces sp. DSM 11171, consists mostly of nonproteinogenic phenylglycine-type amino acids. It possesses antibacterial activity against methicillin-resistant Staphylococcus aureus strains and antiviral activity against HIV. Inhibition of the early steps of bacterial peptidoglycan synthesis indicated a mode of action different from those of other peptide antibiotics. Here we describe the identification and assignment of the Feglymycin (feg) biosynthesis gene cluster, which codes for a 13-module nonribosomal peptide synthetase (NRPS) system. Inactivation of an NRPS gene and supplementation of a hydroxymandelate oxidase mutant with the amino acid l-Hpg proved the identity of the feg cluster. Feeding of Hpg-related unnatural amino acids was not successful. This characterization of the feg cluster is an important step to understanding the biosynthesis of this potent antibacterial peptide.
Total synthesis of Feglymycin based on a linear/convergent hybrid approach using micro-flow amide bond formation
Nat Commun 2016 Nov 28;7:13491.PMID:27892469DOI:10.1038/ncomms13491.
Feglymycin is a naturally occurring, anti-HIV and antimicrobial 13-mer peptide that includes highly racemizable 3,5-dihydroxyphenylglycines (Dpgs). Here we describe the total synthesis of Feglymycin based on a linear/convergent hybrid approach. Our originally developed micro-flow amide bond formation enabled highly racemizable peptide chain elongation based on a linear approach that was previously considered impossible. Our developed approach will enable the practical preparation of biologically active oligopeptides that contain highly racemizable amino acids, which are attractive drug candidates.
Alanine scan of the peptide antibiotic Feglymycin: assessment of amino acid side chains contributing to antimicrobial activity
Chembiochem 2013 Mar 18;14(5):625-32.PMID:23447362DOI:10.1002/cbic.201300032.
The antibiotic Feglymycin is a linear 13-mer peptide synthesized by the bacterium Streptomyces sp. DSM 11171. It mainly consists of the nonproteinogenic amino acids 4-hydroxyphenylglycine and 3,5-dihydroxyphenylglycine. An alanine scan of Feglymycin was performed by solution-phase peptide synthesis in order to assess the significance of individual amino acid side chains for biological activity. Hence, 13 peptides were synthesized from di- and tripeptide building blocks, and subsequently tested for antibacterial activity against Staphylococcus aureus strains. Furthermore we tested the inhibition of peptidoglycan biosynthesis enzymes MurA and MurC, which are inhibited by Feglymycin. Whereas the antibacterial activity is significantly based on the three amino acids D-Hpg1, L-Hpg5, and L-Phe12, the inhibitory activity against MurA and MurC depends mainly on L-Asp13. The difference in the position dependence for antibacterial activity and enzyme inhibition suggests multiple molecular targets in the modes of action of Feglymycin.