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Micrococcin P1 Sale

(Synonyms: 微球菌素 P1) 目录号 : GC44192

A macrocyclic peptide antibiotic

Micrococcin P1 Chemical Structure

Cas No.:67401-56-3

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500μg
¥5,396.00
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2.5mg
¥17,542.00
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产品描述

Micrococcin P1 is a macrocyclic peptide antibiotic that functions as an acceptor-site-specific inhibitor of ribosomal protein synthesis, effectively preventing the growth of Gram-positive bacteria without affecting that of Gram-negative bacteria.[1][2]

Reference:
[1]. Carnio, M.C., Hötzel, A., Rudolf, M., et al. The macrocyclic peptide antibiotic micrococcin P(1) is secreted by the food-borne bacterium Staphylococcus equorum WS 2733 and inhibits Listeria monocytogenes on soft cheese. Applied and Environmental Microbiology 66(6), 2378-2384 (2000).
[2]. Mikolajka, A., Liu, H., Chen, Y., et al. Differential effects of thiopeptide and orthosomycin antibiotics on translational GTPases. Chemistry & Biology 18(5), 589-600 (2011)

Chemical Properties

Cas No. 67401-56-3 SDF
别名 微球菌素 P1
化学名 2’-[(11S,14Z,21S,28S)-14-ethylidene-9,10,11,12,13,14,20,21,27,28-decahydro-28-[(1R)-1-hydroxyethyl]-11-[(1R)-1-hydroxyethyl]-21-(1-methylethyl)-9,12,19,26-tetraoxo-19H,26H-8,5:18,15:25,22:32,29-tetranitrilo-5H,15H-pyrido[3,2-m][1,11,17,24,4,7,20,27]tetrathiatetraazacyclotriacontin-2-yl]-N-[(1Z)-1-[[[(2R)-2-hydroxypropyl]amino]carbonyl]-1-propen-1-yl]-[2,4’-bithiazole]-4-carboxamide
Canonical SMILES O=C(C1=CSC(C2=CSC(C3=NC(C4=CSC([C@H]([C@H](O)C)NC(C5=CSC6=N5)=O)=N4)=C(C7=NC(C(N[C@]([C@H](O)C)([H])C(N/C(C8=NC(C(N[C@H]6C(C)C)=O)=CS8)=C\C)=O)=O)=CS7)C=C3)=N2)=N1)N/C(C(NC[C@H](O)C)=O)=C\C
分子式 C48H49N13O9S6 分子量 1144.4
溶解度 Soluble in ethanol, DlMSO, DMF, methano 储存条件 Store at -20°C
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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。
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1 mM 0.8738 mL 4.3691 mL 8.7382 mL
5 mM 0.1748 mL 0.8738 mL 1.7476 mL
10 mM 0.0874 mL 0.4369 mL 0.8738 mL
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Research Update

Micrococcin P1: structure, biology and synthesis

Nat Prod Rep 2010 Mar;27(3):330-42.PMID:20179875DOI:10.1039/b919071f.

Micrococcin P1, 1, is an antibiotic that exhibits noteworthy antibacterial, antiprotozoal, antimalarial,cytotoxic, and gene-modulating activities. This notwithstanding, its precise structure remained undefined until mid-2009, when our group carried out the total synthesis of a substance that proved to be spectroscopically and polarimetrically identical to the natural product. This work lifted all structural and stereochemical ambiguities that have surrounded micrococcin since its discovery. Of course,knowledge of the precise structure of the molecule is essential in understanding intimate details of its mode of action and in charting possible medicinal chemistry activity. This review summarizes present knowledge about the sources, properties, and chemical synthesis of Micrococcin P1.

Micrococcin P1 and P2 from Epibiotic Bacteria Associated with Isolates of Moorea producens from Kenya

Mar Drugs 2022 Feb 7;20(2):128.PMID:35200657DOI:10.3390/md20020128.

Epibiotic bacteria associated with the filamentous marine cyanobacterium Moorea producens were explored as a novel source of antibiotics and to establish whether they can produce cyclodepsipeptides on their own. Here, we report the isolation of Micrococcin P1 (1) (C48H49N13O9S6; obs. m/z 1144.21930/572.60381) and micrococcin P2 (2) (C48H47N13O9S6; obs. m/z 1142.20446/571.60370) from a strain of Bacillus marisflavi isolated from M. producens' filaments. Interestingly, most bacteria isolated from M. producens' filaments were found to be human pathogens. Stalked diatoms on the filaments suggested a possible terrestrial origin of some epibionts. CuSO4·5H2O assisted differential genomic DNA isolation and phylogenetic analysis showed that a Kenyan strain of M. producens differed from L. majuscula strain CCAP 1446/4 and L. majuscula clones. Organic extracts of the epibiotic bacteria Pseudoalteromonas carrageenovora and Ochrobactrum anthropi did not produce cyclodepsipeptides. Further characterization of 24 Firmicutes strains from M. producens identified extracts of B. marisflavi as most active. Our results showed that the genetic basis for synthesizing Micrococcin P1 (1), discovered in Bacillus cereus ATCC 14579, is species/strain-dependent and this reinforces the need for molecular identification of M. producens species worldwide and their epibionts. These findings indicate that M. producens-associated bacteria are an overlooked source of antimicrobial compounds.

Micrococcin P1, a naturally occurring macrocyclic peptide inhibiting hepatitis C virus entry in a pan-genotypic manner

Antiviral Res 2016 Aug;132:287-95.PMID:27387825DOI:10.1016/j.antiviral.2016.07.002.

Hepatitis C virus (HCV) is considered a major public health concern worldwide. Despite recent advances in curing chronic hepatitis C, unmet medical needs still remain, especially due to the high economic burden of therapies. Accordingly, our study aimed to identify affordable novel HCV inhibitors by screening of natural product compound libraries. We identified Micrococcin P1, a macrocyclic peptide antibiotic, inhibiting HCV entry in a pan-genotypic manner with an EC50 range of 0.1-0.5 μM. Micrococcin P1 interfered with HCV entry at an attachment step. Furthermore, Micrococcin P1 efficiently inhibited HCV spread by blocking cell-free infection as well as cell-to-cell transmission, without affecting the secretion of infectious virions. Interestingly, the putative molecular target of Micrococcin P1 is glycoprotein E2 (IIe-630-Thr), as revealed by selection for viral drug resistance. In addition, Micrococcin P1 inhibited sofosbuvir-resistant HCV strains and showed synergy in combination with selected HCV drugs, suggesting an alternative treatment paradigm for patients. In conclusion, we identified Micrococcin P1 as specifically inhibiting entry of all HCV genotypes and demonstrated that Micrococcin P1 potentially could add value to therapies in combination with current HCV interventions.

Micrococcin P1 - A bactericidal thiopeptide active against Mycobacterium tuberculosis

Tuberculosis (Edinb) 2016 Sep;100:95-101.PMID:27553416DOI:10.1016/j.tube.2016.07.011.

The lack of proper treatment for serious infectious diseases due to the emergence of multidrug resistance reinforces the need for the discovery of novel antibiotics. This is particularly true for tuberculosis (TB) for which 3.7% of new cases and 20% of previously treated cases are estimated to be caused by multi-drug resistant strains. In addition, in the case of TB, which claimed 1.5 million lives in 2014, the treatment of the least complicated, drug sensitive cases is lengthy and disagreeable. Therefore, new drugs with novel targets are urgently needed to control resistant Mycobacterium tuberculosis strains. In this manuscript we report the characterization of the thiopeptide Micrococcin P1 as an anti-tubercular agent. Our biochemical experiments show that this antibiotic inhibits the elongation step of protein synthesis in mycobacteria. We have further identified micrococcin resistant mutations in the ribosomal protein L11 (RplK); the mutations were located in the proline loop at the N-terminus. Reintroduction of the mutations into a clean genetic background, confirmed that they conferred resistance, while introduction of the wild type RplK allele into resistant strains re-established sensitivity. We also identified a mutation in the 23S rRNA gene. These data, in good agreement with previous structural studies suggest that also in M. tuberculosis Micrococcin P1 functions by binding to the cleft between the 23S rRNA and the L11 protein loop, thus interfering with the binding of elongation factors Tu and G (EF-Tu and EF-G) and inhibiting protein translocation.

Total synthesis of Micrococcin P1 and thiocillin I enabled by Mo(vi) catalyst

Chem Sci 2018 Dec 3;10(7):1971-1975.PMID:30881626DOI:10.1039/c8sc04885a.

Thiopeptides are a class of potent antibiotics with promising therapeutic potential. We developed a novel Mo(vi)-oxide/picolinic acid catalyst for the cyclodehydration of cysteine peptides to form thiazoline heterocycles. With this powerful tool in hand, we completed the total syntheses of two representative thiopeptide antibiotics: Micrococcin P1 and thiocillin I. These two concise syntheses (15 steps, longest linear sequence) feature a C-H activation strategy to install the trisubstituted pyridine core and thiazole groups. The synthetic material displays promising antimicrobial properties measured against a series of Gram-positive bacteria.