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Thiocillin I Sale

(Synonyms: 高硫青霉素I) 目录号 : GC45038

An antibiotic

Thiocillin I Chemical Structure

Cas No.:59979-01-0

规格 价格 库存 购买数量
500μg
¥3,854.00
现货
2.5mg
¥13,500.00
现货

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Sample solution is provided at 25 µL, 10mM.

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产品描述

Thiocillin I is an antibiotic originally isolated from Bacillus that has activity against Gram-positive, but not Gram-negative, bacteria. It inhibits the growth of B. subtilis, B. anthracis, S. aureus, S. pyogenes, and S. pneumoniae strains in vitro (MICs = 0.2-3.13 μg/ml). Thiocillin I exhibits antibiotic activity in a mouse model of S. pyogenes infection (ED50 = 2.91 mg/kg).

Chemical Properties

Cas No. 59979-01-0 SDF
别名 高硫青霉素I
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)(O)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 C48H49N13O10S6 分子量 1160.4
溶解度 DMF: soluble,DMSO: soluble,Ethanol: soluble,Methanol: soluble 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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溶解性数据

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1 mM 0.8618 mL 4.3089 mL 8.6177 mL
5 mM 0.1724 mL 0.8618 mL 1.7235 mL
10 mM 0.0862 mL 0.4309 mL 0.8618 mL
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Research Update

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.

Dynamic interspecies interactions and robustness in a four-species model biofilm

Microbiologyopen 2021 Nov;10(6):e1254.PMID:34964290DOI:10.1002/mbo3.1254.

Interspecific interactions within biofilms determine relative species abundance, growth dynamics, community resilience, and success or failure of invasion by an extraneous organism. However, deciphering interspecific interactions and assessing their contribution to biofilm properties and function remain a challenge. Here, we describe the constitution of a model biofilm composed of four bacterial species belonging to four different genera (Rhodocyclus sp., Pseudomonas fluorescens, Kocuria varians, and Bacillus cereus), derived from a biofilm isolated from an industrial milk pasteurization unit. We demonstrate that the growth dynamics and equilibrium composition of this biofilm are highly reproducible. Based on its equilibrium composition, we show that the establishment of this four-species biofilm is highly robust against initial, transient perturbations but less so towards continuous perturbations. By comparing biofilms formed from different numbers and combinations of the constituent species and by fitting a growth model to the experimental data, we reveal a network of dynamic, positive, and negative interactions that determine the final composition of the biofilm. Furthermore, we reveal that the molecular determinant of one negative interaction is the Thiocillin I synthesized by the B. cereus strain, and demonstrate its importance for species distribution and its impact on robustness by mutational analysis of the biofilm ecosystem.

Total synthesis and complete structural assignment of Thiocillin I

J Am Chem Soc 2011 Apr 20;133(15):5900-4.PMID:21446660DOI:10.1021/ja110166x.

The total synthesis of the thiopeptide antibiotic, Thiocillin I, is described. This work unequivocally defines the full structure (constitution and configuration) of the natural product as 1.

Thiopeptide biosynthesis featuring ribosomally synthesized precursor peptides and conserved posttranslational modifications

Chem Biol 2009 Feb 27;16(2):141-7.PMID:19246004DOI:10.1016/j.chembiol.2009.01.007.

Thiopeptides, with potent activity against various drug-resistant pathogens, contain a characteristic macrocyclic core consisting of multiple thiazoles, dehydroamino acids, and a 6-membered nitrogen heterocycle. Their biosynthetic pathways remain elusive, in spite of great efforts by in vivo feeding experiments. Here, cloning, sequencing, and characterization of the thiostrepton and siomycin A gene clusters unveiled a biosynthetic paradigm for the thiopeptide specific core formation, featuring ribosomally synthesized precursor peptides and conserved posttranslational modifications. The paradigm generality for thiopeptide biosynthesis was supported by genome mining and ultimate confirmation of the Thiocillin I production in Bacillus cereus ATCC 14579, a strain that was previously unknown as a thiopeptide producer. These findings set the stage to accelerate the discovery of thiopeptides by prediction at the genetic level and to generate structural diversity by applying combinatorial biosynthesis methods.