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Bromamphenicol Sale

目录号 : GC42978

A dibrominated derivative of chloramphenicol

Bromamphenicol Chemical Structure

Cas No.:17371-30-1

规格 价格 库存 购买数量
5mg
¥1,181.00
现货
25mg
¥5,327.00
现货

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Sample solution is provided at 25 µL, 10mM.

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产品描述

Bromamphenicol is a dibrominated derivative of the antibiotic chloramphenicol. It inhibits rat liver mitochondrial and E. coli protein synthesis by 90.6 and 98.8%, respectively, when used at a concentration of 93 μM, and inhibits DNA synthesis in human lymphoblastoid cells by 83% at 1 mM. Bromamphenicol can also bind to the major adhesin subunit DraE from E. coli.

Chemical Properties

Cas No. 17371-30-1 SDF
Canonical SMILES OC[C@@H](NC(C(Br)Br)=O)[C@H](O)C1=CC=C([N+]([O-])=O)C=C1
分子式 C11H12Br2N2O5 分子量 412
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。
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。
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溶解性数据

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1 mg 5 mg 10 mg
1 mM 2.4272 mL 12.1359 mL 24.2718 mL
5 mM 0.4854 mL 2.4272 mL 4.8544 mL
10 mM 0.2427 mL 1.2136 mL 2.4272 mL
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Research Update

A structural study of the interaction between the Dr haemagglutinin DraE and derivatives of chloramphenicol

Acta Crystallogr D Biol Crystallogr 2009 Jun;65(Pt 6):513-22.PMID:19465765DOI:PMC2685729

Dr adhesins are expressed on the surface of uropathogenic and diffusely adherent strains of Escherichia coli. The major adhesin subunit (DraE/AfaE) of these organelles mediates attachment of the bacterium to the surface of the host cell and possibly intracellular invasion through its recognition of the complement regulator decay-accelerating factor (DAF) and/or members of the carcinoembryonic antigen (CEA) family. The adhesin subunit of the Dr haemagglutinin, a Dr-family member, additionally binds type IV collagen and is inhibited in all its receptor interactions by the antibiotic chloramphenicol (CLM). In this study, previous structural work is built upon by reporting the X-ray structures of DraE bound to two chloramphenicol derivatives: chloramphenicol succinate (CLS) and Bromamphenicol (BRM). The CLS structure demonstrates that acylation of the 3-hydroxyl group of CLM with succinyl does not significantly perturb the mode of binding, while the BRM structure implies that the binding pocket is able to accommodate bulkier substituents on the N-acyl group. It is concluded that modifications of the 3-hydroxyl group would generate a potent Dr haemagglutinin inhibitor that would not cause the toxic side effects that are associated with the normal bacteriostatic activity of CLM.