2-bromo-N-(2-iodophenyl)acetamide | 1339628-12-4

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: 2-bromo-N-(2-iodophenyl)acetamide
• CAS: 1339628-12-4
• 化学式: C₈H₇BrINO
• mdl: MFCD18839922
• 分子量: 339.958
• InChiKey: MRBIPBIGIOLLHJ-UHFFFAOYSA-N

物化性质

• 沸点：
  406.9±30.0 °C(Predicted)
• 密度：
  2.154±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  2.3
• 重原子数：
  12
• 可旋转键数：
  2
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.125
• 拓扑面积：
  29.1
• 氢给体数：
  1
• 氢受体数：
  1

反应信息

• 作为反应物：
  描述：

  2-bromo-N-(2-iodophenyl)acetamide 在 Crabtree's catalyst 、 氢气 、 sodium hydride 作用下， 以 四氢呋喃 、 二氯甲烷 、 1,2-二氯乙烷 、 mineral oil 为溶剂， 20.0~90.0 ℃ 、4.05 MPa 条件下， 反应 59.0h， 生成 rac-3-(8-ethyl-5,6,7,8-tetrahydroindolizin-8-yl)-N-(2-iodophenyl)propanamide
  参考文献：
  名称：

  （±）-Rhazinal的形式全合成：评估自由基方法

  摘要：

  摘要 我们描述了外消旋的天然产物鼠李糖苷的正式全合成，方法是将最近报道的四氢吲哚嗪中间体快速合成成由Trauner报道的环化前体。合成着重于功能基团的早期和趋同引入，同时描述了该方法遇到的合成挑战。 我们描述了外消旋的天然产物鼠李糖苷的正式全合成，方法是将最近报道的四氢吲哚嗪中间体快速合成成由Trauner报道的环化前体。合成着重于功能基团的早期和趋同引入，同时描述了该方法遇到的合成挑战。

  DOI：

  10.1055/s-0036-1588956
• 作为产物：
  描述：

  2-碘苯胺 、 溴乙酰溴 在 三乙胺 作用下， 以 二氯甲烷 为溶剂， 反应 1.0h， 以88%的产率得到2-bromo-N-(2-iodophenyl)acetamide
  参考文献：
  名称：

  （±）-Rhazinal的形式全合成：评估自由基方法

  摘要：

  摘要 我们描述了外消旋的天然产物鼠李糖苷的正式全合成，方法是将最近报道的四氢吲哚嗪中间体快速合成成由Trauner报道的环化前体。合成着重于功能基团的早期和趋同引入，同时描述了该方法遇到的合成挑战。 我们描述了外消旋的天然产物鼠李糖苷的正式全合成，方法是将最近报道的四氢吲哚嗪中间体快速合成成由Trauner报道的环化前体。合成着重于功能基团的早期和趋同引入，同时描述了该方法遇到的合成挑战。

  DOI：

  10.1055/s-0036-1588956

文献信息

• Nickel-Mediated Inter- and Intramolecular C–S Coupling of Thiols and Thioacetates with Aryl Iodides at Room Temperature
  作者：Xiao-Bo Xu、Jian Liu、Jian-Jian Zhang、Ya-Wen Wang、Yu Peng

  DOI：10.1021/ol303366u

  日期：2013.2.1

  A Ni(0)-catalyzed intermolecular cross-coupling of various functionalized thiols and aryl Iodides has been developed and successfully extended to less explored intramolecular versions, where thioacetates could also be utilized as the strategic surrogate. Air-stable precatalysts, very mild conditions, and an easy protocol allow rapid access to medicinally useful aryl thioethers, as demonstrated in the facile synthesis of (+/-)-chuangxinmycin as a key step.
• Three-Step Synthesis of Triazolobenzodiazepinones via Sonogashira/Huisgen Protocol
  作者：Giorgio Molteni

  DOI：10.3987/com-13-12752

  日期：——

  The sequential Sonogashira coupling/intramolecular azide cycloaddition (Huisgen cycloaddition) protocol was performed onto N-(2-iodophenyl)-2-azidoacetamide as the acyclic precursor giving tricyclic 1,2,3-triazolo-[5,1-d][1,4]benzodiazepin-2-ones. These target products were thus obtained through a three-step synthesis in variable yields depending upon the substituent placed onto the acetylenic counterpart. The influence of catalyst concentration, reaction temperature and reaction medium upon cycloadduct yields were also studied.
• Ebselen Inhibits Hepatitis C Virus NS3 Helicase Binding to Nucleic Acid and Prevents Viral Replication
  作者：Sourav Mukherjee、Warren S. Weiner、Chad E. Schroeder、Denise S. Simpson、Alicia M. Hanson、Noreena L. Sweeney、Rachel K. Marvin、Jean Ndjomou、Rajesh Kolli、Dragan Isailovic、Frank J. Schoenen、David N. Frick

  DOI：10.1021/cb500512z

  日期：2014.10.17

  The hepatitis C virus (HCV) nonstructural protein 3 (NS3) is both a protease, which cleaves viral and host proteins, and a helicase that separates nucleic acid strands, using ATP hydrolysis to fuel the reaction. Many antiviral drugs, and compounds in clinical trials, target the NS3 protease, but few helicase inhibitors that function as antivirals have been reported. This study focuses on the analysis of the mechanism by which ebselen (2-phenyl-1,2-benzisoselenazol-3-one), a compound previously shown to be a HCV antiviral agent, inhibits the NS3 helicase. Ebselen inhibited the abilities of NS3 to unwind nucleic acids, to bind nucleic acids, and to hydrolyze ATP, and about 1 mu M ebselen was sufficient to inhibit each of these activities by 50%. However, ebselen had no effect on the activity of the NS3 protease, even at 100 times higher ebselen concentrations. At concentrations below 10 mu M, the ability of ebselen to inhibit HCV helicase was reversible, but prolonged incubation of HCV helicase with higher ebselen concentrations led to irreversible inhibition and the formation of covalent adducts between ebselen and all 14 cysteines present in HCV helicase. Ebselen analogues with sulfur replacing the selenium were just as potent HCV helicase inhibitors as ebselen, but the length of the linker between the phenyl and benzisoselenazol rings was critical. Modifications of the phenyl ring also affected compound potency over 30-fold, and ebselen was a far more potent helicase inhibitor than other, structurally unrelated, thiol-modifying agents. Ebselen analogues were also more effective antiviral agents, and they were less toxic to hepatocytes than ebselen. Although the above structure-activity relationship studies suggest that ebselen targets a specific site on NS3, we were unable to confirm binding to either the NS3 ATP binding site or nucleic acid binding cleft by examining the effects of ebselen on NS3 proteins lacking key cysteines.