S-[4-(bromomethyl)phenyl] benzenecarbothioc acid | 77552-03-5

• 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: S-[4-(bromomethyl)phenyl] benzenecarbothioc acid
• 英文别名: p-(Bromomethyl)-S-benzoylthiophenol
• CAS: 77552-03-5
• 化学式: C₁₄H₁₁BrOS
• 分子量: 307.211
• InChiKey: MBTJRIQEJRWUAU-UHFFFAOYSA-N

物化性质

• 沸点：
  391.0±34.0 °C(Predicted)
• 密度：
  1.48±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  4.51
• 重原子数：
  17.0
• 可旋转键数：
  3.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.07
• 拓扑面积：
  17.07
• 氢给体数：
  0.0
• 氢受体数：
  2.0

反应信息

• 作为反应物：
  描述：

  S-[4-(bromomethyl)phenyl] benzenecarbothioc acid 在 水 、 氢溴酸 作用下， 以 乙腈 为溶剂， 反应 1.5h， 生成 N1,N6-bis(4-mercaptobenzyl)-N1,N1,N6,N6-tetramethylhexane-1,6-diammonium bromide
  参考文献：
  名称：

  Oxidative folding of lysozyme with aromatic dithiols, and aliphatic and aromatic monothiols

  摘要：

  In vitro protein folding of disulfide containing proteins is aided by the addition of a redox buffer, which is composed of a small molecule disulfide and/or a small molecule thiol. In this study, we examined redox buffers containing asymmetric dithiols 1-5, which possess an aromatic and aliphatic thiol, and symmetric dithiols 6 and 7, which possess two aromatic thiols, for their ability to fold reduced lysozyme at pH 7.0 and 8.0. Most in vivo protein folding catalysts are dithiols. When compared to glutathione and glutathione disulfide, the standard redox buffer, dithiols 1-5 improved the protein folding rates but not the yields. However, dithiols 6 and 7, and the corresponding monothiol 8 increased the folding rates 8-17 times and improved the yields 15-42% at 1 mg/mL lysozyme. Moreover, aromatic dithiol 6 increased the in vitro folding yield as compared to the corresponding aromatic monothiol 8. Therefore, aromatic dithiols should be useful for protein folding, especially at high protein concentrations. (C) 2011 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2011.11.049
• 作为产物：
  描述：

  对甲苯二硫醚 在 aluminum (III) chloride 、 N-溴代丁二酰亚胺(NBS) 、 锌 作用下， 以 乙腈 、 苯 为溶剂， 反应 2.0h， 生成 S-[4-(bromomethyl)phenyl] benzenecarbothioc acid
  参考文献：
  名称：

  单壁碳纳米管的同时内部和外部功能化

  摘要：

  用带正电的二硫化物大环化合物处理单壁碳纳米管（SWCNT）产生了一种独特的材料，其中SWCNT从外部用大环化合物装饰，而在内部包含聚碘化物链。这种单壁碳纳米管豆荚材料的湿化学合成是朝着需要宏观量的用途迈出的重要一步。

  DOI：

  10.1002/anie.202402417

文献信息

• Properties of phenolic and thiophenolic surfactant micelles
  作者：Robert A. Moss、Frank M. Dix

  DOI：10.1021/jo00328a008

  日期：1981.7
• Rate enhancement of the oxidative folding of lysozyme by the use of aromatic thiol containing redox buffers
  作者：Minakshi C. Gurbhele-Tupkar、Lissette R. Perez、Yenia Silva、Watson J. Lees

  DOI：10.1016/j.bmc.2007.11.047

  日期：2008.3

  Almost all therapeutic proteins and most extracellular proteins contain disulfide bonds. The production of these proteins in bacteria or in vitro is challenging due to the need to form the correctly matched disulfide bonds during folding. One important parameter for efficient in vitro folding is the composition of the redox buffer, a mixture of a small molecule thiol and small molecule disulfide. The effects of different redox buffers on protein folding, however, have received limited attention. The oxidative folding of denatured reduced lysozyme was followed in the presence of redox buffers containing varying concentrations of five different aromatic thiols or the traditional aliphatic thiol glutathione (GSH). Aromatic thiols eliminated the lag phase at low disulfide concentrations, increased the folding rate constant up to 11-fold, and improved the yield of active protein relative to GSH. The yield of active protein was similar for four of the five aromatic thiols and for glutathione at pH 7 as well as for glutathione at pH 8.2. At pH 6 the positively charged aromatic thiol provided a higher yield than the negatively charged thiols. (C) 2007 Elsevier Ltd. All rights reserved.