2,2,3,3,4,4,4-heptafluorobutyl chloroformate | 108156-21-4

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 有机碳酸及其衍生物
• 英文名称: 2,2,3,3,4,4,4-heptafluorobutyl chloroformate
• 英文别名: 2,2,3,3,4,4,4-heptaflorobutyl chloroformate；2,2,3,3,4,4,4-Heptafluorobutyl chloroformate；2,2,3,3,4,4,4-heptafluorobutyl carbonochloridate
• CAS: 108156-21-4
• 化学式: C₅H₂ClF₇O₂
• 分子量: 262.512
• InChiKey: BTGGZMZAVPCGMB-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.6
• 重原子数：
  15
• 可旋转键数：
  4
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.8
• 拓扑面积：
  26.3
• 氢给体数：
  0
• 氢受体数：
  9

反应信息

• 作为反应物：
  描述：

  2,2,3,3,4,4,4-heptafluorobutyl chloroformate 在 盐酸 、 甲酸 、 三乙胺 作用下， 以 四氢呋喃 为溶剂， 反应 3.0h， 生成 2,2,3,3,4,4,4-heptafluorobutyl N-(L-prolylmethyl)-N-isopropylcarbamate hydrochloride
  参考文献：
  名称：

  Peptidyl carbamates incorporating amino acid isosteres as novel elastase inhibitors

  摘要：

  The design and synthesis of 13 novel peptidyl carbamates are described. When tested for inhibitory activity toward porcine pancreatic elastase, trypsin, and chymotrypsin, six compounds were found to specifically inhibit elastase without affecting the other two serine proteases. All the active inhibitors had an amino acid isostere at the P1 position. Kinetic studies indicated that the inhibition was competitive with Ki values ranging from 4.23 X 10(-5) to 2.4 X 10(-6) M. The degree of inhibition was found to be dependent on the specificity of the peptide chain for the extended subsites on the enzyme as well as on the nature of P1'. Preliminary work on one inhibitor indicates that the inhibition is reversible and proceeds via the rapid formation of a strong enzyme-inhibitor complex, followed by slow acylation of the serine residue on the active site of the enzyme. Peptidyl carbamates represent a novel class of elastase inhibitors.

  DOI：

  10.1021/jm00158a025
• 作为产物：
  描述：

  光气 、 2,2,3,3,4,4,4-七氟-1-丁醇 在 amine 作用下， 以 乙醚 为溶剂， 反应 3.75h， 以82%的产率得到2,2,3,3,4,4,4-heptafluorobutyl chloroformate
  参考文献：
  名称：

  Synthesis and in vitro evaluation of new derivatives of 2-substituted-6-fluorobenzo[d]thiazoles as cholinesterase inhibitors

  摘要：

  A series of novel cholinesterase inhibitors based on 2-substituted 6-fluorobenzo[d]thiazole were synthesised and characterised by IR, H-1, C-13 and F-19 NMR spectroscopy and HRMS. Purity was checked by elemental analyses. The novel carbamates were tested for their ability to inhibit acetylcholinesterase (AChE) and butyrylcholinesterase (BChE). The toxicity of the most active compounds was investigated using a standard in vitro test with HepG2 cells, and the ratio between biological activity and toxicity was determined. In addition, the toxicity of the most active compounds was evaluated against MCF7 cells using the xCELLigence system. Structure-activity relationships reflecting the dependence of cholinesterase inhibitors on the lipophilicity of the compounds as well as on the Taft polar and steric substituent constants are discussed. The specific orientation of the inhibitors in the binding site of acetylcholinesterase was determined using molecular docking of the most active compound. (C) 2013 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2013.01.052

文献信息

• Synthesis, structural characterization, docking, lipophilicity and cytotoxicity of 1-[(1R)-1-(6-fluoro-1,3-benzothiazol-2-yl)ethyl]-3-alkyl carbamates, novel acetylcholinesterase and butyrylcholinesterase pseudo-irreversible inhibitors
  作者：Vladimír Pejchal、Šárka Štěpánková、Marcela Pejchalová、Karel Královec、Radim Havelek、Zdeňka Růžičková、Haresh Ajani、Rabindranath Lo、Martin Lepšík

  DOI：10.1016/j.bmc.2016.02.033

  日期：2016.4

  confirmed by optical rotation measurements. The synthesized compounds were evaluated for their AChE and BChE inhibitory activities. In addition, the cytotoxicity of the most active compounds was investigated against human cell lines employing XTT tetrazolium salt reduction assay and xCELLigence system allowing a label-free assessment of the cells proliferation. Our results demonstrated that the inhibitory mechanism

  在当前的研究中，合成了十六种新颖的（R）-1-（6-氟苯并[ d ]噻唑-2-基）乙胺衍生物作为乙酰胆碱酯酶（AChE）和丁酰胆碱酯酶（BChE）抑制剂。化学结构以及合成化合物的纯度由IR，1 H，13 C，19证实F NMR，高分辨率质谱和元素分析。通过旋光度测量确认光学活性。评价合成的化合物的AChE和BChE抑制活性。此外，使用XTT四唑盐减量测定法和xCELLigence系统研究了最具活性的化合物对人细胞的细胞毒性，该方法可对细胞增殖进行无标记评估。我们的结果表明，与以前对氨基甲酸酯的研究一致，该抑制机制被证实是伪不可逆的。表示为3b，3d，3l和3n的化合物在所有评估的化合物中均显示出最佳的AChE抑制活性，且效力比标准药物卡巴拉汀大10倍之多。使用最先进的共价对接和评分方法确定结合模式。获得的数据清楚地表明，苯并噻唑氨基甲酸酯的3b，3d，3l和3n具有对AChE和BChE的高
• Synthesis and in vitro evaluation of new derivatives of 2-substituted-6-fluorobenzo[d]thiazoles as cholinesterase inhibitors
  作者：Aleš Imramovský、Vladimír Pejchal、Šárka Štěpánková、Katarína Vorčáková、Josef Jampílek、Ján Vančo、Petr Šimůnek、Karel Královec、Lenka Brůčková、Jana Mandíková、František Trejtnar

  DOI：10.1016/j.bmc.2013.01.052

  日期：2013.4

  A series of novel cholinesterase inhibitors based on 2-substituted 6-fluorobenzo[d]thiazole were synthesised and characterised by IR, H-1, C-13 and F-19 NMR spectroscopy and HRMS. Purity was checked by elemental analyses. The novel carbamates were tested for their ability to inhibit acetylcholinesterase (AChE) and butyrylcholinesterase (BChE). The toxicity of the most active compounds was investigated using a standard in vitro test with HepG2 cells, and the ratio between biological activity and toxicity was determined. In addition, the toxicity of the most active compounds was evaluated against MCF7 cells using the xCELLigence system. Structure-activity relationships reflecting the dependence of cholinesterase inhibitors on the lipophilicity of the compounds as well as on the Taft polar and steric substituent constants are discussed. The specific orientation of the inhibitors in the binding site of acetylcholinesterase was determined using molecular docking of the most active compound. (C) 2013 Elsevier Ltd. All rights reserved.
• Peptidyl carbamates incorporating amino acid isosteres as novel elastase inhibitors
  作者：George A. Digenis、Bushra J. Agha、Kiyoshi Tsuji、Masayuki Kato、Masaki Shinogi

  DOI：10.1021/jm00158a025

  日期：1986.8

  The design and synthesis of 13 novel peptidyl carbamates are described. When tested for inhibitory activity toward porcine pancreatic elastase, trypsin, and chymotrypsin, six compounds were found to specifically inhibit elastase without affecting the other two serine proteases. All the active inhibitors had an amino acid isostere at the P1 position. Kinetic studies indicated that the inhibition was competitive with Ki values ranging from 4.23 X 10(-5) to 2.4 X 10(-6) M. The degree of inhibition was found to be dependent on the specificity of the peptide chain for the extended subsites on the enzyme as well as on the nature of P1'. Preliminary work on one inhibitor indicates that the inhibition is reversible and proceeds via the rapid formation of a strong enzyme-inhibitor complex, followed by slow acylation of the serine residue on the active site of the enzyme. Peptidyl carbamates represent a novel class of elastase inhibitors.