1-甲基-5-四唑基氯硫代甲酸酯 | 102284-63-9

• 分子结构分类: 有机化合物 - 有机硫化合物 - 硫醚类
• 中文名称: 1-甲基-5-四唑基氯硫代甲酸酯
• 英文名称: 1-methyl-5-tetrazolyl chlorothioformate
• 英文别名: 1-methyl-5-tetrazolyl thiochloroformate；S-(1-methyltetrazol-5-yl) chloromethanethioate
• CAS: 102284-63-9
• 化学式: C₃H₃ClN₄OS
• 分子量: 178.602
• InChiKey: RQCJIJANLKANGC-UHFFFAOYSA-N

物化性质

• 沸点：
  347.3±25.0 °C(Predicted)
• 密度：
  1.83±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  1
• 重原子数：
  10
• 可旋转键数：
  2
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.33
• 拓扑面积：
  86
• 氢给体数：
  0
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  1-甲基-5-四唑基氯硫代甲酸酯 、 N-(N'-t-Boc-L-prolyl)methyl-N-isopropylamine 在 三乙胺 作用下， 以 四氢呋喃 为溶剂， 反应 1.0h， 以74%的产率得到S-1-methyl-5-tetrazolyl N-<(N-boc-L-prolyl)methyl>-N-isopropylthiocarbamate
  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 、 1-甲基-5-巯基-1H-四氮唑 在 三乙胺 作用下， 以 四氢呋喃 、 苯 为溶剂， 以0.62 g (89.7%)的产率得到1-甲基-5-四唑基氯硫代甲酸酯
  参考文献：
  名称：

  Peptide elastase inhibitors and methods

  摘要：

  以下是酶弹性蛋白酶抑制剂的通用公式：##STR1## 其中Z从R"O--Suc--组成的群体中选择，其中R"是1到3个碳原子的低碳烷基和CF.sub.3 CO--; X是氧或硫；R'从1到4个碳原子的直链或次级支链烷基，2到3个碳原子的烯烃基，2到4个碳原子的炔烃基，3到6个碳原子的环烷基和苄基中选择，R从取代或未取代的苯基中选择，其中取代基从硝基和五氟取代基中选择；苄基，CH.sub.2 CF.sub.2 CF.sub.2 CF.sub.3，1-低碳烷基四唑基，1-苯基四唑基，2-硫代-3-噻唑烷基-，吡啶基和苯并噻唑基，条件是当R为对硝基苯基时，R'不是叔丁基、苄基或环己基，且当X为硫时，R不是苄基。

  公开号：

  US04643991A1

文献信息

• Peptide elastase inhibitors and methods
  申请人：The University of Kentucky Research Foundation

  公开号：US04643991A1

  公开（公告）日：1987-02-17

  Compounds useful as inhibitors of the enzyme elastase are of the following general formula: ##STR1## wherein Z is selected from the group consisting of R"O--Suc-- where R" is lower alkyl of 1 to 3 carbon atoms and CF.sub.3 CO--; X is oxygen or sulfur; R' is selected from the group consisting of straight or secondary branch-chained alkyl of 1 to 4 carbon atoms, alkenyl of 2 to 3 carbon atoms, alkynyl of 2 to 4 carbon atoms, cycloalkyl of 3 to 6 carbon atoms, and benzyl, and R is selected from the group consisting of susbstituted or unsubstituted phenyl wherein the substituents are selected from the group consisting of nitro, and pentafluoro; benzyl, CH.sub.2 CF.sub.2 CF.sub.2 CF.sub.3, 1-lower alkyl tetrazolyl, 1-phenyltetrazolyl, 2-thioxo-3-thiazolidinyl-, pyridyl and benzothiazolyl, provided that when R is paranitrophenyl, R' is other than tertiary-butyl, benzyl or cyclohexyl, and when X is sulfur, R is other than benzyl.

  以下是酶弹性蛋白酶抑制剂的通用公式：##STR1## 其中Z从R"O--Suc--组成的群体中选择，其中R"是1到3个碳原子的低碳烷基和CF.sub.3 CO--; X是氧或硫；R'从1到4个碳原子的直链或次级支链烷基，2到3个碳原子的烯烃基，2到4个碳原子的炔烃基，3到6个碳原子的环烷基和苄基中选择，R从取代或未取代的苯基中选择，其中取代基从硝基和五氟取代基中选择；苄基，CH.sub.2 CF.sub.2 CF.sub.2 CF.sub.3，1-低碳烷基四唑基，1-苯基四唑基，2-硫代-3-噻唑烷基-，吡啶基和苯并噻唑基，条件是当R为对硝基苯基时，R'不是叔丁基、苄基或环己基，且当X为硫时，R不是苄基。
• 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.