1,7,7-三甲基降冰片烷-2-硫醇 | 5391-78-6

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 异戊烯醇脂质
• 中文名称: 1,7,7-三甲基降冰片烷-2-硫醇
• 英文名称: bornane-2-thiol
• 英文别名: Camphanthiol-(2)；Bornan-2-thiol；Thioborneol；Bornanthiol-2；2-Bornanethiol；1,7,7-trimethylbicyclo[2.2.1]heptane-2-thiol
• CAS: 5391-78-6
• 化学式: C₁₀H₁₈S
• 分子量: 170.319
• InChiKey: YZBDTMJKESVEBP-UHFFFAOYSA-N

物化性质

• 沸点：
  205.9±9.0 °C(Predicted)
• 密度：
  0.98±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  3.7
• 重原子数：
  11
• 可旋转键数：
  0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  1.0
• 拓扑面积：
  1
• 氢给体数：
  1
• 氢受体数：
  1

安全信息

• 海关编码：
  2930909090

反应信息

• 作为反应物：
  描述：

  1,7,7-三甲基降冰片烷-2-硫醇 在 铬酸 作用下， 生成 硫代樟脑
  参考文献：
  名称：

  Houben; Doescher, Chemische Berichte, 1906, vol. 39, p. 3505

  摘要：

  DOI：
• 作为产物：
  描述：

  camphor dithioketal 、 正丁基锂 生成 1,7,7-三甲基降冰片烷-2-硫醇
  参考文献：
  名称：

  WILSON, S. R.;CALDERA, P.;JESTER, M. A., J. ORG. CHEM., 1982, 47, N 17, 3319-3321

  摘要：

  DOI：

文献信息

• Wuyts, Chemische Berichte, 1903, vol. 36, p. 864
  作者：Wuyts

  DOI：——

  日期：——
• Borsche; Lange, Chemische Berichte, 1906, vol. 39, p. 2348
  作者：Borsche、Lange

  DOI：——

  日期：——
• The N-terminal region of cystatin A (stefin A) binds to papain subsequent to the two hairpin loops of the inhibitor. Demonstration of two-step binding by rapid-kinetic studies of cystatin A labeled at the N-terminus with a fluorescent reporter group
  作者：Sergio Estrada、Elke Raub-Segall、Ingemar Björk、Steven T. Olson

  DOI：10.1110/ps.9.11.2218

  日期：——

  AbstractThe three‐dimensional structures of cystatins, and other evidence, suggest that the flexible N‐terminal region of these inhibitors may bind to target proteinases independent of the two rigid hairpin loops forming the remainder of the inhibitory surface. In an attempt to demonstrate such two‐step binding, which could not be identified in previous kinetics studies, we introduced a cysteine residue before the N‐terminus of cystatin A and labeled this residue with fluorescent probes. Binding of AANS‐ and AEDANS‐labeled cystatin A to papain resulted in ∼4‐fold and 1.2‐fold increases of probe fluorescence, respectively, reflecting the interaction of the N‐terminal region with the enzyme. Observed pseudo‐first‐order rate constants, measured by the loss of papain activity in the presence of a fluorogenic substrate, for the reaction of the enzyme with excess AANS‐cystatin A increased linearly with the concentration of the latter. In contrast, pseudo‐first‐order rate constants, obtained from measurements of the change of probe fluorescence with either excess enzyme or labeled inhibitor, showed an identical hyperbolic dependence on the concentration of the reactant in excess. This dependence demonstrates that the binding occurs in two steps, and implies that the labeled N‐terminal region of cystatin A interacts with the proteinase in the second step, subsequent to the hairpin loops. The comparable affinities and dissociation rate constants for the binding of labeled and unlabeled cystatin A to papain indicate that the label did not appreciably perturb the interaction, and that unlabeled cystatin therefore also binds in a similar two‐step manner. Such independent binding of the N‐terminal regions of cystatins to target proteinases after the hairpin loops may be characteristic of most cystatin–proteinase reactions.
• Houben; Doescher, Chemische Berichte, 1906, vol. 39, p. 3505
  作者：Houben、Doescher

  DOI：——

  日期：——
• WILSON, S. R.;CALDERA, P.;JESTER, M. A., J. ORG. CHEM., 1982, 47, N 17, 3319-3321
  作者：WILSON, S. R.、CALDERA, P.、JESTER, M. A.

  DOI：——

  日期：——