p-n-propylbenzamidinium chloride | 29147-97-5

• 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: p-n-propylbenzamidinium chloride
• 英文别名: p-n-propylbenzamidine hydrochloride；4-propylbenzenecarboximidamide;hydrochloride
• CAS: 29147-97-5
• 化学式: C₁₀H₁₄N₂*ClH
• 分子量: 198.695
• InChiKey: OWBZTQZODPJBSZ-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.34
• 重原子数：
  13
• 可旋转键数：
  3
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.3
• 拓扑面积：
  49.9
• 氢给体数：
  3
• 氢受体数：
  1

反应信息

• 作为反应物：
  描述：

  p-n-propylbenzamidinium chloride 、 乙氧基甲叉丙二酸二乙酯 在 sodium ethanolate 作用下， 以 乙醇 为溶剂， 生成 6-oxo-2-(4-propyl-phenyl)-1,6-dihydro-pyrimidine-5-carboxylic acid ethyl ester
  参考文献：
  名称：

  Phenyl-pyrimidines

  摘要：

  公式为##STR1##的苯基嘧啶，其中R.sub.1和R.sub.2如下所述。最终产物可用作液晶。

  公开号：

  US03997536A1
• 作为产物：
  描述：

  对甲苯腈 在 三甲基铝 、 氯化铵 、 sodium amide 作用下， 以 乙醚 、 氨 、 甲苯 为溶剂， 反应 4.5h， 生成 p-n-propylbenzamidinium chloride
  参考文献：
  名称：

  Understanding Binding Affinity:  A Combined Isothermal Titration Calorimetry/Molecular Dynamics Study of the Binding of a Series of Hydrophobically Modified Benzamidinium Chloride Inhibitors to Trypsin

  摘要：

  The binding of a series of p-alkylbenzamidinium chloride inhibitors to the serine proteinase trypsin over a range of temperatures has been studied using isothermal titration (micro)calorimetry and molecular dynamics simulation techniques. The inhibitors have small structural variations at the para position of the benzamidinium ion. They show small differences in relative binding affinity but large compensating differences in enthalpy and entropy. Binding affinity decreases with increased branching at the first carbon but increases with increasing the length of a linear alkyl substituent, suggesting that steric hindrance and hydrophobic interactions play dominant roles in binding. Structural analysis showed that the backbone of the enzyme was unaffected by the change of the para substituent. In addition, binding does not correlate strongly with octanol/water partition data. To further characterize this system, the change in the heat capacity on binding, the change in solvent-accessible surface area on binding, the effect of inhibitor binding on the hydration of the active site, the pK(a) of His57, and interactions within the catalytic triad have been investigated. Although the changes in inhibitor structure are small, it is demonstrated that simple concepts such as steric hindrance, hydrophobicity, and buried surface area are insufficient to explain the binding data. Other factors, such as access to the binding site and the cost of dehydration of the active site, are of equal or greater importance.

  DOI：

  10.1021/ja034676g

文献信息

• Biering, A.; Demus, D.; Lichter, L., Molecular Crystals and Liquid Crystals (1969-1991), 1980, vol. 62, p. 1 - 24
  作者：Biering, A.、Demus, D.、Lichter, L.、Sackmann, H.、Wiegeleben, A.、et al.

  DOI：——

  日期：——
• Kraus, G.; Zaschke, H., Journal fur praktische Chemie (Leipzig 1954), 1981, vol. 323, # 2, p. 199 - 206
  作者：Kraus, G.、Zaschke, H.

  DOI：——

  日期：——
• BOLLER A.; COREGHETTI M.; SCHERRER H., Z. NATURFORSCH., 1978, B33, NO 4, 433-438
  作者：BOLLER A.、 COREGHETTI M.、 SCHERRER H.

  DOI：——

  日期：——
• Pyrimidine
  申请人：MERCK PATENT GmbH

  公开号：EP0158137B1

  公开（公告）日：1990-01-10
• US3997536A
  申请人：——

  公开号：US3997536A

  公开（公告）日：1976-12-14