alanylphenylalanine amide hydrochloride | 60240-16-6

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: alanylphenylalanine amide hydrochloride
• 英文别名: H-Ala-Phe-NH2 . HCl；(2S)-2-[[(2S)-2-aminopropanoyl]amino]-3-phenylpropanamide;hydrochloride
• CAS: 60240-16-6
• 化学式: C₁₂H₁₇N₃O₂*ClH
• mdl: MFCD00035522
• 分子量: 271.747
• InChiKey: ZBPKZDKCUDGUCQ-GNAZCLTHSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -0.27
• 重原子数：
  18
• 可旋转键数：
  5
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.333
• 拓扑面积：
  98.2
• 氢给体数：
  4
• 氢受体数：
  3

安全信息

• 海关编码：
  2924299090

反应信息

• 作为反应物：
  描述：

  alanylphenylalanine amide hydrochloride 在 sodium carbonate 作用下， 以 乙二醇二甲醚 、 水 、 N,N-二甲基甲酰胺 为溶剂， 反应 24.0h， 生成 4-Guanidino-benzoic acid [(S)-1-((S)-1-carbamoyl-2-phenyl-ethylcarbamoyl)-ethylcarbamoyl]-methyl ester
  参考文献：
  名称：

  Inactivation of trypsin-like proteases by depsipeptides of p-guanidinobenzoic acid

  摘要：

  A number of esters of p-guanidinobenzoic acid have been synthesized which contain a glycolyl peptide as the departing group. In the case of several enzymes such as trypsin and plasma kallikrein, depsipeptides were obtained which were considerably more reactive than the ethyl ester in inactivation of the protease by acyl-enzyme formation; the depsipeptide processing -CH2CO-Phe-NH2 as a leaving group displayed the highest reactivity. They were less effective in the case of urokinase, plasmin, and urinary kallikrein. Boar acrosin was very susceptible to inactivation by both ethyl and peptidyl esters. Depsipeptides possessing a longer peptide chain and a secondary carbon as a leaving group showed lower activities. The results demonstrate the productive use of the departing group region of protease active centers to obtain selectivity.

  DOI：

  10.1021/jm00138a011

文献信息

• Inactivation of trypsin-like proteases by depsipeptides of p-guanidinobenzoic acid
  作者：Vishwas S. Ganu、Elliott Shaw

  DOI：10.1021/jm00138a011

  日期：1981.6

  A number of esters of p-guanidinobenzoic acid have been synthesized which contain a glycolyl peptide as the departing group. In the case of several enzymes such as trypsin and plasma kallikrein, depsipeptides were obtained which were considerably more reactive than the ethyl ester in inactivation of the protease by acyl-enzyme formation; the depsipeptide processing -CH2CO-Phe-NH2 as a leaving group displayed the highest reactivity. They were less effective in the case of urokinase, plasmin, and urinary kallikrein. Boar acrosin was very susceptible to inactivation by both ethyl and peptidyl esters. Depsipeptides possessing a longer peptide chain and a secondary carbon as a leaving group showed lower activities. The results demonstrate the productive use of the departing group region of protease active centers to obtain selectivity.