L-2-amino-7-phenylheptanoic acid | 167113-43-1

• 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: L-2-amino-7-phenylheptanoic acid
• 英文别名: (S)-2-amino-7-phenylheptanoic acid；(2S)-2-amino-7-phenylheptanoic acid
• CAS: 167113-43-1
• 化学式: C₁₃H₁₉NO₂
• 分子量: 221.299
• InChiKey: XXWNWKHODOSRHI-LBPRGKRZSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.7
• 重原子数：
  16
• 可旋转键数：
  7
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.46
• 拓扑面积：
  63.3
• 氢给体数：
  2
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  二碳酸二叔丁酯 、 L-2-amino-7-phenylheptanoic acid 在 sodium hydroxide 作用下， 以 1,4-二氧六环 为溶剂， 以100%的产率得到L-2-(Boc-amino)-7-phenylheptanoic acid
  参考文献：
  名称：

  Design and Synthesis of Renin Inhibitors: Incorporation of Transition-State Isostere Side Chains That Span from the S1 to the S3 Binding Pockets and Examination of P3-Modified Renin Inhibitors

  摘要：

  A series of renin inhibitors were designed to examine the topography of the contiguous binding pocket of renin that is normally occupied by the P1 and P3 side chains. Molecular modeling suggested that extending the P1 hydrophobic side chain into the adjacent hydrophobic S3 enzyme pocket was feasible. Novel transition state isosteres with modified P1-->P3 side chains were synthesized and provided enhanced binding affinity when incorporated into renin inhibitors in which the P3 Phe was substituted by Gly. In a complementary approach, the binding affinities of a variety of P3-P4-modified peptidomimetic renin inhibitors that lacked substantial hydrophobic side chains at these sites were measured.

  DOI：

  10.1021/jm00015a012
• 作为产物：
  描述：

  (5-溴正戊基)苯 在 CoCl₂ 氢氧化钾 、 sodium ethanolate 作用下， 以 1,4-二氧六环 、 乙醇 、 水 为溶剂， 反应 77.5h， 生成 L-2-amino-7-phenylheptanoic acid
  参考文献：
  名称：

  Design and Synthesis of Renin Inhibitors: Incorporation of Transition-State Isostere Side Chains That Span from the S1 to the S3 Binding Pockets and Examination of P3-Modified Renin Inhibitors

  摘要：

  A series of renin inhibitors were designed to examine the topography of the contiguous binding pocket of renin that is normally occupied by the P1 and P3 side chains. Molecular modeling suggested that extending the P1 hydrophobic side chain into the adjacent hydrophobic S3 enzyme pocket was feasible. Novel transition state isosteres with modified P1-->P3 side chains were synthesized and provided enhanced binding affinity when incorporated into renin inhibitors in which the P3 Phe was substituted by Gly. In a complementary approach, the binding affinities of a variety of P3-P4-modified peptidomimetic renin inhibitors that lacked substantial hydrophobic side chains at these sites were measured.

  DOI：

  10.1021/jm00015a012

文献信息

• Method for detecting proteases and active infection in biological fluids and tissues
  申请人：Wardell Mark R.

  公开号：US10024817B2

  公开（公告）日：2018-07-17

  Electrochemical biosensing devices and methods detect the activity of proteases and active infection in biological samples. The devices and methods utilize distance constraints between a redox reporter and an electrode to create a change in current that is detected. The distance constraints are released when an analyte containing a specified protease or proteases reacts with a protein substrate sequence in the analyte. The particular protease or proteases to be detected can be selected by using biosensors with particular substrate sequences. The devices and methods are not only qualitative, they can be used to quantitatively evaluate protease content in samples.

  电化学生物传感装置和方法可检测生物样本中蛋白酶的活性和活性感染。这些装置和方法利用氧化还原反应器与电极之间的距离约束来产生可检测的电流变化。当含有特定蛋白酶的分析物与分析物中的蛋白质底物序列发生反应时，距离约束被释放。可以通过使用具有特定底物序列的生物传感器来选择要检测的特定蛋白酶。这些装置和方法不仅可以定性，还可用于定量评估样品中的蛋白酶含量。
• Method for Detecting Proteases and Active Infection in Biological Fluids and Tissues
  申请人：Wardell Mark R.

  公开号：US20160109401A1

  公开（公告）日：2016-04-21

  Electrochemical biosensing devices and methods detect the activity of proteases and active infection in biological samples. The devices and methods utilize distance constraints between a redox reporter and an electrode to create a change in current that is detected. The distance constraints are released when an analyte containing a specified protease or proteases reacts with a protein substrate sequence in the analyte. The particular protease or proteases to be detected can be selected by using biosensors with particular substrate sequences. The devices and methods are not only qualitative, they can be used to quantitatively evaluated protease content in samples.