N-(3-phenylpropionyl)-L-valine methyl ester | 85541-12-4

• 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: N-(3-phenylpropionyl)-L-valine methyl ester
• 英文别名: methyl (2S)-3-methyl-2-(3-phenylpropanoylamino)butanoate
• CAS: 85541-12-4
• 化学式: C₁₅H₂₁NO₃
• 分子量: 263.337
• InChiKey: OPVNZTBDSGJMDN-AWEZNQCLSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.7
• 重原子数：
  19
• 可旋转键数：
  7
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.47
• 拓扑面积：
  55.4
• 氢给体数：
  1
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  N-(3-phenylpropionyl)-L-valine methyl ester 在 sodium hydroxide 作用下， 以 甲醇 为溶剂， 反应 1.0h， 生成 N-(3-phenylpropionyl)-L-valine
  参考文献：
  名称：

  Inhibition of Peptidylglycine .alpha.-Amidating Monooxygenase by N-Substituted Homocysteine Analogs

  摘要：

  C-terminal amidation is a posttranslational modification found in many neuropeptides. Peptidylglycine cl-amidating monooxygenase (PAM) catalyzes the synthesis of the biologically essential C-terminal amide from a glycine-extended precursor peptide. Reported herein are the first potent inhibitors of PAM. Dipeptides containing a C-terminal homocysteine and an N-acylated hydrophobic amino acid were found to inhibit PAM with IC(50)s in the low nanomolar range. Inhibition potency was dependent on both the carboxylate and the thiolate functionalities of the homocysteine and on the hydrophobic groups of the second amino acid. The thiolate was postulated to produce high binding affinities through coordination with the active-site copper. The compound series also exhibited potent inhibition of PAM in rat dorsal root ganglion cells as demonstrated by a dose-dependent increase in the substance P-Gly/substance P ratio. These results indicate that the compounds have sufficient potency and intracellular bioavailability to aid future studies focused on neuropeptide function and the contributions of neuropeptides to various disease processes.

  DOI：

  10.1021/jm00052a002
• 作为产物：
  描述：

  L-缬氨酸甲酯盐酸盐 、 3-苯丙酰氯 在 三乙胺 作用下， 以 乙醚 为溶剂， 以70%的产率得到N-(3-phenylpropionyl)-L-valine methyl ester
  参考文献：
  名称：

  Davies, John S.; Merritt, Raymond K.; Treadgold, Richard C., Journal of the Chemical Society. Perkin transactions I, 1982, # 12, p. 2939 - 2948

  摘要：

  DOI：

文献信息

• Nickel-Catalyzed Reduction of Secondary and Tertiary Amides
  作者：Bryan J. Simmons、Marie Hoffmann、Jaeyeon Hwang、Moritz K. Jackl、Neil K. Garg

  DOI：10.1021/acs.orglett.7b00683

  日期：2017.4.7

  The nickel-catalyzed reduction of secondary and tertiary amides to give amine products is reported. The transformation is tolerant of extensive variation with respect to the amide substrate, proceeds in the presence of esters and epimerizable stereocenters, and can be used to achieve the reduction of lactams. Moreover, this methodology provides a simple tactic for accessing medicinally relevant α-deuterated

  据报道，镍催化的仲和叔酰胺的还原生成胺产物。该转化耐受酰胺底物的广泛变化，在酯和可差向异构的立体中心存在下进行，并可用于实现内酰胺的还原。而且，该方法学提供了一种用于获取医学上相关的α-氘代胺的简单策略。
• Facile Reduction of Amides Using Nickel Catalysis: Reduction of 12-Aminododecanolactam
  作者：Bryan Simmons

  DOI：10.15227/orgsyn.096.0436

  日期：——
• Inhibition of Peptidylglycine .alpha.-Amidating Monooxygenase by N-Substituted Homocysteine Analogs
  作者：Mark D. Erion、Jenny Tan、Mary Wong、Arco Y. Jeng

  DOI：10.1021/jm00052a002

  日期：1994.12

  C-terminal amidation is a posttranslational modification found in many neuropeptides. Peptidylglycine cl-amidating monooxygenase (PAM) catalyzes the synthesis of the biologically essential C-terminal amide from a glycine-extended precursor peptide. Reported herein are the first potent inhibitors of PAM. Dipeptides containing a C-terminal homocysteine and an N-acylated hydrophobic amino acid were found to inhibit PAM with IC(50)s in the low nanomolar range. Inhibition potency was dependent on both the carboxylate and the thiolate functionalities of the homocysteine and on the hydrophobic groups of the second amino acid. The thiolate was postulated to produce high binding affinities through coordination with the active-site copper. The compound series also exhibited potent inhibition of PAM in rat dorsal root ganglion cells as demonstrated by a dose-dependent increase in the substance P-Gly/substance P ratio. These results indicate that the compounds have sufficient potency and intracellular bioavailability to aid future studies focused on neuropeptide function and the contributions of neuropeptides to various disease processes.
• Davies, John S.; Merritt, Raymond K.; Treadgold, Richard C., Journal of the Chemical Society. Perkin transactions I, 1982, # 12, p. 2939 - 2948
  作者：Davies, John S.、Merritt, Raymond K.、Treadgold, Richard C.、Morley, John S.

  DOI：——

  日期：——