tert-butyl 2-hydrazineyl-2-oxoacetate | 92819-78-8

• 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: tert-butyl 2-hydrazineyl-2-oxoacetate
• 英文别名: Oxalsaeure-mono-tert.-butylester-hydrazid；Oxalsaeure-tert.-butylester-hydrazid；tert-butyl carbazate；tert-butyl 2-hydrazinyl-2-oxoacetate
• CAS: 92819-78-8
• 化学式: C₆H₁₂N₂O₃
• 分子量: 160.173
• InChiKey: VQZSATCQAKEJBO-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.6
• 重原子数：
  11
• 可旋转键数：
  3
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.67
• 拓扑面积：
  81.4
• 氢给体数：
  2
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  tert-butyl 2-hydrazineyl-2-oxoacetate 生成 N^β,N^β-bis(tert-butoxycarbonyl)-hydrazine
  参考文献：
  名称：

  New Methods of Introducing the Carbo-t-butoxy Amino-Protecting Group. Preparation and Use of t-Butyl Cyanoformate and t-Butyl Iminodicarboxylate¹

  摘要：

  DOI：

  10.1021/jo01033a003
• 作为产物：
  描述：

  乙二酸 1-(1,1-二甲基乙基) 2-乙酯 在 一水合肼 作用下， 以 二氯甲烷 为溶剂， 生成 tert-butyl 2-hydrazineyl-2-oxoacetate
  参考文献：
  名称：

  New Methods of Introducing the Carbo-t-butoxy Amino-Protecting Group. Preparation and Use of t-Butyl Cyanoformate and t-Butyl Iminodicarboxylate¹

  摘要：

  DOI：

  10.1021/jo01033a003

文献信息

• Two-Component Coupling of Carbodiimides and Hydrazides Provides Convergent Access to Biologically Active Compounds
  作者：Elisabeth T. Hennessy、Maximilian D. Palkowitz、Josep Saurí、Aaron C. Sather

  DOI：10.1021/acs.orglett.2c02555

  日期：2022.9.2

  A novel, convergent synthesis of aminotriazoloquinazolines is reported. These heterocycles are reliably prepared via a “click-like” reaction between readily available aryl carbodiimides and acyl or aryl hydrazides. Such products are of particular interest with respect to their inhibitory activity against the A2A and A2B adenosine receptors, and the title two-component coupling reaction has greatly

  报道了一种新型的氨基三唑并喹唑啉的聚合合成。这些杂环是通过容易获得的芳基碳二亚胺和酰基或芳基酰肼之间的“点击样”反应可靠地制备的。此类产品在其对 A 2A和 A 2B腺苷受体的抑制活性方面特别令人感兴趣，并且标题双组分偶联反应极大地加速了该领域中有效/选择性化学物质的发现。
• Aza-Peptidyl Michael Acceptor and Epoxide Inhibitors—Potent and Selective Inhibitors of Schistosoma mansoni and Ixodes ricinus Legumains (Asparaginyl Endopeptidases)
  作者：Asli Ovat、Fanuel Muindi、Crystal Fagan、Michelle Brouner、Elizabeth Hansell、Jan Dvořák、Daniel Sojka、Petr Kopáček、James H. McKerrow、Conor R. Caffrey、James C. Powers

  DOI：10.1021/jm900849h

  日期：2009.11.26

  Aza-peptide Michael acceptors and epoxides with the general structure of YCO-Ala-Ala-AAsn-trans-CH=CHCOR and YCO-Ala-Ala-AAsn-EP-COR, respectively, are shown to be potent inhibitors of asparaginyl endopeptidases (legumains) from the bloodfluke, Schistosoma mansoni (SmAE), and the hard tick, Ixodes ricinus (IrAE). Structure-activity relationships (SARs) were determined for a set of 41 aza-peptide Michael acceptors and eight aza-peptide epoxides. Both enzymes prefer disubstituted amides to monosubstituted amides in the P1' position, and potency increased as we increased the hydrophobicity of the inhibitor in this position. Extending the inhibitor to P5 resulted in increased potency, especially against IrAE, and both enzymes prefer small over large hydrophobic residues at P2. Aza-peptide Michael acceptor inhibitors are more potent than aza-peptide epoxide inhibitors, and for some of these compounds, second-order inhibiton rate constants are the fastest yet discovered. Given the central functions of these enzymes in both parasites, the data presented here may facilitate the eventual design of selective antiparasitic drugs.