2-[2-(tert-butoxycarbonyl)hydrazono]acetic acid | 1072934-75-8

• 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: 2-[2-(tert-butoxycarbonyl)hydrazono]acetic acid
• 英文别名: 2-[2-(Tert-butoxycarbonyl)hydrazono]acetic acid；2-[(2-methylpropan-2-yl)oxycarbonylhydrazinylidene]acetic acid
• CAS: 1072934-75-8
• 化学式: C₇H₁₂N₂O₄
• 分子量: 188.183
• InChiKey: DZLIKTHCVGMTLR-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.4
• 重原子数：
  13
• 可旋转键数：
  4
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.57
• 拓扑面积：
  88
• 氢给体数：
  2
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  2-[2-(tert-butoxycarbonyl)hydrazono]acetic acid 在 palladium 10% on activated carbon 、 氢气 作用下， 以 甲醇 为溶剂， 20.0 ℃ 、330.01 kPa 条件下， 反应 1.5h， 以78%的产率得到(2-{[(2-甲基-2-丙基)氧基]羰基}肼基)乙酸
  参考文献：
  名称：

  3-Cyano-3-aza-β-amino Acid Derivatives as Inhibitors of Human Cysteine Cathepsins

  摘要：

  Nitrile-type inhibitors are known to interact with cysteine proteases in a covalent-reversible manner. The chemotype of 3-cyano-3-aza-beta-amino acid derivatives was designed in which the N-cyano group is centrally arranged in the molecule to allow for interactions with the nonprimed and primed binding regions of the target enzymes. These compounds were evaluated as inhibitors of the human cysteine cathepsins K, S, B, and L. They exhibited slow-binding behavior and were found to be exceptionally potent, in particular toward cathepsin K, with second-order rate constants up to 52 900 x 10(3) M-1 s(-1).

  DOI：

  10.1021/ml500238q
• 作为产物：
  描述：

  肼基甲酸叔丁酯 、 乙醛酸 以 乙醇 为溶剂， 反应 19.0h， 以47%的产率得到2-[2-(tert-butoxycarbonyl)hydrazono]acetic acid
  参考文献：
  名称：

  3-Cyano-3-aza-β-amino Acid Derivatives as Inhibitors of Human Cysteine Cathepsins

  摘要：

  Nitrile-type inhibitors are known to interact with cysteine proteases in a covalent-reversible manner. The chemotype of 3-cyano-3-aza-beta-amino acid derivatives was designed in which the N-cyano group is centrally arranged in the molecule to allow for interactions with the nonprimed and primed binding regions of the target enzymes. These compounds were evaluated as inhibitors of the human cysteine cathepsins K, S, B, and L. They exhibited slow-binding behavior and were found to be exceptionally potent, in particular toward cathepsin K, with second-order rate constants up to 52 900 x 10(3) M-1 s(-1).

  DOI：

  10.1021/ml500238q

文献信息

• Aza-β^<i>3</i>-cyclotetrapeptides
  作者：Arnaud Salaün、Clémence Mocquet、Romain Perochon、Aurélien Lecorgne、Barbara Le Grel、Michel Potel、Philippe Le Grel

  DOI：10.1021/jo8013963

  日期：2008.11.7

  The cyclization of aza-beta(3)-tetrapeptides gives access to new CTP (cyclotetrapeptide) analogues. These stereocontrolled templates are assembled without any asymmetric synthesis. X-ray crystallographic structure and NMR analysis show that the macrocyclic scaffold is characterized by a fully cooperative intramolecular H-bond network, in sharp contrast with the nanotubular assemblies observed for beta(3)-cyclotetrapeptides. This folding property reduces considerably the polarity of aza-beta(3)-tetrapeptides and should be useful in addressing intracellular targets.
• Petasis boronic acid–Mannich reactions of substituted hydrazines: synthesis of α-hydrazinocarboxylic acids
  作者：David E. Portlock、Dinabandhu Naskar、Laura West、Min Li

  DOI：10.1016/s0040-4039(02)01511-3

  日期：2002.9

  N-1-(Carbamate protected)-N-2-(alkyl or aryl substituted) hydrazines can serve as amine substrates for the Petasis boronic acid-Mannich reaction, providing a practical synthetic route for the preparation of alpha-hydrazinocarboxylic acids. The scope and limitations of this method have been examined. (C) 2002 Published by Elsevier Science Ltd.
• 3-Cyano-3-aza-β-amino Acid Derivatives as Inhibitors of Human Cysteine Cathepsins
  作者：Janina Schmitz、Anna-Madeleine Beckmann、Adela Dudic、Tianwei Li、Robert Sellier、Ulrike Bartz、Michael Gütschow

  DOI：10.1021/ml500238q

  日期：2014.10.9

  Nitrile-type inhibitors are known to interact with cysteine proteases in a covalent-reversible manner. The chemotype of 3-cyano-3-aza-beta-amino acid derivatives was designed in which the N-cyano group is centrally arranged in the molecule to allow for interactions with the nonprimed and primed binding regions of the target enzymes. These compounds were evaluated as inhibitors of the human cysteine cathepsins K, S, B, and L. They exhibited slow-binding behavior and were found to be exceptionally potent, in particular toward cathepsin K, with second-order rate constants up to 52 900 x 10(3) M-1 s(-1).