DAz-1 | 1112977-84-0

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: DAz-1
• 英文别名: N-(3-azidopropyl)-3,5-dioxocyclohexane-1-carboxamide
• CAS: 1112977-84-0
• 化学式: C₁₀H₁₄N₄O₃
• 分子量: 238.246
• InChiKey: ZMZUOTZOCOMDDO-UHFFFAOYSA-N

物化性质

• 溶解度：
  DMF：可混溶； DMSO：可混溶；乙醇：可混溶； PBS（pH 7.2）：20 mg/ml

计算性质

• 辛醇/水分配系数(LogP)：
  0.2
• 重原子数：
  17
• 可旋转键数：
  5
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.7
• 拓扑面积：
  77.6
• 氢给体数：
  1
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  DAz-1 、 CSA 以 aq. phosphate buffer 、 乙腈 为溶剂， 生成
  参考文献：
  名称：

  Profiling the reactivity of cyclic C-nucleophiles towards electrophilic sulfur in cysteine sulfenic acid

  摘要：

  蛋白质半胱氨酸硫醇氧化为硫酸基，称为S-硫酰基化，是一种可逆的翻译后修饰，对调节蛋白质功能起着至关重要的作用，并与疾病状态相关。

  DOI：

  10.1039/c5sc02569a
• 作为产物：
  描述：

  3-methoxy-5-oxo-cyclohex-3-ene-1-carboxylic acid 在 盐酸 、 水 、 O-(benzotriazol-1-yl)-N,N,N',N'-tetramethyluronium tetrafluoroborate 、 N,N-二异丙基乙胺 作用下， 以 四氢呋喃 、 N,N-二甲基甲酰胺 为溶剂， 反应 1.25h， 生成 DAz-1
  参考文献：
  名称：

  Facile synthesis and biological evaluation of a cell-permeable probe to detect redox-regulated proteins

  摘要：

  We have developed an improved synthesis for the cell-permeable, sulfenic acid probe DAz-1. Using DAz-1, we detect sulfenic acid modi. cations in the cell-cycle regulatory phosphatase Cdc25A. In addition, we show that DAz-1 has superior potency in cells compared to a biotinylated derivative. Collectively, these. findings set the stage for the development of activity-based inhibitors of Cdc25 cell-cycle phosphatases, which are sensitive to the redox state of the active-site cysteine and demonstrate the advantage of bioorthogonal conjugation methods to detect protein sulfenic acids in cells. (C) 2008 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2008.11.073

文献信息

• Profiling the reactivity of cyclic C-nucleophiles towards electrophilic sulfur in cysteine sulfenic acid
  作者：Vinayak Gupta、Kate S. Carroll

  DOI：10.1039/c5sc02569a

  日期：——

  Oxidation of a protein cysteine thiol to sulfenic acid, termedS-sulfenylation, is a reversible post-translational modification that plays a crucial role in regulating protein function and is correlated with disease states.

  蛋白质半胱氨酸硫醇氧化为硫酸基，称为S-硫酰基化，是一种可逆的翻译后修饰，对调节蛋白质功能起着至关重要的作用，并与疾病状态相关。
• Targeted Covalent Probes and Inhibitors of Proteins Containing Redox-Sensitive Cysteines
  申请人：THE SCRIPPS RESEARCH INSTITUTE

  公开号：US20160195532A1

  公开（公告）日：2016-07-07

  Covalent, irreversible small-molecule inhibitors that modify the sulfenyl form (i.e., sulfenic acid, RSOH and sulfenamide, RSNR′2) of therapeutically important proteins (particularly kinases and phosphatases) are disclosed, where the compositions include a compound having a substituted aryl or heterocyclic core structure that promotes binding interactions with a specific protein, and a nucleophilic reaction center (carbon, nitrogen, sulfur, or phosphorous) that is capable of forming a covalent bond with a sulfenic acid- or sulfenamide-modified cysteine residue in the protein. Methods for synthesizing these compounds are also disclosed, as well as methods of using them for determining the bioactivity of a chemical composition comprising an active compound toward a specific protein and for determining the potency of an inhibitor against a specific protein.
• US9977024B2
  申请人：——

  公开号：US9977024B2

  公开（公告）日：2018-05-22
• Facile synthesis and biological evaluation of a cell-permeable probe to detect redox-regulated proteins
  作者：Young Ho Seo、Kate S. Carroll

  DOI：10.1016/j.bmcl.2008.11.073

  日期：2009.1

  We have developed an improved synthesis for the cell-permeable, sulfenic acid probe DAz-1. Using DAz-1, we detect sulfenic acid modi. cations in the cell-cycle regulatory phosphatase Cdc25A. In addition, we show that DAz-1 has superior potency in cells compared to a biotinylated derivative. Collectively, these. findings set the stage for the development of activity-based inhibitors of Cdc25 cell-cycle phosphatases, which are sensitive to the redox state of the active-site cysteine and demonstrate the advantage of bioorthogonal conjugation methods to detect protein sulfenic acids in cells. (C) 2008 Elsevier Ltd. All rights reserved.