Ac-Asp(O-t-Bu)-Glu(O-t-Bu)-Val-OH | 263859-12-7

• 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: Ac-Asp(O-t-Bu)-Glu(O-t-Bu)-Val-OH
• 英文别名: Ac-Asp(OtBu)(OtBu)-Glu(OtBu)(OtBu)-Val-OH；(2S)-2-[[(2S)-2-[[(2S)-2-acetamido-4-[(2-methylpropan-2-yl)oxy]-4-oxobutanoyl]amino]-5-[(2-methylpropan-2-yl)oxy]-5-oxopentanoyl]amino]-3-methylbutanoic acid
• CAS: 263859-12-7
• 化学式: C₂₄H₄₁N₃O₉
• 分子量: 515.604
• InChiKey: UVEGRNFDMKIGNV-BXWFABGCSA-N

物化性质

• 沸点：
  779.0±60.0 °C(Predicted)
• 密度：
  1.156±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  1.2
• 重原子数：
  36
• 可旋转键数：
  16
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.75
• 拓扑面积：
  177
• 氢给体数：
  4
• 氢受体数：
  9

反应信息

• 作为反应物：
  描述：

  Ac-Asp(O-t-Bu)-Glu(O-t-Bu)-Val-OH 在 benzotriazol-1-yloxyl-tris-(pyrrolidino)-phosphonium hexafluorophosphate 、 N,N-二异丙基乙胺 、 三氟乙酸 作用下， 以 二氯甲烷 为溶剂， 反应 2.17h， 生成 (S)-3-{(S)-2-[(S)-2-((S)-2-Acetylamino-3-carboxy-propionylamino)-4-carboxy-butyrylamino]-3-methyl-butyrylamino}-4-cyclopropyl-4-oxo-butyric acid
  参考文献：
  名称：

  Using Peptidic Inhibitors to Systematically Probe the S1‘ Site of Caspase-3 and Caspase-7

  摘要：

  Fifteen ketone-containing peptides were designed, synthesized, and used to probe the effect of substitution at the P1' position on caspase-3 and -7 inhibition. Even with the large bias of Ac-Asp-Glu-Val-Asp at the P4-P1 positions, certain peptides with cyclic functionality in the P1' position show a dramatically reduced ability to inhibit these caspases. Additionally, trends toward isozyme selectivity were also uncovered for particular P1' substituents. The data indicate that substitution in the P1' position can drastically affect both caspase inhibition and selectivity.

  DOI：

  10.1021/ol051287d
• 作为产物：
  描述：

  L-天门冬氨酸-4-叔丁基酯 在 吗啉 、 四(三苯基膦)钯 、 benzotriazol-1-yloxyl-tris-(pyrrolidino)-phosphonium hexafluorophosphate 、 N,N-二异丙基乙胺 作用下， 以 四氢呋喃 、 二氯甲烷 为溶剂， 反应 16.33h， 生成 Ac-Asp(O-t-Bu)-Glu(O-t-Bu)-Val-OH
  参考文献：
  名称：

  Using Peptidic Inhibitors to Systematically Probe the S1‘ Site of Caspase-3 and Caspase-7

  摘要：

  Fifteen ketone-containing peptides were designed, synthesized, and used to probe the effect of substitution at the P1' position on caspase-3 and -7 inhibition. Even with the large bias of Ac-Asp-Glu-Val-Asp at the P4-P1 positions, certain peptides with cyclic functionality in the P1' position show a dramatically reduced ability to inhibit these caspases. Additionally, trends toward isozyme selectivity were also uncovered for particular P1' substituents. The data indicate that substitution in the P1' position can drastically affect both caspase inhibition and selectivity.

  DOI：

  10.1021/ol051287d

文献信息

• Cell-Permeable [^99mTc(CO₃)]-Labeled Fluorogenic Caspase 3 Substrate for Dual-Modality Detection of Apoptosis
  作者：Chiyi Xiong、Wei Lu、Rui Zhang、Mei Tian、William Tong、Juri Gelovani、Chun Li

  DOI：10.1002/chem.200900766

  日期：2009.9.14

  To image apoptosis in vivo, a small, membrane‐permeable probe comprising a caspase 3 substrate, a fluorogenic dye, and a radionuclide was synthesized (see scheme). This dual‐modality probe was specifically cleaved by caspase 3 upon exposure to apoptotic cells, allowing the imaging of caspase 3 activities (see figure) and apoptosis by using both optical and nuclear imaging techniques.

  为了在体内对细胞凋亡进行成像，合成了一种包含半胱天冬酶 3 底物、荧光染料和放射性核素的小型透膜探针（参见方案）。这种双模态探针在暴露于凋亡细胞时被 caspase 3 特异性切割，从而允许使用光学和核成像技术对 caspase 3 活性（见图）和细胞凋亡进行成像。
• N-DEVD-N′-morpholinecarbonyl-rhodamine 110: novel caspase-3 fluorogenic substrates for cell-based apoptosis assay
  作者：Zhi-Qiang Wang、Jinfang Liao、Zhenjun Diwu

  DOI：10.1016/j.bmcl.2005.02.081

  日期：2005.5

  A novel caspase-3 substrate N-Ac-DEVD-N'-MC-R110, which is a fluorogenic substrate cleavable in a single step, has been prepared. It has a significantly higher enzyme turnover rate and sensitivity for detecting caspase-3 activity both in solution and living cells than existing fluorogenic substrates. (c) 2005 Elsevier Ltd. All rights reserved.
• Using Peptidic Inhibitors to Systematically Probe the S1‘ Site of Caspase-3 and Caspase-7
  作者：David R. Goode、Anil K. Sharma、Paul J. Hergenrother

  DOI：10.1021/ol051287d

  日期：2005.8.1

  Fifteen ketone-containing peptides were designed, synthesized, and used to probe the effect of substitution at the P1' position on caspase-3 and -7 inhibition. Even with the large bias of Ac-Asp-Glu-Val-Asp at the P4-P1 positions, certain peptides with cyclic functionality in the P1' position show a dramatically reduced ability to inhibit these caspases. Additionally, trends toward isozyme selectivity were also uncovered for particular P1' substituents. The data indicate that substitution in the P1' position can drastically affect both caspase inhibition and selectivity.