cis-3-indole acrylic acid | 29953-72-8

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 吲哚及其衍生物
• 英文名称: cis-3-indole acrylic acid
• 英文别名: Indoleacrylic acid；(Z)-3-(1H-indol-3-yl)prop-2-enoic acid
• CAS: 29953-72-8
• 化学式: C₁₁H₉NO₂
• 分子量: 187.198
• InChiKey: PLVPPLCLBIEYEA-WAYWQWQTSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.2
• 重原子数：
  14
• 可旋转键数：
  2
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.0
• 拓扑面积：
  53.1
• 氢给体数：
  2
• 氢受体数：
  2

反应信息

• 作为反应物：
  描述：

  Fmoc-D,L-Hcy(Trt)-OH 、 cis-3-indole acrylic acid 、 Fmoc-D-苯丙氨酸 生成 (2R)-2-[[2-[[(Z)-3-(1H-indol-3-yl)prop-2-enoyl]amino]-4-sulfanylbutanoyl]amino]-3-phenylpropanoic acid
  参考文献：
  名称：

  Homo-cysteinyl peptide inhibitors of the L1 metallo-β-lactamase, and SAR as determined by combinatorial library synthesis

  摘要：

  Homo-cysteinyl peptides were found to be more active than cysteinyl peptides toward L1 metallo-beta-lactamase as reversible competitive inhibitors. A combinatorial library of more than 90 homo-cysteinyl peptides was synthesized and screened for their inhibitory activity toward the L1 enzyme. A systematic structure-activity relationship analysis has revealed the preferred interaction groups for Ll conserved binding sites of beta-lactam substrates. The most active compound 95b, had a K-i of 2.1 nM. (c) 2006 Published by Elsevier Ltd.

  DOI：

  10.1016/j.bmcl.2006.07.001
• 作为产物：
  描述：

  反式吲哚-3-烯丙酸 以 乙酸乙酯 为溶剂， 反应 24.0h， 生成 cis-3-indole acrylic acid
  参考文献：
  名称：

  Photoinduced, Family-Specific, Site-Selective Cleavage of TIM-Barrel Proteins

  摘要：

  Nonenzymatic, chemical methods for the controlled cleavage of proteins at predictable sites in a site-specific manner are rare and of strong potential utility in clean, post-translational manipulation of protein structure for use in, for example, proteomics, sequencing, and tagged-protein production. Unprecedented photochemical, site-selective cleavage of a His-Trp (HW) motif in the GH1 family TIM-barrel proteins is observed upon exposure to 240-308 nm light to cleanly release N-terminal primary amide and C-terminal indolylenamide fragments. We also show that this photocleaveable motif can be transferred to fusion proteins for use in photoresponsive affinty purification. The presence of this motif in proteins found only in organisms that are not typically exposed to tight raises the possibility of direct biological relevance for this new type of protein reaction.

  DOI：

  10.1021/ja9026105

文献信息

• Photoinduced, Family-Specific, Site-Selective Cleavage of TIM-Barrel Proteins
  作者：Nicola Floyd、Neil J. Oldham、Christopher J. Eyles、Stephen Taylor、Dmitry A. Filatov、Mark Brouard、Benjamin G. Davis

  DOI：10.1021/ja9026105

  日期：2009.9.9

  Nonenzymatic, chemical methods for the controlled cleavage of proteins at predictable sites in a site-specific manner are rare and of strong potential utility in clean, post-translational manipulation of protein structure for use in, for example, proteomics, sequencing, and tagged-protein production. Unprecedented photochemical, site-selective cleavage of a His-Trp (HW) motif in the GH1 family TIM-barrel proteins is observed upon exposure to 240-308 nm light to cleanly release N-terminal primary amide and C-terminal indolylenamide fragments. We also show that this photocleaveable motif can be transferred to fusion proteins for use in photoresponsive affinty purification. The presence of this motif in proteins found only in organisms that are not typically exposed to tight raises the possibility of direct biological relevance for this new type of protein reaction.
• Homo-cysteinyl peptide inhibitors of the L1 metallo-β-lactamase, and SAR as determined by combinatorial library synthesis
  作者：Qin Sun、Andy Law、Michael W. Crowder、H. Mario Geysen

  DOI：10.1016/j.bmcl.2006.07.001

  日期：2006.10

  Homo-cysteinyl peptides were found to be more active than cysteinyl peptides toward L1 metallo-beta-lactamase as reversible competitive inhibitors. A combinatorial library of more than 90 homo-cysteinyl peptides was synthesized and screened for their inhibitory activity toward the L1 enzyme. A systematic structure-activity relationship analysis has revealed the preferred interaction groups for Ll conserved binding sites of beta-lactam substrates. The most active compound 95b, had a K-i of 2.1 nM. (c) 2006 Published by Elsevier Ltd.