tert-butyl 2-(((9H-fluoren-9-yl)methoxy)carbonylamino)-5-(2-(2,4-dinitrophenylamino)ethylamino)-5-oxopentanoate | 951312-87-1

• 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-(((9H-fluoren-9-yl)methoxy)carbonylamino)-5-(2-(2,4-dinitrophenylamino)ethylamino)-5-oxopentanoate
• 英文别名: tert-butyl (2S)-5-[2-(2,4-dinitroanilino)ethylamino]-2-(9H-fluoren-9-ylmethoxycarbonylamino)-5-oxopentanoate
• CAS: 951312-87-1
• 化学式: C₃₂H₃₅N₅O₉
• 分子量: 633.658
• InChiKey: ZZWXTSITLOYUBC-MHZLTWQESA-N

计算性质

• 辛醇/水分配系数(LogP)：
  5.5
• 重原子数：
  46
• 可旋转键数：
  14
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.34
• 拓扑面积：
  197
• 氢给体数：
  3
• 氢受体数：
  10

反应信息

• 作为反应物：
  描述：

  tert-butyl 2-(((9H-fluoren-9-yl)methoxy)carbonylamino)-5-(2-(2,4-dinitrophenylamino)ethylamino)-5-oxopentanoate 在 三氟乙酸 作用下， 以 二氯甲烷 为溶剂， 反应 5.0h， 以87%的产率得到2-(((9H-fluoren-9-yl)methoxy)carbonylamino)-5-(2-(2,4-dinitrophenylamino)ethylamino)-5-oxopentanoic acid
  参考文献：
  名称：

  Development of a FRET Assay for Monitoring of HIV gp41 Core Disruption

  摘要：

  The fusogenic core assembly of human immunodeficiency virus type 1 (HIV-1) fusion protein gp41 is a critical transformation for viral entry. Molecules that are able to intercept this process are of great therapeutic value as HIV-1 fusion inhibitors. In the search for such molecules, assay systems that can be adapted to high-throughput screens are valuable. Given that gp41 fusogenic transformation is characterized by the hexameric association of heptads located at the N and C terminal regions of the protein ectodomain, the corresponding heptad peptides (CHR and NHR), known to form the six-helix bundle core of gp41 fusion active form, are potentially useful in developing a fluorescence resonance energy transfer (FRET) system for identification of HIV fusion inhibitors. We demonstrate that by strategically placing two FRET probes on these two peptides, we are able to monitor the intermolecular co-association by fluorescence quenching between the fluorescence donor and acceptor. The utility of the system is that it should be adaptable to high-throughput screening (HTS) toward peptide or small-molecule HIV fusion inhibitors targeting the gp41 core. Herein, we report the design, synthesis, and development of a N- and C- terminal peptide FRET pair for screening of gp41 six-helix bundle disruption.

  DOI：

  10.1021/jo070836l
• 作为产物：
  描述：

  N1-(2,4-硝基苯基)-1,2-乙二胺 、 芴甲氧羰基-L-谷氨酸 1-叔丁酯 在 1-羟基苯并三唑 、 达卡巴嗪 作用下， 以 二甲基亚砜 、 N,N-二甲基甲酰胺 为溶剂， 反应 10.5h， 以96%的产率得到tert-butyl 2-(((9H-fluoren-9-yl)methoxy)carbonylamino)-5-(2-(2,4-dinitrophenylamino)ethylamino)-5-oxopentanoate
  参考文献：
  名称：

  Development of a FRET Assay for Monitoring of HIV gp41 Core Disruption

  摘要：

  The fusogenic core assembly of human immunodeficiency virus type 1 (HIV-1) fusion protein gp41 is a critical transformation for viral entry. Molecules that are able to intercept this process are of great therapeutic value as HIV-1 fusion inhibitors. In the search for such molecules, assay systems that can be adapted to high-throughput screens are valuable. Given that gp41 fusogenic transformation is characterized by the hexameric association of heptads located at the N and C terminal regions of the protein ectodomain, the corresponding heptad peptides (CHR and NHR), known to form the six-helix bundle core of gp41 fusion active form, are potentially useful in developing a fluorescence resonance energy transfer (FRET) system for identification of HIV fusion inhibitors. We demonstrate that by strategically placing two FRET probes on these two peptides, we are able to monitor the intermolecular co-association by fluorescence quenching between the fluorescence donor and acceptor. The utility of the system is that it should be adaptable to high-throughput screening (HTS) toward peptide or small-molecule HIV fusion inhibitors targeting the gp41 core. Herein, we report the design, synthesis, and development of a N- and C- terminal peptide FRET pair for screening of gp41 six-helix bundle disruption.

  DOI：

  10.1021/jo070836l

文献信息

• Development of a FRET Assay for Monitoring of HIV gp41 Core Disruption
  作者：Yang Xu、Mark S. Hixon、Philip E. Dawson、Kim D. Janda

  DOI：10.1021/jo070836l

  日期：2007.8.31

  The fusogenic core assembly of human immunodeficiency virus type 1 (HIV-1) fusion protein gp41 is a critical transformation for viral entry. Molecules that are able to intercept this process are of great therapeutic value as HIV-1 fusion inhibitors. In the search for such molecules, assay systems that can be adapted to high-throughput screens are valuable. Given that gp41 fusogenic transformation is characterized by the hexameric association of heptads located at the N and C terminal regions of the protein ectodomain, the corresponding heptad peptides (CHR and NHR), known to form the six-helix bundle core of gp41 fusion active form, are potentially useful in developing a fluorescence resonance energy transfer (FRET) system for identification of HIV fusion inhibitors. We demonstrate that by strategically placing two FRET probes on these two peptides, we are able to monitor the intermolecular co-association by fluorescence quenching between the fluorescence donor and acceptor. The utility of the system is that it should be adaptable to high-throughput screening (HTS) toward peptide or small-molecule HIV fusion inhibitors targeting the gp41 core. Herein, we report the design, synthesis, and development of a N- and C- terminal peptide FRET pair for screening of gp41 six-helix bundle disruption.