2-(4-hydroxy-3-nitrophenyl)acetonitrile

• 分子结构分类: 有机化合物 - 苯类化合物 - 酚类
• 英文名称: 2-(4-hydroxy-3-nitrophenyl)acetonitrile
• 英文别名: 4-Hydroxy-3-nitrophenylacetonitrile
• 化学式: C₈H₆N₂O₃
• 分子量: 178.147
• InChiKey: AQYHTKGDJSKVFT-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.7
• 重原子数：
  13
• 可旋转键数：
  1
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.12
• 拓扑面积：
  89.8
• 氢给体数：
  1
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  2-(4-hydroxy-3-nitrophenyl)acetonitrile 生成 2-(3-Amino-4-hydroxyphenyl)acetonitrile
  参考文献：
  名称：

  YAMANEH, TAKEHXIKO;KONDO, XIDEHO;FUSEH, IOXIDEH;XASIDZUMEH;KANO, FUMIXIKO+

  摘要：

  DOI：
• 作为产物：
  描述：

  对羟基苯乙腈 在 硫酸 、 硝酸 作用下， 以 二氯甲烷 为溶剂， 以96%的产率得到2-(4-hydroxy-3-nitrophenyl)acetonitrile
  参考文献：
  名称：

  Discovery and Optimization of Salicylic Acid-Derived Sulfonamide Inhibitors of the WD Repeat-Containing Protein 5–MYC Protein–Protein Interaction

  摘要：

  The treatment of tumors driven by overexpression or amplification of MYC oncogenes remains a significant challenge in drug discovery. Here, we present a new strategy toward the inhibition of MYC via the disruption of the protein-protein interaction between MYC and its chromatin cofactor WD Repeat-Containing Protein 5. Blocking the association of these proteins is hypothesized to disrupt the localization of MYC to chromatin, thus disrupting the ability of MYC to sustain tumorigenesis. Utilizing a high-throughput screening campaign and subsequent structure-guided design, we identify small-molecule inhibitors of this interaction with potent in vitro binding affinity and report structurally related negative controls that can be used to study the effect of this disruption. Our work suggests that disruption of this protein-protein interaction may provide a path toward an effective approach for the treatment of multiple tumors and anticipate that the molecules disclosed can be used as starting points for future efforts toward compounds with improved drug-like properties.

  DOI：

  10.1021/acs.jmedchem.9b01411

文献信息

• Remarkable Chichibabin-type cyclotrimerisation of 3-nitrotyrosine, tyrosine and phenylalanine to 3,5-diphenylpyridine derivatives induced by hypochlorous acid
  作者：L. Panzella、P. Di Donato、S. Comes、A. Napolitano、A. Palumbo、M. d’Ischia

  DOI：10.1016/j.tetlet.2005.07.106

  日期：2005.9

  Reaction of 3-nitrotyrosine with HOCl in aqueous phosphate buffer (pH 7.4) leads to a mixture of extractable products, including 3,5-di(4-hydroxy-3-nitrophenyl)pyridine (15% isolated yield) and 3,5-di(4-hydroxy-3-nitrophenyl)-2-(4-hydroxy-3-nitrophenylmethyl)pyridine (3%) arising by a Chichibabin-like pyridine synthesis via N-chloroimine intermediates. Under the same conditions, phenylalanine gives 3,5-diphenylpyridine in 9% isolated yield, while tyrosine leads to 3,5-di(4-hydroxyphenyl)pyridine (3%) and 3-(3-chloro-4-hydroxyphenyl)-5-(4-hydroxyphenyl)pyridine (3%). (c) 2005 Elsevier Ltd. All rights reserved.
• YAMANEH, TAKEHXIKO;KONDO, XIDEHO;FUSEH, IOXIDEH;XASIDZUMEH;KANO, FUMIXIKO+
  作者：YAMANEH, TAKEHXIKO、KONDO, XIDEHO、FUSEH, IOXIDEH、XASIDZUMEH、KANO, FUMIXIKO+

  DOI：——

  日期：——
• US4016193A
  申请人：——

  公开号：US4016193A

  公开（公告）日：1977-04-05
• Discovery and Optimization of Salicylic Acid-Derived Sulfonamide Inhibitors of the WD Repeat-Containing Protein 5–MYC Protein–Protein Interaction
  作者：Jonathan D. Macdonald、Selena Chacón Simon、Changho Han、Feng Wang、J. Grace Shaw、Jennifer E. Howes、Jiqing Sai、Joannes P. Yuh、Demarco Camper、Bethany M. Alicie、Joseph Alvarado、Sameer Nikhar、William Payne、Erin R. Aho、Joshua A. Bauer、Bin Zhao、Jason Phan、Lance R. Thomas、Olivia W. Rossanese、William P. Tansey、Alex G. Waterson、Shaun R. Stauffer、Stephen W. Fesik

  DOI：10.1021/acs.jmedchem.9b01411

  日期：2019.12.26

  The treatment of tumors driven by overexpression or amplification of MYC oncogenes remains a significant challenge in drug discovery. Here, we present a new strategy toward the inhibition of MYC via the disruption of the protein-protein interaction between MYC and its chromatin cofactor WD Repeat-Containing Protein 5. Blocking the association of these proteins is hypothesized to disrupt the localization of MYC to chromatin, thus disrupting the ability of MYC to sustain tumorigenesis. Utilizing a high-throughput screening campaign and subsequent structure-guided design, we identify small-molecule inhibitors of this interaction with potent in vitro binding affinity and report structurally related negative controls that can be used to study the effect of this disruption. Our work suggests that disruption of this protein-protein interaction may provide a path toward an effective approach for the treatment of multiple tumors and anticipate that the molecules disclosed can be used as starting points for future efforts toward compounds with improved drug-like properties.