94G7 | 1220690-27-6

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯酚醚
• 英文名称: 94G7
• 英文别名: 3-Hydroxy-1-[2-(3-methoxyphenyl)ethyl]-2-methylpyridine-4-thione
• CAS: 1220690-27-6
• 化学式: C₁₅H₁₇NO₂S
• 分子量: 275.371
• InChiKey: OAJXGDFLUJGMMI-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3
• 重原子数：
  19
• 可旋转键数：
  4
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.27
• 拓扑面积：
  64.8
• 氢给体数：
  1
• 氢受体数：
  4

反应信息

• 作为产物：
  描述：

  3-hydroxy-2-methylpyran-4(1H)-thione 、 3-甲氧基苯乙胺 在 盐酸 作用下， 以 水 为溶剂， 165.0 ℃ 、1.72 MPa 条件下， 反应 0.03h， 生成 94G7
  参考文献：
  名称：

  用于靶向金属蛋白酶的螯合剂片段文库

  摘要：

  针对金属蛋白酶筛选基于多种金属结合基团的螯合剂片段文库。确定了先导命中并合成了一个扩展的选定化合物库，从而产生了针对几个金属蛋白靶标的大量高亲和力命中。研究结果清楚地表明，螯合剂可用于生成适用于针对重要金属蛋白的基于片段的先导设计 (FBLD) 的文库。

  DOI：

  10.1002/cmdc.200900516

文献信息

• Chelator Fragment Libraries for Targeting Metalloproteinases
  作者：Arpita Agrawal、Sherida L. Johnson、Jennifer A. Jacobsen、Melissa T. Miller、Li-Hsing Chen、Maurizio Pellecchia、Seth M. Cohen

  DOI：10.1002/cmdc.200900516

  日期：2010.2.1

  A chelator fragment library based on a variety of metal binding groups was screened against a metalloproteinase. Lead hits were identified and an expanded library of select compounds was synthesized, resulting in numerous high‐affinity hits against several metalloprotein targets. The findings clearly demonstrate that chelators can be used to generate libraries suitable for fragment‐based lead design

  针对金属蛋白酶筛选基于多种金属结合基团的螯合剂片段文库。确定了先导命中并合成了一个扩展的选定化合物库，从而产生了针对几个金属蛋白靶标的大量高亲和力命中。研究结果清楚地表明，螯合剂可用于生成适用于针对重要金属蛋白的基于片段的先导设计 (FBLD) 的文库。
• Development of a High-Throughput Screen and Its Use in the Discovery of <i>Streptococcus pneumoniae</i> Immunoglobulin A1 Protease Inhibitors
  作者：Amanda L. Garner、Jessica L. Fullagar、Joshua A. Day、Seth M. Cohen、Kim D. Janda

  DOI：10.1021/ja404180x

  日期：2013.7.10

  Streptococcus pneumoniae relies on a number of virulence factors, including immunoglobulin A1 protease (IgA1P), a Zn2+ metalloprotease produced on the extracellular surface of the bacteria, to promote pathogenic colonization. IgA1P exhibits a unique function, in that it catalyzes the proteolysis of human IgA1 at its hinge region to leave the bacterial cell surface masked by IgA1 Fab, enabling the bacteria to evade the hosts immune system and adhere to host epithelial cells to promote colonization. Thus, S. pneumoniae IgA1P has emerged as a promising antibacterial target; however, the lack of an appropriate screening assay has limited the investigation of this metalloprotease virulence factor. Relying on electrostatics-mediated AuNP aggregation, we have designed a promising high-throughput colorimetric assay for IgA1P. By using this assay, we have uncovered inhibitors of the enzyme that should be useful in deciphering its role in pneumococcal colonization and virulence.