2-(4-methoxyphenylsulfonyl)-4-oxo-4-(trityloxyamino)butanoic acid | 913987-16-3

• 分子结构分类: 有机化合物 - 苯类化合物 - 三苯基化合物
• 英文名称: 2-(4-methoxyphenylsulfonyl)-4-oxo-4-(trityloxyamino)butanoic acid
• CAS: 913987-16-3
• 化学式: C₃₀H₂₇NO₇S
• 分子量: 545.613
• InChiKey: DDBCESJUAACXSO-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.35
• 重原子数：
  39.0
• 可旋转键数：
  11.0
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.13
• 拓扑面积：
  119.0
• 氢给体数：
  2.0
• 氢受体数：
  6.0

反应信息

• 作为反应物：
  描述：

  2-(4-methoxyphenylsulfonyl)-4-oxo-4-(trityloxyamino)butanoic acid 、 炔丙胺 在 N,N-二异丙基乙胺 、 N-[(dimethylamino)-3-oxo-1H-1,2,3-triazolo[4,5-b]pyridin-1-yl-methylene]-N-methylmethanaminium hexafluorophosphate 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 以75%的产率得到2-(4-methoxyphenylsulfonyl)-N¹-(prop-2-ynyl)-N⁴-(trityloxy)succinamide
  参考文献：
  名称：

  “Click” synthesis of small molecule probes for activity-based fingerprinting of matrix metalloproteases

  摘要：

  通过使用“点击化学”，我们实现了多种基于亲和性的羟胺探针的简便合成，这些探针能够在蛋白组学实验中生成多种金属蛋白酶（包括基质金属蛋白酶MMPs）的活性指纹。

  DOI：

  10.1039/b609446e
• 作为产物：
  描述：

  4-(benzyloxy)-2-(4-methoxyphenylsulfonyl)-4-oxobutanoic acid 在 palladium on activated charcoal 哌啶 、 4-二甲氨基吡啶 、 氢气 、 N,N'-二环己基碳二亚胺 作用下， 以 四氢呋喃 、 二氯甲烷 、 N,N-二甲基甲酰胺 为溶剂， 反应 1.75h， 生成 2-(4-methoxyphenylsulfonyl)-4-oxo-4-(trityloxyamino)butanoic acid
  参考文献：
  名称：

  “Click” synthesis of small molecule probes for activity-based fingerprinting of matrix metalloproteases

  摘要：

  通过使用“点击化学”，我们实现了多种基于亲和性的羟胺探针的简便合成，这些探针能够在蛋白组学实验中生成多种金属蛋白酶（包括基质金属蛋白酶MMPs）的活性指纹。

  DOI：

  10.1039/b609446e

文献信息

• Quantitative Inhibitor Fingerprinting of Metalloproteases Using Small Molecule Microarrays
  作者：Mahesh Uttamchandani、Wei L. Lee、Jun Wang、Shao Q. Yao

  DOI：10.1021/ja073914v

  日期：2007.10.1

  Current methods to identify interactions on small molecule microarrays (SIMMs) introduce false positives that are difficult to dissect from the "real" binding events without tedious downstream re-evaluation. To specifically elucidate only activity-dependent ligand binding interactions, we have developed a technique that can be universally applied to present SMM systems. Our method makes use of a dual-color application strategy and is based on the simultaneous application of differentially treated samples. Overcoming the limitations of slide-to-slide variation, this method directly revealed activity-dependent interactions through a one-step application of protein samples on SMMs. Besides providing lead molecules for further development, the high-throughput screening results confer activity-dependent fingerprints for quantitative characterization and differentiation of proteins. The procedure was tested using a synthetic hydroxamate peptide library with 1400 discrete sequences permuted combinatorially across P1', P2', and P3' positions. Functional profiling across a panel of metalloproteases provided 44 800 datapoints within just eight SMM slides. These data were globally analyzed for activities, specificity, potency, and hierarchical clustering providing unique insights into inhibitor design and preference within this group of enzymes. Quantitative KID measurements performed on SMMs using one of the enzymes in the panel, Anthrax Lethal Factor, the toxic component of a notorious bioterror agent, unraveled several lead micromolar binders for further development. Overall, the effectiveness of the SMM platform is shown to be enhanced and extended using the strategy presented in this work.