(S)-2-Iodomethyl-4-isobutyl-5-methyl-1,1-dioxo-1λ6-[1,2,5]thiadiazolidin-3-one | 170919-17-2

• 分子结构分类: 有机化合物 - 有机杂环化合物
• 英文名称: (S)-2-Iodomethyl-4-isobutyl-5-methyl-1,1-dioxo-1λ6-[1,2,5]thiadiazolidin-3-one
• CAS: 170919-17-2
• 化学式: C₈H₁₅IN₂O₃S
• 分子量: 346.189
• InChiKey: YABMOEVBRJXXAN-ZETCQYMHSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.81
• 重原子数：
  15.0
• 可旋转键数：
  3.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.88
• 拓扑面积：
  57.69
• 氢给体数：
  0.0
• 氢受体数：
  3.0

反应信息

• 作为反应物：
  描述：

  阿司匹林 、 (S)-2-Iodomethyl-4-isobutyl-5-methyl-1,1-dioxo-1λ6-[1,2,5]thiadiazolidin-3-one 在 1,8-二氮杂双环[5.4.0]十一碳-7-烯 作用下， 以 二氯甲烷 为溶剂， 以70%的产率得到[(4S)-5-methyl-4-(2-methylpropyl)-1,1,3-trioxo-1,2,5-thiadiazolidin-2-yl]methyl 2-acetyloxybenzoate
  参考文献：
  名称：

  Effects of structure on inhibitory activity in a series of mechanism-based inhibitors of human neutrophil elastase

  摘要：

  A structurally-diverse series of carboxylate derivatives based on the 1,2,5-thiadiazolidin-one 1,1 dioxide scaffold were synthesized and used to probe the S' subsites of human neutrophil elastase (HNE) and neutrophil proteinase 3 (Pr 3). Several compounds are potent inhibitors of HNE but devoid of inhibitory activity toward Pr 3, suggesting that the S' subsites of HNE exhibit significant plasticity and can, unlike Pr 3, tolerate various large hydrophobic groups. The results provide a promising framework for the design of highly selective inhibitors of the two enzymes. (c) 2010 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2010.07.071
• 作为产物：
  描述：

  (S)-2-Chloromethyl-4-isobutyl-5-methyl-1,1-dioxo-1λ6-[1,2,5]thiadiazolidin-3-one 在 sodium iodide 作用下， 以 丙酮 为溶剂， 生成 (S)-2-Iodomethyl-4-isobutyl-5-methyl-1,1-dioxo-1λ6-[1,2,5]thiadiazolidin-3-one
  参考文献：
  名称：

  Inhibition of serine proteases by functionalized sulfonamides coupled to the 1,2,5-thiadiazolidin-3-one 1,1 dioxide scaffold

  摘要：

  A challenge associated with drug design is the development of selective inhibitors of proteases (serine or cysteine) that exhibit the same primary substrate specificity, that is, show a preference for the same P-1 residue. While these proteases have similar active sites, nevertheless there are subtle differences in their S and S' subsites which can be exploited. We describe herein for the first time the use of functionalized sulfonamides as a design and diversity element which, when coupled to the 1,2,5-thiadiazolidin-3-one 1,1 dioxide scaffold yields potent, time-dependent inhibitors of the serine proteases human leukocyte elastase (HLE), proteinase 3 (PR 3) and cathepsin G(Cat G). Our preliminary findings suggest that (a) appending to the 1,2,5-thiadiazolidin-3-one 1,1 dioxide scaffold recognition and diversity elements that interact with both the S and S' subsites of a target protease may result in optimal enzyme selectivity and potency and, (b) functionalized sulfonamides constitute a powerful design and diversity element with low intrinsic chemical reactivity and potentially wide applicability (C) 2001 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0968-0896(01)00037-2