{4-[2-(1H-Indol-3-yl)-ethylcarbamoyl]-butyl}-carbamic acid tert-butyl ester | 177949-38-1

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 吲哚及其衍生物
• 英文名称: {4-[2-(1H-Indol-3-yl)-ethylcarbamoyl]-butyl}-carbamic acid tert-butyl ester
• CAS: 177949-38-1
• 化学式: C₂₀H₂₉N₃O₃
• 分子量: 359.469
• InChiKey: NDCVCJPBUMLIGE-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.52
• 重原子数：
  26.0
• 可旋转键数：
  8.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.5
• 拓扑面积：
  83.22
• 氢给体数：
  3.0
• 氢受体数：
  3.0

反应信息

• 作为反应物：
  描述：

  {4-[2-(1H-Indol-3-yl)-ethylcarbamoyl]-butyl}-carbamic acid tert-butyl ester 在 4-二甲氨基吡啶 、 三乙胺 、 三氟乙酸 作用下， 以 二氯甲烷 、 N,N-二甲基甲酰胺 为溶剂， 反应 25.0h， 生成 N-(2-(1-acetyl-1H-indol-3-yl)ethyl)-5-aminopentanamide
  参考文献：
  名称：

  Development of cyclic peptomer inhibitors targeting the polo-box domain of polo-like kinase 1

  摘要：

  The polo-box domain (PBD) of polo-like kinase 1 (Plk1) is essentially required for the function of Plk1 in cell proliferation. The availability of the phosphopeptide-binding pocket on PBD provides a unique opportunity to develop novel protein-protein interaction inhibitors. Recent identification of a minimal 5-residue-long phosphopeptide, PLHSpT, as a Plk1 PBD-specific ligand has led to the development of several peptide-based inhibitors, but none of them is cyclic peptide. Through the combination of single-peptoid mimics and thio-ether bridged cyclization, we successfully demonstrated for the first time two cyclic peptomers, PL-116 and PL-120, dramatically improved the binding affinity without losing mono-specificity against Plk1 PBD in comparison with the linear parental peptide, PLHSpT. These cyclic peptomers could serve as promising templates for future drug designs to inhibit Plk1 PBD. (C) 2013 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2013.02.020
• 作为产物：
  描述：

  色胺 、 Boc-5-氨基戊酸 在 N,N'-二环己基碳二亚胺 作用下， 以 二氯甲烷 为溶剂， 反应 0.17h， 以99%的产率得到{4-[2-(1H-Indol-3-yl)-ethylcarbamoyl]-butyl}-carbamic acid tert-butyl ester
  参考文献：
  名称：

  Development of cyclic peptomer inhibitors targeting the polo-box domain of polo-like kinase 1

  摘要：

  The polo-box domain (PBD) of polo-like kinase 1 (Plk1) is essentially required for the function of Plk1 in cell proliferation. The availability of the phosphopeptide-binding pocket on PBD provides a unique opportunity to develop novel protein-protein interaction inhibitors. Recent identification of a minimal 5-residue-long phosphopeptide, PLHSpT, as a Plk1 PBD-specific ligand has led to the development of several peptide-based inhibitors, but none of them is cyclic peptide. Through the combination of single-peptoid mimics and thio-ether bridged cyclization, we successfully demonstrated for the first time two cyclic peptomers, PL-116 and PL-120, dramatically improved the binding affinity without losing mono-specificity against Plk1 PBD in comparison with the linear parental peptide, PLHSpT. These cyclic peptomers could serve as promising templates for future drug designs to inhibit Plk1 PBD. (C) 2013 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2013.02.020

文献信息

• Enzyme catalysed oxidation of nazlinin and nazlinin derivatives. Characterisation of the reaction products
  作者：Elisabeth Cheng、Jens Botzem、Martin J. Wanner、Brigitte E.A. Burm、Gerrit-Jan Koomen

  DOI：10.1016/0040-4020(96)00286-4

  日期：1996.5

  catalyse the oxidative transformation of Nitraria alkaloids. Nazlinin yielded indoloquinolizidine 4, an alkaloid which has been obtained as a natural product from Nitraria plant extracts. Oxidative deamination of 1-(4-butylamino)-β-carboline 10 with PKDO yielded an unstable aldehyde (11), which cyclised to a new, arborescidine-type azepine (12). Addition of alcohol dehydrogenase during the oxidative deamination

  猪肾脏二胺氧化酶（PKDO）被用来催化白屈菜生物碱的氧化转化。Nazlinin产生吲哚并喹喔啉4，这是一种生物碱，是从Nitraria植物提取物中得到的天然产物。1-（4-丁基氨基）-β-咔啉10用PKDO进行氧化脱氨基反应生成不稳定的醛（11），然后将其环化为新的阿波西啶型氮杂环庚烷（12）。在氧化脱氨过程中添加醇脱氢酶可将醛原位还原为相应的醇13。托帕醌类似物9这些伯胺作为化学计量的氧化剂有效。通过与化学合成的化合物进行比较来表征酶反应产物。