bis[2-(isobutylamino)ethyl]carbamic acid tert-butyl ester | 1076203-18-3

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: bis[2-(isobutylamino)ethyl]carbamic acid tert-butyl ester
• CAS: 1076203-18-3
• 化学式: C₁₇H₃₇N₃O₂
• 分子量: 315.5
• InChiKey: KCYSZRIQXBGODC-UHFFFAOYSA-N

反应信息

• 作为反应物：
  描述：

  bis[2-(isobutylamino)ethyl]carbamic acid tert-butyl ester 、 对硝基苯磺酰氯 在 三乙胺 作用下， 以 二氯甲烷 为溶剂， 反应 12.0h， 以80%的产率得到bis{2-[isobutyl(4-nitrobenzenesulfonyl)amino]ethyl}carbamic acid tert-butyl ester
  参考文献：
  名称：

  Achiral oligoamines as versatile tool for the development of aspartic protease inhibitors

  摘要：

  Due to the important role that aspartic proteases play in many patho-physiological processes, they have intensively been targeted by modern drug development. However, up to now, only for two family members, renin and HIV protease, approved drugs are available. Inhibitor development, mostly guided by mimicking the natural peptide substrates, resulted in very potent inhibitors for several targets, but the pharmacokinetic properties of these compounds were often not optimal. Herein we report a novel approach for lead structure discovery of non-peptidic aspartic protease inhibitors using easily accessible achiral linear oligoamines as starting point. An initial library comprising 11 inhibitors was developed and screened against six selected aspartic proteases. Several hits could be identified, among them selective as well as rather promiscuous inhibitors. The design concept was confirmed by determination of the crystal structure of two derivatives in complex with the HIV-1 protease, and represents a promising basis for the further inhibitor development. (C) 2008 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2008.08.012
• 作为产物：
  描述：

  在 sodium tetrahydroborate 作用下， 以 甲醇 为溶剂， 反应 2.0h， 以346 mg的产率得到bis[2-(isobutylamino)ethyl]carbamic acid tert-butyl ester
  参考文献：
  名称：

  Achiral oligoamines as versatile tool for the development of aspartic protease inhibitors

  摘要：

  Due to the important role that aspartic proteases play in many patho-physiological processes, they have intensively been targeted by modern drug development. However, up to now, only for two family members, renin and HIV protease, approved drugs are available. Inhibitor development, mostly guided by mimicking the natural peptide substrates, resulted in very potent inhibitors for several targets, but the pharmacokinetic properties of these compounds were often not optimal. Herein we report a novel approach for lead structure discovery of non-peptidic aspartic protease inhibitors using easily accessible achiral linear oligoamines as starting point. An initial library comprising 11 inhibitors was developed and screened against six selected aspartic proteases. Several hits could be identified, among them selective as well as rather promiscuous inhibitors. The design concept was confirmed by determination of the crystal structure of two derivatives in complex with the HIV-1 protease, and represents a promising basis for the further inhibitor development. (C) 2008 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2008.08.012