tert-butyl (1S)-[1-(benzylcarbamoyl)butyl]carbamate | 875105-51-4

• 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: tert-butyl (1S)-[1-(benzylcarbamoyl)butyl]carbamate
• 英文别名: tert-butyl N-[(2S)-1-(benzylamino)-1-oxopentan-2-yl]carbamate
• CAS: 875105-51-4
• 化学式: C₁₇H₂₆N₂O₃
• 分子量: 306.405
• InChiKey: QGAPPLVJSYPWKE-AWEZNQCLSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.1
• 重原子数：
  22
• 可旋转键数：
  8
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.53
• 拓扑面积：
  67.4
• 氢给体数：
  2
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  tert-butyl (1S)-[1-(benzylcarbamoyl)butyl]carbamate 在 盐酸 、 sodium cyanoborohydride 作用下， 以 甲醇 、 乙酸乙酯 为溶剂， 生成 tert-butyl N-[(2R)-1-[[(2S)-1-(benzylamino)-1-oxopentan-2-yl]amino]-3-tritylsulfanylpropan-2-yl]carbamate
  参考文献：
  名称：

  Pseudodipeptide Inhibitors of Protein Farnesyltransferase

  摘要：

  A series of pseudodipeptide amides are described that inhibit Ras protein farnesyltransferase (PFTase). These inhibitors are truncated versions of the C-terminal tetrapeptide (CAAX motif) of Ras that serves as the signal sequence for PFTase-catalyzed protein farnesylation. In contrast to CAAX peptidomimetics previously reported, these inhibitors do not have a C-terminal carboxyl moiety, yet they inhibit farnesylation in vitro at <100 nM. Despite the absence of the X residue in the CAAX motif, which normally directs prenylation specificity, these pseudodipeptides are greater than 100-fold selective for PFTase over type 1 protein geranylgeranyltransferase.

  DOI：

  10.1021/jm00020a010
• 作为产物：
  描述：

  N-tert-butoxycarbonyl-L-norvaline 、 苄胺 在 1-(3-二甲基氨基丙基)-3-乙基碳二亚胺 、 三乙胺 、 3-羟基-1,2,3-苯并三嗪-4(3H)-酮 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 生成 tert-butyl (1S)-[1-(benzylcarbamoyl)butyl]carbamate
  参考文献：
  名称：

  Pseudodipeptide Inhibitors of Protein Farnesyltransferase

  摘要：

  A series of pseudodipeptide amides are described that inhibit Ras protein farnesyltransferase (PFTase). These inhibitors are truncated versions of the C-terminal tetrapeptide (CAAX motif) of Ras that serves as the signal sequence for PFTase-catalyzed protein farnesylation. In contrast to CAAX peptidomimetics previously reported, these inhibitors do not have a C-terminal carboxyl moiety, yet they inhibit farnesylation in vitro at <100 nM. Despite the absence of the X residue in the CAAX motif, which normally directs prenylation specificity, these pseudodipeptides are greater than 100-fold selective for PFTase over type 1 protein geranylgeranyltransferase.

  DOI：

  10.1021/jm00020a010

文献信息

• Inhibitors of peptidyl arginine deiminase (PAD) enzymes and uses thereof
  申请人：UNIVERSITY HEALTH NETWORK

  公开号：US10716791B2

  公开（公告）日：2020-07-21

  The present application relates to a-substituted amino acid compounds of the Formula (I), compositions comprising these compounds and their use, in particular for the treatment of diseases, disorders or conditions characterized by or associated with the hypercitrullination of proteins by peptidyl arginine deiminase (PAD) enzymes.

  本申请涉及式（I）的 a-取代氨基酸化合物、包含这些化合物的组合物及其用途，特别是用于治疗以肽基精氨酸脱氨酶（PAD）对蛋白质的高瓜氨酸化为特征或与之相关的疾病、失调或病症。
• Exploration of acyl sulfonamides as carboxylic acid replacements in protease inhibitors of the hepatitis C virus full-length NS3
  作者：Robert Rönn、Yogesh A. Sabnis、Thomas Gossas、Eva Åkerblom、U. Helena Danielson、Anders Hallberg、Anja Johansson

  DOI：10.1016/j.bmc.2005.08.045

  日期：2006.1

  The hepatitis C virus (HCV) NS3 protease has emerged as a promising anti-HCV drug target. Herein, we present an investigation of NS3 inhibitors comprising the acyl sulfonamide functionality. A series of tetra- and tripeptide based acyl sulfonamide inhibitors and their structure-activity relationships from both enzymatic and cell-based in vitro assays are presented. In summary, the acidity of the acyl sulfonamide functionality, the character of the P1 side chain, and the acyl sulfonamide substituent were found to be important for the inhibitory potencies. (c) 2005 Elsevier Ltd. All rights reserved.
• Pseudodipeptide Inhibitors of Protein Farnesyltransferase
  作者：S. Jane deSolms、Albert A. Deana、Elizabeth A. Giuliani、Samuel L. Graham、Nancy E. Kohl、Scott D. Mosser、Allen I. Oliff、David L. Pompliano、Elaine Rands

  DOI：10.1021/jm00020a010

  日期：1995.9

  A series of pseudodipeptide amides are described that inhibit Ras protein farnesyltransferase (PFTase). These inhibitors are truncated versions of the C-terminal tetrapeptide (CAAX motif) of Ras that serves as the signal sequence for PFTase-catalyzed protein farnesylation. In contrast to CAAX peptidomimetics previously reported, these inhibitors do not have a C-terminal carboxyl moiety, yet they inhibit farnesylation in vitro at <100 nM. Despite the absence of the X residue in the CAAX motif, which normally directs prenylation specificity, these pseudodipeptides are greater than 100-fold selective for PFTase over type 1 protein geranylgeranyltransferase.