(-)-ethyl 2-[(benzyloxycarbonyl)(1-((tert-butoxycarbonyl-L-leucinyl)-L-leucinyl)-(S)-piperidin-3-yl)amino]acetate | 1365998-97-5

• 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: (-)-ethyl 2-[(benzyloxycarbonyl)(1-((tert-butoxycarbonyl-L-leucinyl)-L-leucinyl)-(S)-piperidin-3-yl)amino]acetate
• 英文别名: ethyl 2-[[(3S)-1-[(2S)-4-methyl-2-[[(2S)-4-methyl-2-[(2-methylpropan-2-yl)oxycarbonylamino]pentanoyl]amino]pentanoyl]piperidin-3-yl]-phenylmethoxycarbonylamino]acetate
• CAS: 1365998-97-5
• 化学式: C₃₄H₅₄N₄O₈
• 分子量: 646.825
• InChiKey: XLAYPRALGLSXOH-KCHLEUMXSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  5.5
• 重原子数：
  46
• 可旋转键数：
  18
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.68
• 拓扑面积：
  144
• 氢给体数：
  2
• 氢受体数：
  8

反应信息

• 作为反应物：
  描述：

  (-)-ethyl 2-[(benzyloxycarbonyl)(1-((tert-butoxycarbonyl-L-leucinyl)-L-leucinyl)-(S)-piperidin-3-yl)amino]acetate 在 palladium 10% on activated carbon 、 氨 、 氢气 作用下， 以 甲醇 、 乙醇 为溶剂， 反应 122.0h， 生成 tert-butyl ((S)-1-(((S)-1-((S)-3-((2-amino-2-oxoethyl)amino)piperidin-1-yl)-4-methyl-1-oxopentan-2-yl)amino)-4-methyl-1-oxopentan-2-yl)carbamate
  参考文献：
  名称：

  3-Aminopiperidine-Based Peptide Analogues as the First Selective Noncovalent Inhibitors of the Bacterial Cysteine Protease IdeS

  摘要：

  A series of eight peptides corresponding to the amino acid sequence of the hinge region of IgG and 17 newly synthesized peptide analogues containing a piperidine moiety as a replacement of a glycine residue were tested as potential inhibitors of the bacterial IgG degrading enzyme of Streptococcus pyogenes, IdeS. None of the peptides showed any inhibitory activity of IdeS, but several piperidine-based analogues were identified as inhibitors. Two different analysis methods were used: an SDS-PAGE based assay to detect IgG cleavage products and a surface plasmon resonance spectroscopy based assay to quantify the degree of inhibition. To investigate the selectivity of the inhibitors for IdeS, all compounds were screened against two other related cysteine proteases (SpeB and papain). The selectivity results show that larger analogues that are active inhibitors of IdeS are even more potent as inhibitors of papain, whereas smaller analogues that are active inhibitors of IdeS inhibit neither SpeB nor papain. Two compounds were identified that exhibit high selectivity against IdeS and will be used for further studies.

  DOI：

  10.1021/jm201517a
• 作为产物：
  描述：

  (S)-1-Boc-3-氨基哌啶 在 三乙酰氧基硼氢化钠 、 1-羟基苯并三唑 、 溶剂黄146 、 1-(3-二甲基氨基丙基)-3-乙基碳二亚胺 、 sodium sulfate 、 三乙胺 、 三氟乙酸 作用下， 以 二氯甲烷 、 甲苯 为溶剂， 反应 84.5h， 生成 (-)-ethyl 2-[(benzyloxycarbonyl)(1-((tert-butoxycarbonyl-L-leucinyl)-L-leucinyl)-(S)-piperidin-3-yl)amino]acetate
  参考文献：
  名称：

  3-Aminopiperidine-Based Peptide Analogues as the First Selective Noncovalent Inhibitors of the Bacterial Cysteine Protease IdeS

  摘要：

  A series of eight peptides corresponding to the amino acid sequence of the hinge region of IgG and 17 newly synthesized peptide analogues containing a piperidine moiety as a replacement of a glycine residue were tested as potential inhibitors of the bacterial IgG degrading enzyme of Streptococcus pyogenes, IdeS. None of the peptides showed any inhibitory activity of IdeS, but several piperidine-based analogues were identified as inhibitors. Two different analysis methods were used: an SDS-PAGE based assay to detect IgG cleavage products and a surface plasmon resonance spectroscopy based assay to quantify the degree of inhibition. To investigate the selectivity of the inhibitors for IdeS, all compounds were screened against two other related cysteine proteases (SpeB and papain). The selectivity results show that larger analogues that are active inhibitors of IdeS are even more potent as inhibitors of papain, whereas smaller analogues that are active inhibitors of IdeS inhibit neither SpeB nor papain. Two compounds were identified that exhibit high selectivity against IdeS and will be used for further studies.

  DOI：

  10.1021/jm201517a

文献信息

• 3-Aminopiperidine-Based Peptide Analogues as the First Selective Noncovalent Inhibitors of the Bacterial Cysteine Protease IdeS
  作者：Kristina Berggren、Reine Vindebro、Claes Bergström、Christian Spoerry、Helena Persson、Tomas Fex、Jan Kihlberg、Ulrich von Pawel-Rammingen、Kristina Luthman

  DOI：10.1021/jm201517a

  日期：2012.3.22

  A series of eight peptides corresponding to the amino acid sequence of the hinge region of IgG and 17 newly synthesized peptide analogues containing a piperidine moiety as a replacement of a glycine residue were tested as potential inhibitors of the bacterial IgG degrading enzyme of Streptococcus pyogenes, IdeS. None of the peptides showed any inhibitory activity of IdeS, but several piperidine-based analogues were identified as inhibitors. Two different analysis methods were used: an SDS-PAGE based assay to detect IgG cleavage products and a surface plasmon resonance spectroscopy based assay to quantify the degree of inhibition. To investigate the selectivity of the inhibitors for IdeS, all compounds were screened against two other related cysteine proteases (SpeB and papain). The selectivity results show that larger analogues that are active inhibitors of IdeS are even more potent as inhibitors of papain, whereas smaller analogues that are active inhibitors of IdeS inhibit neither SpeB nor papain. Two compounds were identified that exhibit high selectivity against IdeS and will be used for further studies.