methyl (S)-2-(tert-butoxycarbonylamino)-6-(methanesulfonyloxy)hexanoate

• 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: methyl (S)-2-(tert-butoxycarbonylamino)-6-(methanesulfonyloxy)hexanoate
• 英文别名: methyl (2S)-2-[(2-methylpropan-2-yl)oxycarbonylamino]-6-methylsulfonyloxyhexanoate
• 化学式: C₁₃H₂₅NO₇S
• 分子量: 339.41
• InChiKey: OGPQZSKINMXTFD-JTQLQIEISA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.4
• 重原子数：
  22
• 可旋转键数：
  11
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.85
• 拓扑面积：
  116
• 氢给体数：
  1
• 氢受体数：
  7

反应信息

• 作为反应物：
  描述：

  组胺 、 methyl (S)-2-(tert-butoxycarbonylamino)-6-(methanesulfonyloxy)hexanoate 在 1,8-二氮杂双环[5.4.0]十一碳-7-烯 作用下， 以 甲醇 为溶剂， 以66%的产率得到methyl (2S)-6-[2-(1H-imidazol-5-yl)ethylamino]-2-[(2-methylpropan-2-yl)oxycarbonylamino]hexanoate
  参考文献：
  名称：

  A facile synthesis of (S)-gizzerosine, a potent agonist of the histamine H2-receptor

  摘要：

  A simple and direct approach for the synthesis of (S)-gizzerosine, an amino acid responsible for the disease, black vomit, and a potent histamine H-2-receptor, has been developed in 10 steps and in 31% overall yield from L-aspartic acid. The key steps involved a two-carbon homologation of an L-aspartic acid semi-aldehyde and direct alkylation of unprotected histamine with a 6-hydroxynorleucine derivative. (c) 2007 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.tetlet.2007.09.165
• 作为产物：
  描述：

  dimethyl (S)-2-[(tert-butoxycarbonyl)amino]hexanedioate 在 甲醇 、 4-二甲氨基吡啶 、 sodium tetrahydroborate 、 二异丁基氢化铝 、 三乙胺 、 三氟乙酸 作用下， 以 乙醚 、 正己烷 、 二氯甲烷 、 乙腈 为溶剂， 反应 98.58h， 生成 methyl (S)-2-(tert-butoxycarbonylamino)-6-(methanesulfonyloxy)hexanoate
  参考文献：
  名称：

  Synthesis and inhibitory activity of substrate-analog fructosyl peptide oxidase inhibitors

  摘要：

  Fructosyl peptide oxidases (FPOXs) play a crucial role in the diagnosis of diabetes. Their main function is to cleave fructosyl amino acids or fructosyl peptides into glucosone and the corresponding amino acids/dipeptides. In this study, the substrate-analog FPOX inhibitors 1a-c were successfully designed and synthesized. These inhibitors mimic N-alpha-fructosyl-L-valine (Fru-Val), [N-alpha-fructosyl-L-valyl]-L-histidine (Fru-ValHis), and N-epsilon-fructosyl-L-lysine (epsilon Fru-Lys), respectively. The secondary nitrogen atom in the natural substrates, linking fructose and amino acid or dipeptide moieties, was substituted in 1a-c with a sulfur atom to avoid enzymatic cleavage. Kinetic studies revealed that 1a-c act as competitive inhibitors against an FPOX obtained from Coniochaeta sp., and K-i values of 11.1, 66.8, and 782 mu M were obtained for 1a-c, respectively. (C) 2015 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2015.07.045

文献信息

• A facile synthesis of (S)-gizzerosine, a potent agonist of the histamine H2-receptor
  作者：Kate N. Fanning、Andrew Sutherland

  DOI：10.1016/j.tetlet.2007.09.165

  日期：2007.11

  A simple and direct approach for the synthesis of (S)-gizzerosine, an amino acid responsible for the disease, black vomit, and a potent histamine H-2-receptor, has been developed in 10 steps and in 31% overall yield from L-aspartic acid. The key steps involved a two-carbon homologation of an L-aspartic acid semi-aldehyde and direct alkylation of unprotected histamine with a 6-hydroxynorleucine derivative. (c) 2007 Elsevier Ltd. All rights reserved.
• Synthesis and inhibitory activity of substrate-analog fructosyl peptide oxidase inhibitors
  作者：Bunta Watanabe、Atsushi Ichiyanagi、Kozo Hirokawa、Keiko Gomi、Toru Nakatsu、Hiroaki Kato、Naoki Kajiyama

  DOI：10.1016/j.bmcl.2015.07.045

  日期：2015.9

  Fructosyl peptide oxidases (FPOXs) play a crucial role in the diagnosis of diabetes. Their main function is to cleave fructosyl amino acids or fructosyl peptides into glucosone and the corresponding amino acids/dipeptides. In this study, the substrate-analog FPOX inhibitors 1a-c were successfully designed and synthesized. These inhibitors mimic N-alpha-fructosyl-L-valine (Fru-Val), [N-alpha-fructosyl-L-valyl]-L-histidine (Fru-ValHis), and N-epsilon-fructosyl-L-lysine (epsilon Fru-Lys), respectively. The secondary nitrogen atom in the natural substrates, linking fructose and amino acid or dipeptide moieties, was substituted in 1a-c with a sulfur atom to avoid enzymatic cleavage. Kinetic studies revealed that 1a-c act as competitive inhibitors against an FPOX obtained from Coniochaeta sp., and K-i values of 11.1, 66.8, and 782 mu M were obtained for 1a-c, respectively. (C) 2015 Elsevier Ltd. All rights reserved.