N-cyclohexylfumaramic acid | 113467-97-3

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 脂肪酰基
• 英文名称: N-cyclohexylfumaramic acid
• 英文别名: (E)-4-(cyclohexylamino)-4-oxobut-2-enoic acid；trans-3-cyclohexylcarbamoylpropenoic acid；HOOC-CH=CHCONH-cyclohexyl；N-cyclohexyl-maleamic acid；N-Cyclohexyl-maleamidsaeure；fumaric mono(cyclohexyl)amide；(2E)-4-(cyclohexylamino)-4-oxobut-2-enoic acid
• CAS: 113467-97-3
• 化学式: C₁₀H₁₅NO₃
• mdl: MFCD00185902
• 分子量: 197.234
• InChiKey: DEWAGGNAHQGYBD-VOTSOKGWSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.1
• 重原子数：
  14
• 可旋转键数：
  3
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.6
• 拓扑面积：
  66.4
• 氢给体数：
  2
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  N-cyclohexylfumaramic acid 在 1,4-二氧六环 、 钯 、 溶剂黄146 作用下， 生成 N⁴-cyclohexyl-asparagine
  参考文献：
  名称：

  Syntheses of Aspartic Acid Derivatives. II. N-Alkylated α- and β-Asparagines

  摘要：

  DOI：

  10.1021/ja01594a034
• 作为产物：
  描述：

  trans-3-cyclohexylcarbamoylpropenoic acid ethyl ester 在 水 、 sodium hydroxide 作用下， 以 乙醇 为溶剂， 以81%的产率得到N-cyclohexylfumaramic acid
  参考文献：
  名称：

  Aza-Peptidyl Michael Acceptor and Epoxide Inhibitors—Potent and Selective Inhibitors of Schistosoma mansoni and Ixodes ricinus Legumains (Asparaginyl Endopeptidases)

  摘要：

  Aza-peptide Michael acceptors and epoxides with the general structure of YCO-Ala-Ala-AAsn-trans-CH=CHCOR and YCO-Ala-Ala-AAsn-EP-COR, respectively, are shown to be potent inhibitors of asparaginyl endopeptidases (legumains) from the bloodfluke, Schistosoma mansoni (SmAE), and the hard tick, Ixodes ricinus (IrAE). Structure-activity relationships (SARs) were determined for a set of 41 aza-peptide Michael acceptors and eight aza-peptide epoxides. Both enzymes prefer disubstituted amides to monosubstituted amides in the P1' position, and potency increased as we increased the hydrophobicity of the inhibitor in this position. Extending the inhibitor to P5 resulted in increased potency, especially against IrAE, and both enzymes prefer small over large hydrophobic residues at P2. Aza-peptide Michael acceptor inhibitors are more potent than aza-peptide epoxide inhibitors, and for some of these compounds, second-order inhibiton rate constants are the fastest yet discovered. Given the central functions of these enzymes in both parasites, the data presented here may facilitate the eventual design of selective antiparasitic drugs.

  DOI：

  10.1021/jm900849h

文献信息

• N-PHENYLMALEIMIDE COMPOUND AND COPOLYMER COMPOSITION OBTAINED USING SAME
  申请人：Nippon Shokubai Co., Ltd.

  公开号：EP2690116A1

  公开（公告）日：2014-01-29

  The present invention provides an N-phenylmaleimide compound that can improve the quality of the obtained copolymer by using N-phenylmaleimide containing impurities in specific amounts or less as at least one component of the copolymerization monomers. The N-phenylmaleimide compound of the present invention contains 0.1% by weight or less of N-(2,5-dioxo-1-phenyl-3-pyrrolidinyl)-N-phenylmaleamic acid (PPMA) and/or 0.3% by weight or less of N-phenylfumaramic acid (PFA).

  本发明提供了一种N-苯基马来酰亚胺化合物，通过使用含有特定量或更少量杂质的N-苯基马来酰亚胺作为共聚单体的至少一种组分，可以提高所得共聚物的质量。本发明的 N-苯基马来酰亚胺化合物含有 0.1%（重量）或更少的 N-(2,5-二氧代-1-苯基-3-吡咯烷基)-N-苯基马来酸（PPMA）和/或 0.3%（重量）或更少的 N-苯基富马酸（PFA）。
• Syntheses of Aspartic Acid Derivatives. II. N-Alkylated α- and β-Asparagines
  作者：Y. Liwschitz、Yolan Edlitz-Pfeffermann、Y. Lapidoth

  DOI：10.1021/ja01594a034

  日期：1956.7
• Aza-Peptidyl Michael Acceptor and Epoxide Inhibitors—Potent and Selective Inhibitors of Schistosoma mansoni and Ixodes ricinus Legumains (Asparaginyl Endopeptidases)
  作者：Asli Ovat、Fanuel Muindi、Crystal Fagan、Michelle Brouner、Elizabeth Hansell、Jan Dvořák、Daniel Sojka、Petr Kopáček、James H. McKerrow、Conor R. Caffrey、James C. Powers

  DOI：10.1021/jm900849h

  日期：2009.11.26

  Aza-peptide Michael acceptors and epoxides with the general structure of YCO-Ala-Ala-AAsn-trans-CH=CHCOR and YCO-Ala-Ala-AAsn-EP-COR, respectively, are shown to be potent inhibitors of asparaginyl endopeptidases (legumains) from the bloodfluke, Schistosoma mansoni (SmAE), and the hard tick, Ixodes ricinus (IrAE). Structure-activity relationships (SARs) were determined for a set of 41 aza-peptide Michael acceptors and eight aza-peptide epoxides. Both enzymes prefer disubstituted amides to monosubstituted amides in the P1' position, and potency increased as we increased the hydrophobicity of the inhibitor in this position. Extending the inhibitor to P5 resulted in increased potency, especially against IrAE, and both enzymes prefer small over large hydrophobic residues at P2. Aza-peptide Michael acceptor inhibitors are more potent than aza-peptide epoxide inhibitors, and for some of these compounds, second-order inhibiton rate constants are the fastest yet discovered. Given the central functions of these enzymes in both parasites, the data presented here may facilitate the eventual design of selective antiparasitic drugs.