N-chloroacetyl-L-phenylalanine isopentylamide

• 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: N-chloroacetyl-L-phenylalanine isopentylamide
• 英文别名: (2S)-2-[(2-chloroacetyl)amino]-N-(3-methylbutyl)-3-phenylpropanamide
• 化学式: C₁₆H₂₃ClN₂O₂
• 分子量: 310.824
• InChiKey: ANKBGLVGKUDHSE-AWEZNQCLSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.7
• 重原子数：
  21
• 可旋转键数：
  8
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.5
• 拓扑面积：
  58.2
• 氢给体数：
  2
• 氢受体数：
  2

反应信息

• 作为产物：
  描述：

  Z-Phe-O-COO-isoBu 在 palladium on activated charcoal 氢气 、 sodium carbonate 作用下， 以 甲醇 、 二氯甲烷 、 氯仿 为溶剂， 反应 19.33h， 生成 N-chloroacetyl-L-phenylalanine isopentylamide
  参考文献：
  名称：

  N-Haloacetyl-amino-acid amides as active-site-directed inhibitors of papain and cathepsin B

  摘要：

  A series of N-haloacetyl-amino-acid amides were synthesized and tested as models of cysteine-protease inhibitors. They irreversibly inactivated papain and cathepsin B via a reversible enzyme--inhibitor intermediate. Apparent second-order rate constants of inactivation ranging from 65 to 16 700 M-1 s-1 were observed. Reactivity against papain, as compared to glutathione, was increased 16 400-fold for N-bromoacetyl-leucine isopentylamide and 25 700-fold for the corresponding iodoacetyl derivative; these increases are probably due to proximity effects. No inhibition of trypsin, chymotrypsin and porcine pancreatic elastase was observed. Haloacetamides represent an interesting class of easily synthesized, efficient. irreversible inhibitors of cysteine proteases, which have low non-specific alkylating properties.

  DOI：

  10.1016/0223-5234(92)90018-v

文献信息

• N-Haloacetyl-amino-acid amides as active-site-directed inhibitors of papain and cathepsin B
  作者：C Giordano、C Gallina、V Ottaviano、V Consalvi、R Scandurra

  DOI：10.1016/0223-5234(92)90018-v

  日期：1992.12

  A series of N-haloacetyl-amino-acid amides were synthesized and tested as models of cysteine-protease inhibitors. They irreversibly inactivated papain and cathepsin B via a reversible enzyme--inhibitor intermediate. Apparent second-order rate constants of inactivation ranging from 65 to 16 700 M-1 s-1 were observed. Reactivity against papain, as compared to glutathione, was increased 16 400-fold for N-bromoacetyl-leucine isopentylamide and 25 700-fold for the corresponding iodoacetyl derivative; these increases are probably due to proximity effects. No inhibition of trypsin, chymotrypsin and porcine pancreatic elastase was observed. Haloacetamides represent an interesting class of easily synthesized, efficient. irreversible inhibitors of cysteine proteases, which have low non-specific alkylating properties.