2-(N-acetyl)-L-phenylalanylamido-2-deoxy-β-D-glucose | 141265-94-3

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: 2-(N-acetyl)-L-phenylalanylamido-2-deoxy-β-D-glucose
• 英文别名: (2S)-2-acetamido-3-phenyl-N-[(2R,3R,4R,5S,6R)-2,4,5-trihydroxy-6-(hydroxymethyl)oxan-3-yl]propanamide
• CAS: 141265-94-3
• 化学式: C₁₇H₂₄N₂O₇
• 分子量: 368.387
• InChiKey: UWYNURYACYERAL-WTUOYXTGSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -1.3
• 重原子数：
  26
• 可旋转键数：
  6
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.53
• 拓扑面积：
  148
• 氢给体数：
  6
• 氢受体数：
  7

反应信息

• 作为产物：
  描述：

  N-乙酰-L-苯丙氨酸 在 N-甲基吗啉 、 sodium methylate 、 氯甲酸异丁酯 作用下， 以 四氢呋喃 、 甲醇 为溶剂， 反应 16.0h， 生成 2-(N-acetyl)-L-phenylalanylamido-2-deoxy-β-D-glucose
  参考文献：
  名称：

  Synthesis and properties of d-glucosamine N-peptidyl derivatives as substrate analog inhibitors of papain and cathepsin B

  摘要：

  N-peptidyl derivatives of D-glucosamine 7c-7n were synthesized and tested as 7c-7n were synthesized and tested as reversible, substrate analog inhibitors of cysteine and serine-proteases. D-Glucosamine itself showed fair inhibiting properties against cysteine-proteases. Derivatives 7c-7i, designed to improve binding at papain active site, displayed reversible inhibition with K(i) ranging from 67-860-mu-M for papain and from 111-2400-mu-M for cathepsin B. Representative serine proteases were unaffected. No inhibitory activity against human leukocyte elastase was observed for derivatives 7m and 7n bearing very effective peptidyl recognizing units for this enzyme.

  DOI：

  10.1016/0223-5234(91)90001-4

文献信息

• Synthesis and properties of d-glucosamine N-peptidyl derivatives as substrate analog inhibitors of papain and cathepsin B
  作者：C Giordano、C Gallina、V Consalvi、R Scandurra

  DOI：10.1016/0223-5234(91)90001-4

  日期：1991.11

  N-peptidyl derivatives of D-glucosamine 7c-7n were synthesized and tested as 7c-7n were synthesized and tested as reversible, substrate analog inhibitors of cysteine and serine-proteases. D-Glucosamine itself showed fair inhibiting properties against cysteine-proteases. Derivatives 7c-7i, designed to improve binding at papain active site, displayed reversible inhibition with K(i) ranging from 67-860-mu-M for papain and from 111-2400-mu-M for cathepsin B. Representative serine proteases were unaffected. No inhibitory activity against human leukocyte elastase was observed for derivatives 7m and 7n bearing very effective peptidyl recognizing units for this enzyme.