5-adamantan-1-yl-2,4-dihydroxy-N-(2-hydroxy-benzyl)-benzamide | 1365531-27-6

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: 5-adamantan-1-yl-2,4-dihydroxy-N-(2-hydroxy-benzyl)-benzamide
• 英文别名: 5-(1-adamantyl)-2,4-dihydroxy-N-[(2-hydroxyphenyl)methyl]benzamide
• CAS: 1365531-27-6
• 化学式: C₂₄H₂₇NO₄
• 分子量: 393.483
• InChiKey: KYTBXVRSVFWBHP-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  6.1
• 重原子数：
  29
• 可旋转键数：
  4
• 环数：
  6.0
• sp3杂化的碳原子比例：
  0.46
• 拓扑面积：
  89.8
• 氢给体数：
  4
• 氢受体数：
  4

反应信息

• 作为产物：
  描述：

  2,4-二羟基苯甲酸 在 硫酸 、 碳酸氢钠 、 溶剂黄146 、 N,N'-二环己基碳二亚胺 作用下， 以 1,4-二氧六环 、 二氯甲烷 、 水 为溶剂， 反应 14.0h， 生成 5-adamantan-1-yl-2,4-dihydroxy-N-(2-hydroxy-benzyl)-benzamide
  参考文献：
  名称：

  Adamantyl N-benzylbenzamide: New series of depigmentation agents with tyrosinase inhibitory activity

  摘要：

  A new series of polyhydroxylated N-benzylbenzamide derivatives containing an adamantyl moiety has been synthesized, and the depigmenting and tyrosinase inhibitory activities of the molecules were evaluated. The lipophilic character of the adamantyl moiety appeared to confer greater depigmentation power on the benzamide derivatives as compared to those lacking adamantyl substitution. Molecular modeling was applied in order to elucidate the interactions between ligands and tyrosinase that led to inhibition. (C) 2012 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2011.12.144

文献信息

• Adamantyl N-benzylbenzamide: New series of depigmentation agents with tyrosinase inhibitory activity
  作者：Heung Soo Baek、Yong Deog Hong、Chang Seok Lee、Ho Sik Rho、Song Seok Shin、Young-Ho Park、Yung Hyup Joo

  DOI：10.1016/j.bmcl.2011.12.144

  日期：2012.3

  A new series of polyhydroxylated N-benzylbenzamide derivatives containing an adamantyl moiety has been synthesized, and the depigmenting and tyrosinase inhibitory activities of the molecules were evaluated. The lipophilic character of the adamantyl moiety appeared to confer greater depigmentation power on the benzamide derivatives as compared to those lacking adamantyl substitution. Molecular modeling was applied in order to elucidate the interactions between ligands and tyrosinase that led to inhibition. (C) 2012 Elsevier Ltd. All rights reserved.