N(α)-[2-(2-phenylethyl)amino-5-chlorobenzoyl]-L-isoleucinyl-D-glutamine

• 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(α)-[2-(2-phenylethyl)amino-5-chlorobenzoyl]-L-isoleucinyl-D-glutamine
• 英文别名: N(α)-[2-(phenylethyl)amino-5-chloro]benzoyl-L-isoleucinyl-D-glutamine；(2R)-5-amino-2-[[(2S)-2-[[5-chloro-2-(2-phenylethylamino)benzoyl]amino]-3-methylpentanoyl]amino]-5-oxopentanoic acid
• 化学式: C₂₆H₃₃ClN₄O₅
• 分子量: 517.025
• InChiKey: GRBTVMBMGVPLRZ-OSZJVERNSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.2
• 重原子数：
  36
• 可旋转键数：
  14
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.38
• 拓扑面积：
  151
• 氢给体数：
  5
• 氢受体数：
  6

反应信息

• 作为产物：
  描述：

  5-氯-2-硝基苯甲酸 、 苯乙醛 、 Fmoc-L-异亮氨酸 、 N-(9-芴甲氧羰基)-D-谷氨酸 1-叔丁酯 在 1-羟基苯并三唑 、 N,N'-二异丙基碳二亚胺 、 哌啶 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 3.67h， 以19.7%的产率得到N(α)-[2-(2-phenylethyl)amino-5-chlorobenzoyl]-L-isoleucinyl-D-glutamine
  参考文献：
  名称：

  New muramyl dipeptide (MDP) mimics without the carbohydrate moiety as potential adjuvant candidates for a therapeutic hepatitis B vaccine (HBV)

  摘要：

  A series of new muramyl dipeptide (MDP) mimics were designed and synthesized via a solid-phase synthetic route. Their adjuvant activities were evaluated ex vivo for investigation of the synergism of the S(28-39) peptide, which is an MHC class I binding epitope of recombinant hepatitis B surface antigen (HBsAg) for both humans and mice. Several compounds without the carbohydrate moiety exerted better adjuvanticity than the MDP-C that has been reported by our laboratory previously. A primary screening test revealed that compounds 6, 14 and 16 exhibited stronger adjuvanticity compared with other MDP mimics. (C) 2011 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2011.05.056

文献信息

• New muramyl dipeptide (MDP) mimics without the carbohydrate moiety as potential adjuvant candidates for a therapeutic hepatitis B vaccine (HBV)
  作者：Nan Zhao、Yao Ma、Shengmei Zhang、Xin Fang、Zhenglun Liang、Gang Liu

  DOI：10.1016/j.bmcl.2011.05.056

  日期：2011.7

  A series of new muramyl dipeptide (MDP) mimics were designed and synthesized via a solid-phase synthetic route. Their adjuvant activities were evaluated ex vivo for investigation of the synergism of the S(28-39) peptide, which is an MHC class I binding epitope of recombinant hepatitis B surface antigen (HBsAg) for both humans and mice. Several compounds without the carbohydrate moiety exerted better adjuvanticity than the MDP-C that has been reported by our laboratory previously. A primary screening test revealed that compounds 6, 14 and 16 exhibited stronger adjuvanticity compared with other MDP mimics. (C) 2011 Elsevier Ltd. All rights reserved.