N-triphenylmethyl-(3S)-3-[(2S,3S,4S)-3-azido-4-methyl-2-triethylsilyloxyhexylamino]-4-(tert-butyldiphenylsilyloxy)butyramide | 439688-97-8

• 分子结构分类: 有机化合物 - 苯类化合物 - 三苯基化合物
• 英文名称: N-triphenylmethyl-(3S)-3-[(2S,3S,4S)-3-azido-4-methyl-2-triethylsilyloxyhexylamino]-4-(tert-butyldiphenylsilyloxy)butyramide
• 英文别名: (3S)-3-[[(2S,3S,4S)-3-azido-4-methyl-2-triethylsilyloxyhexyl]amino]-4-[tert-butyl(diphenyl)silyl]oxy-N-tritylbutanamide
• CAS: 439688-97-8
• 化学式: C₅₂H₆₉N₅O₃Si₂
• 分子量: 868.323
• InChiKey: PERPREHZNYDNPE-IZZAXFEKSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  11.13
• 重原子数：
  62
• 可旋转键数：
  24
• 环数：
  5.0
• sp3杂化的碳原子比例：
  0.4
• 拓扑面积：
  74
• 氢给体数：
  2
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  N-triphenylmethyl-(3S)-3-[(2S,3S,4S)-3-azido-4-methyl-2-triethylsilyloxyhexylamino]-4-(tert-butyldiphenylsilyloxy)butyramide 在 盐酸 、 potassium hydride 、 N,N'-二异丙基碳二亚胺 作用下， 以 四氢呋喃 、 二氯甲烷 、 N,N-二甲基甲酰胺 为溶剂， 反应 149.5h， 生成 N-triphenylmethyl-(3S)-{(2S,6S)-6-[(1S,2S)-1-azido-2-methylbutyl]-2-isopropylmorpholin-3-one-4-yl}-4-(tert-butyldiphenylsilyloxy)butyramide
  参考文献：
  名称：

  Synthesis and Pharmacological Evaluation of an Analogue of the Peptide Hormone Oxytocin That Contains a Mimetic of an Inverse γ-Turn

  摘要：

  Oxytocin is a neurohypophyseal peptide hormone that induces labor and lactation in mammals. An inverse gamma-turn mimetic corresponding to the tripeptide Ile-Val-Asn has been synthesized and incorporated instead of residues 3-5 of oxytocin to probe the hypothesis that a gamma-turn involving these residues is found in the receptor bound conformation of oxytocin. In the turn mimetic, residues i and i + 1 are connected by a psi[CH2O] isostere while a covalent methylene bridge replaces the hydrogen bond that is often found between residues i and i + 2 in gamma-turns. The turn mimetic was assembled from three types of building blocks: an azido epoxide, an a-bromo acid, and a protected beta-amino alcohol. The oxytocin analogue did not induce contractions of the uterus nor did it inhibit oxytocin-induced contractions. It is suggested that the loss of bioactivity is mainly due to the presence of a psi[CH2O] isostere instead of an amide bond between residues i and i + 1 in the turn mimetic.

  DOI：

  10.1021/jm0110744
• 作为产物：
  描述：

  Benzoic acid (S)-3-azido-2-hydroxy-4-methyl-hexyl ester 在 咪唑 、 sodium ethanolate 作用下， 以 四氢呋喃 、 乙醇 、 二氯甲烷 为溶剂， 反应 116.5h， 生成 N-triphenylmethyl-(3S)-3-[(2S,3S,4S)-3-azido-4-methyl-2-triethylsilyloxyhexylamino]-4-(tert-butyldiphenylsilyloxy)butyramide
  参考文献：
  名称：

  Synthesis and Pharmacological Evaluation of an Analogue of the Peptide Hormone Oxytocin That Contains a Mimetic of an Inverse γ-Turn

  摘要：

  Oxytocin is a neurohypophyseal peptide hormone that induces labor and lactation in mammals. An inverse gamma-turn mimetic corresponding to the tripeptide Ile-Val-Asn has been synthesized and incorporated instead of residues 3-5 of oxytocin to probe the hypothesis that a gamma-turn involving these residues is found in the receptor bound conformation of oxytocin. In the turn mimetic, residues i and i + 1 are connected by a psi[CH2O] isostere while a covalent methylene bridge replaces the hydrogen bond that is often found between residues i and i + 2 in gamma-turns. The turn mimetic was assembled from three types of building blocks: an azido epoxide, an a-bromo acid, and a protected beta-amino alcohol. The oxytocin analogue did not induce contractions of the uterus nor did it inhibit oxytocin-induced contractions. It is suggested that the loss of bioactivity is mainly due to the presence of a psi[CH2O] isostere instead of an amide bond between residues i and i + 1 in the turn mimetic.

  DOI：

  10.1021/jm0110744

文献信息

• Synthesis and Pharmacological Evaluation of an Analogue of the Peptide Hormone Oxytocin That Contains a Mimetic of an Inverse γ-Turn
  作者：ZhongQing Yuan、David Blomberg、Ingmar Sethson、Kay Brickmann、Kjell Ekholm、Birgitta Johansson、Anders Nilsson、Jan Kihlberg

  DOI：10.1021/jm0110744

  日期：2002.6.1

  Oxytocin is a neurohypophyseal peptide hormone that induces labor and lactation in mammals. An inverse gamma-turn mimetic corresponding to the tripeptide Ile-Val-Asn has been synthesized and incorporated instead of residues 3-5 of oxytocin to probe the hypothesis that a gamma-turn involving these residues is found in the receptor bound conformation of oxytocin. In the turn mimetic, residues i and i + 1 are connected by a psi[CH2O] isostere while a covalent methylene bridge replaces the hydrogen bond that is often found between residues i and i + 2 in gamma-turns. The turn mimetic was assembled from three types of building blocks: an azido epoxide, an a-bromo acid, and a protected beta-amino alcohol. The oxytocin analogue did not induce contractions of the uterus nor did it inhibit oxytocin-induced contractions. It is suggested that the loss of bioactivity is mainly due to the presence of a psi[CH2O] isostere instead of an amide bond between residues i and i + 1 in the turn mimetic.