H-Thr-Thr-Asn-Tyr-Thr-Asp(OH)-OH | 144333-03-9

• 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: H-Thr-Thr-Asn-Tyr-Thr-Asp(OH)-OH
• 英文别名: H-Thr-Thr-Asn-Tyr-Thr-Asp-OH；(2S)-2-[[(2S,3R)-2-[[(2S)-2-[[(2S)-4-amino-2-[[(2S,3R)-2-[[(2S,3R)-2-amino-3-hydroxybutanoyl]amino]-3-hydroxybutanoyl]amino]-4-oxobutanoyl]amino]-3-(4-hydroxyphenyl)propanoyl]amino]-3-hydroxybutanoyl]amino]butanedioic acid
• CAS: 144333-03-9
• 化学式: C₂₉H₄₃N₇O₁₄
• 分子量: 713.699
• InChiKey: BBJRVZZNGCQXFW-IJPHQCLOSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -7.3
• 重原子数：
  50
• 可旋转键数：
  20
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.52
• 拓扑面积：
  370
• 氢给体数：
  13
• 氢受体数：
  15

反应信息

• 作为产物：
  描述：

  N-苄氧羰基-L-酪氨酸对硝基苯酯 在 palladium on activated charcoal N-甲基吗啉 、 sodium hydroxide 、 氢气 、 溶剂黄146 、 苯甲醚 、 三氟乙酸 作用下， 以 甲醇 、 N,N-二甲基甲酰胺 为溶剂， 25.0 ℃ 、101.33 kPa 条件下， 反应 22.17h， 生成 H-Thr-Thr-Asn-Tyr-Thr-Asp(OH)-OH
  参考文献：
  名称：

  A cyclic peptide T analogue with high chemotactic activity

  摘要：

  Peptide T is an octapeptide (H-Ala-Ser-Thr-Thr-Thr-Asn-Tyr-Thr-OH) based on a consensus sequence that has been identified in HIV proteins. Two conformationally-restricted analogues of peptide T fragment (H-Thr-Thr-Asn-Tyr-Thr-OH) were synthesized by cyclisation of the N-terminal amino group of Thr to the alpha or beta-carboxyl moiety of Asp introduced at the C-terminus of the peptide. The cyclo Thr-Thr-Asn-Tyr-Thr-Asp(OH) (C-alpha) showed high in vitro chemotactic activity, whereas the conformational restriction introduced into Thr-Thr-Asn-Tyr-Thr-Asp-OH was incompatible with the CD4 receptor. The cyclic analogue C-alpha was more active than its ester and the open-chain reference compound H-Thr-Thr-Asn-Tyr-Thr-Asp-OH. It also proved to be highly resistant to degradation by plasma or brain enzymes.

  DOI：

  10.1016/0223-5234(92)90151-p

文献信息

• A cyclic peptide T analogue with high chemotactic activity
  作者：M Marastoni、S Salvadori、G Balboni、V Scaranari、S Spisani、E Reali、AL Giuliani、R Tomatis

  DOI：10.1016/0223-5234(92)90151-p

  日期：1992.6

  Peptide T is an octapeptide (H-Ala-Ser-Thr-Thr-Thr-Asn-Tyr-Thr-OH) based on a consensus sequence that has been identified in HIV proteins. Two conformationally-restricted analogues of peptide T fragment (H-Thr-Thr-Asn-Tyr-Thr-OH) were synthesized by cyclisation of the N-terminal amino group of Thr to the alpha or beta-carboxyl moiety of Asp introduced at the C-terminus of the peptide. The cyclo Thr-Thr-Asn-Tyr-Thr-Asp(OH) (C-alpha) showed high in vitro chemotactic activity, whereas the conformational restriction introduced into Thr-Thr-Asn-Tyr-Thr-Asp-OH was incompatible with the CD4 receptor. The cyclic analogue C-alpha was more active than its ester and the open-chain reference compound H-Thr-Thr-Asn-Tyr-Thr-Asp-OH. It also proved to be highly resistant to degradation by plasma or brain enzymes.