Z-Thr-Asp(OBu^t)-OMe | 144332-93-4

• 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: Z-Thr-Asp(OBu^t)-OMe
• 英文别名: Cbz-Thr-Asp(OtBu)-OMe；4-O-tert-butyl 1-O-methyl (2S)-2-[[(2S,3R)-3-hydroxy-2-(phenylmethoxycarbonylamino)butanoyl]amino]butanedioate
• CAS: 144332-93-4
• 化学式: C₂₁H₃₀N₂O₈
• 分子量: 438.478
• InChiKey: VJMABGDKVUANII-KMFMINBZSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.3
• 重原子数：
  31
• 可旋转键数：
  13
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.52
• 拓扑面积：
  140
• 氢给体数：
  3
• 氢受体数：
  8

反应信息

• 作为反应物：
  描述：

  Z-Thr-Asp(OBu^t)-OMe 在 palladium on activated charcoal N-甲基吗啉 、 sodium hydroxide 、 二苯基膦叠氮化物 、 氢气 、 碳酸氢钠 、 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， 4.0~25.0 ℃ 、101.33 kPa 条件下， 反应 95.17h， 生成 cyclo-Thr-Thr-Asn-Tyr-Thr-Asp(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
• 作为产物：
  描述：

  L-Asparaginsaeure-α-methylester-β-tert-butylester 、 苄氧羰基-苏氨酰-琥珀酰亚胺 在 N-甲基吗啉 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 4.0h， 以89%的产率得到Z-Thr-Asp(OBu^t)-OMe
  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

• Concise Synthesis of 2,5-Diketopiperazines via Catalytic Hydroxy-Directed Peptide Bond Formations
  作者：Masayoshi Koshizuka、Kaito Shinoda、Kazuishi Makino、Naoyuki Shimada

  DOI：10.1021/acs.joc.3c00195

  日期：2023.6.2

  concise synthesis of this type of DKPs through diboronic acid anhydride-catalyzed hydroxy-directed peptide bond formations. The sequential reactions in this report, which consist of three steps, an intermolecular catalytic condensation reaction in which water is the only byproduct, a simple deprotection of the nitrogen-protecting group, and an intramolecular cyclization, enabled the synthesis of functionalized

  具有羟甲基官能团的 2,5-二酮哌嗪 (DKP) 是许多生物活性分子和功能材料中的必需结构。我们已经建立了一个简单的协议，用于通过二硼酸酐催化的羟基定向肽键形成简明合成此类 DKP。本报告中的连续反应由三个步骤组成，其中水是唯一的副产物的分子间催化缩合反应、氮保护基团的简单脱保护和分子内环化，使功能化 DKPs 的合成成为可能。无需任何中间纯化即可获得优异的产量。该协议的效用已通过合成天然产物、phomamide 和 Cyclo(Deala- l -Leu) 得到证明。