TFA*H-D-Val-D-Ala-D-Leu-Aib-D-Val-D-Ala-D-Leu-OBn | 1207335-54-3

• 分子结构分类: 有机化合物 - 有机聚合物 - 多肽
• 英文名称: TFA*H-D-Val-D-Ala-D-Leu-Aib-D-Val-D-Ala-D-Leu-OBn
• CAS: 1207335-54-3
• 化学式: C₂HF₃O₂*C₃₉H₆₅N₇O₈
• 分子量: 874.011
• InChiKey: GUSLGGIRFAOPHB-USOORVJOSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.45
• 重原子数：
  61.0
• 可旋转键数：
  21.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.66
• 拓扑面积：
  264.22
• 氢给体数：
  8.0
• 氢受体数：
  10.0

反应信息

• 作为反应物：
  描述：

  TFA*H-D-Val-D-Ala-D-Leu-Aib-D-Val-D-Ala-D-Leu-OBn 、 Boc-(R)-β³-hVal-(S)-β³-hAla-(S)-β³-hLeu-(R)-β³-hVal-(S)-β³-hAla-(S)-β³-hLeu-OH 在 1-羟基苯并三唑 、 1-(3-二甲基氨基丙基)-3-乙基碳二亚胺 、 三乙胺 作用下， 以 乙二醇二甲醚 、 氯仿 、 甲醇 为溶剂， 反应 26.0h， 以43%的产率得到Boc-(R)-β³-hVal-(S)-β³-hAla-(S)-β³-hLeu-(R)-β³-hVal-(S)-β³-hAla-(S)-β³-hLeu-D-Val-D-Ala-D-Leu-Aib-D-Val-D-Ala-D-Leu-OBn
  参考文献：
  名称：

  β-Peptide Conjugates: Syntheses and CD and NMR Investigations of β/α-Chimeric Peptides, of a DPA-β-Decapeptide, and of a PEGylated β-Heptapeptide

  摘要：

  Abstractβ3‐Peptides consisting of six, seven, and ten homologated proteinogenic amino acid residues have been attached to an α‐heptapeptide (all d‐amino acid residues; 4), to a hexaethylene glycol chain (PEGylation; 5c), and to dipicolinic acid (DPA derivative 6), respectively. The conjugation of the β‐peptides with the second component was carried out through the N‐termini in all three cases. According to NMR analysis (CD3OH solutions), the (M)‐314‐helical structure of the β‐peptidic segments was unscathed in all three chimeric compounds (Figs. 2, 4, and 5). The α‐peptidic section of the α/β‐peptide was unstructured, and so was the oligoethylene glycol chain in the PEGylated compound. Thus, neither does the appendage influence the β‐peptidic secondary structure, nor does the latter cause any order in the attached oligomers to be observed by this method of analysis. A similar conclusion may be drawn from CD spectra (Figs. 1, 3, and 5). These results bode well for the development of delivery systems involving β‐peptides.

  DOI：

  10.1002/hlca.200900325
• 作为产物：
  描述：

  Boc-D-Val-D-Ala-D-Leu-Aib-D-Val-D-Ala-D-Leu-OBn 、 三氟乙酸 以 二氯甲烷 为溶剂， 反应 2.0h， 以0.35 g的产率得到TFA*H-D-Val-D-Ala-D-Leu-Aib-D-Val-D-Ala-D-Leu-OBn
  参考文献：
  名称：

  β-Peptide Conjugates: Syntheses and CD and NMR Investigations of β/α-Chimeric Peptides, of a DPA-β-Decapeptide, and of a PEGylated β-Heptapeptide

  摘要：

  Abstractβ3‐Peptides consisting of six, seven, and ten homologated proteinogenic amino acid residues have been attached to an α‐heptapeptide (all d‐amino acid residues; 4), to a hexaethylene glycol chain (PEGylation; 5c), and to dipicolinic acid (DPA derivative 6), respectively. The conjugation of the β‐peptides with the second component was carried out through the N‐termini in all three cases. According to NMR analysis (CD3OH solutions), the (M)‐314‐helical structure of the β‐peptidic segments was unscathed in all three chimeric compounds (Figs. 2, 4, and 5). The α‐peptidic section of the α/β‐peptide was unstructured, and so was the oligoethylene glycol chain in the PEGylated compound. Thus, neither does the appendage influence the β‐peptidic secondary structure, nor does the latter cause any order in the attached oligomers to be observed by this method of analysis. A similar conclusion may be drawn from CD spectra (Figs. 1, 3, and 5). These results bode well for the development of delivery systems involving β‐peptides.

  DOI：

  10.1002/hlca.200900325