TFA*H-(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-OH | 1207335-39-4

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 肽模拟物
• 英文名称: TFA*H-(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-OH
• CAS: 1207335-39-4
• 化学式: C₂HF₃O₂*C₆₆H₁₂₁N₁₃O₁₄
• 分子量: 1434.79
• InChiKey: VVYXPSLNJVPFKW-LGSHQMFKSA-N

反应信息

• 作为产物：
  描述：

  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-OH 、 三氟乙酸 以 二氯甲烷 为溶剂， 反应 2.0h， 以100%的产率得到TFA*H-(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-OH
  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