Boc-βPhe-Leu-Val-Val-OMe | 500997-47-7

• 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: Boc-βPhe-Leu-Val-Val-OMe
• CAS: 500997-47-7
• 化学式: C₃₂H₅₂N₄O₇
• 分子量: 604.787
• InChiKey: XYCZRQMZNHFJFB-DROSFRCNSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.5
• 重原子数：
  43.0
• 可旋转键数：
  15.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.66
• 拓扑面积：
  151.93
• 氢给体数：
  4.0
• 氢受体数：
  7.0

反应信息

• 作为反应物：
  描述：

  Boc-βPhe-Leu-Val-Val-OMe 在 甲酸 作用下， 反应 48.0h， 生成 Boc-Leu-Val-Val-^DPro-βPhe-Leu-Val-Val-OMe
  参考文献：
  名称：

  -Hairpins Generated from Hybrid Peptide Sequences Containing both - and -Amino Acids

  摘要：

  The incorporation of the P-amino acid residues into specific positions in the strands and U-turn segments of peptide hairpins is being systematically explored. The presence of an additional torsion variable about the C(alpha)-C(beta) bond (theta) enhances the conformational repertoire in beta-residues. The conformational analysis of three designed peptide hairpins composed of alpha/beta-hybrid segments is described: Boc-Leu-Val-Val-(D)Pro-betaPhe-Leu-Val-Val-OMe (1), Boc-Leu-Vil-betaVal-(D)Pro-Gly-betaLeu-Val-Val-OMe (2). and Boc-Lcu-Val-betaPhe-Val-(D)Pro-Gly-Leu-betaPhe-Val-Val-OMe (3). 500-MHz H-1-NMR Analysis supports a preponderance of beta-hairpin conformation in solution for all three peptides, with critical cross-strand NOEs providing evidence for the proposed structures. The crystal structure of peptide 2 reveals a beta-hairpin conformation with two beta-residues occupying facing, non-H-bonded positions in antiparallel beta-strands. Notably, betaVal(3) adopts a gauche conformation about the C(alpha)-C(beta) bond (theta = + 65degrees) without disturbing cross-strand H-bonding. The crystal structure of 2, together with previously published crystal structures of peptides 3 and Boc-Phe-betaPhe-(D)Pro-Gly-betaPhe-betaPhe-OMe, provide an opportunity to visualize the packing of peptide sheets with local 'polar segments' formed as a consequence of reversal peptide-bond orientation. The available structural evidence for hairpins suggests that beta-residues can be accommodated into nucleating turn segments and into both the H-bonding and non-H-bonding positions on the strands.

  DOI：

  10.1002/1522-2675(200210)85:10<3313::aid-hlca3313>3.0.co;2-p
• 作为产物：
  描述：

  (S)-methyl 2-((S)-2-(tert-butoxycarbonylamino)-3-methylbutanamido)-3-methylbutanoate 在 甲酸 作用下， 反应 44.0h， 生成 Boc-βPhe-Leu-Val-Val-OMe
  参考文献：
  名称：

  -Hairpins Generated from Hybrid Peptide Sequences Containing both - and -Amino Acids

  摘要：

  The incorporation of the P-amino acid residues into specific positions in the strands and U-turn segments of peptide hairpins is being systematically explored. The presence of an additional torsion variable about the C(alpha)-C(beta) bond (theta) enhances the conformational repertoire in beta-residues. The conformational analysis of three designed peptide hairpins composed of alpha/beta-hybrid segments is described: Boc-Leu-Val-Val-(D)Pro-betaPhe-Leu-Val-Val-OMe (1), Boc-Leu-Vil-betaVal-(D)Pro-Gly-betaLeu-Val-Val-OMe (2). and Boc-Lcu-Val-betaPhe-Val-(D)Pro-Gly-Leu-betaPhe-Val-Val-OMe (3). 500-MHz H-1-NMR Analysis supports a preponderance of beta-hairpin conformation in solution for all three peptides, with critical cross-strand NOEs providing evidence for the proposed structures. The crystal structure of peptide 2 reveals a beta-hairpin conformation with two beta-residues occupying facing, non-H-bonded positions in antiparallel beta-strands. Notably, betaVal(3) adopts a gauche conformation about the C(alpha)-C(beta) bond (theta = + 65degrees) without disturbing cross-strand H-bonding. The crystal structure of 2, together with previously published crystal structures of peptides 3 and Boc-Phe-betaPhe-(D)Pro-Gly-betaPhe-betaPhe-OMe, provide an opportunity to visualize the packing of peptide sheets with local 'polar segments' formed as a consequence of reversal peptide-bond orientation. The available structural evidence for hairpins suggests that beta-residues can be accommodated into nucleating turn segments and into both the H-bonding and non-H-bonding positions on the strands.

  DOI：

  10.1002/1522-2675(200210)85:10<3313::aid-hlca3313>3.0.co;2-p