(S)-2-[(R)-2-((S)-2-tert-Butoxycarbonylamino-4-methyl-pentanoylamino)-propionylamino]-3-methyl-butyric acid | 186267-34-5

• 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: (S)-2-[(R)-2-((S)-2-tert-Butoxycarbonylamino-4-methyl-pentanoylamino)-propionylamino]-3-methyl-butyric acid
• 英文别名: Boc-Leu-D-Ala-Val-OH；(2S)-3-methyl-2-[[(2R)-2-[[(2S)-4-methyl-2-[(2-methylpropan-2-yl)oxycarbonylamino]pentanoyl]amino]propanoyl]amino]butanoic acid
• CAS: 186267-34-5
• 化学式: C₁₉H₃₅N₃O₆
• 分子量: 401.503
• InChiKey: ZNLCNUGCEROBQD-RDBSUJKOSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.9
• 重原子数：
  28
• 可旋转键数：
  11
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.79
• 拓扑面积：
  134
• 氢给体数：
  4
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  (S)-2-[2-((S)-2-Amino-4-methyl-pentanoylamino)-2-methyl-propionylamino]-3-methyl-butyric acid methyl ester 、 (S)-2-[(R)-2-((S)-2-tert-Butoxycarbonylamino-4-methyl-pentanoylamino)-propionylamino]-3-methyl-butyric acid 在 1-羟基苯并三唑 、 N,N'-二环己基碳二亚胺 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 96.0h， 生成 (S)-2-[2-((S)-2-{(S)-2-[(R)-2-((S)-2-tert-Butoxycarbonylamino-4-methyl-pentanoylamino)-propionylamino]-3-methyl-butyrylamino}-4-methyl-pentanoylamino)-2-methyl-propionylamino]-3-methyl-butyric acid methyl ester
  参考文献：
  名称：

  Conformational variability in short acyclic peptides. Stabilization of multiple β-turn structures in organic solvents

  摘要：

  The conformational characteristics of three hexapeptides Boc-Leu-Xxx-Val-Leu-Aib-Val-OMe (Xxx = Ala 1, D-Ala 2, Gly 3; Aib = alpha-aminoisobutyryl) have been probed in CDCl3 solution by NMR methods using solvent perturbation of chemical shifts and radical broadening of NH resonances to delineate intramolecularly hydrogen bonded NH groups, Nuclear Overhauser effects (NOEs) provide additional information on preferred backbone conformations, The substituent at position 2 acts as a major conformational determinant, While a continuous 3(10) helical conformation is favoured for the peptide with Xxx = Ala, a multiple beta-turns conformation is supported by both NMR and CD data for the peptide with Xxx = D-Ala, In the peptide with Xxx = Gly CD and NMR data suggest that both 3(10) helical and multiple turns conformations are simultaneously populated, The results suggest that incorporation of D-amino acids and Aib residues into all L-sequences may prove useful in generating sequences containing multiple turns.

  DOI：

  10.1039/p29960002701
• 作为产物：
  描述：

  Boc-D-Ala-Val-OMe 在 sodium hydroxide 、 甲酸 、 1-羟基苯并三唑 、 N,N'-二环己基碳二亚胺 作用下， 以 甲醇 、 N,N-二甲基甲酰胺 为溶剂， 反应 48.0h， 生成 (S)-2-[(R)-2-((S)-2-tert-Butoxycarbonylamino-4-methyl-pentanoylamino)-propionylamino]-3-methyl-butyric acid
  参考文献：
  名称：

  Conformational variability in short acyclic peptides. Stabilization of multiple β-turn structures in organic solvents

  摘要：

  The conformational characteristics of three hexapeptides Boc-Leu-Xxx-Val-Leu-Aib-Val-OMe (Xxx = Ala 1, D-Ala 2, Gly 3; Aib = alpha-aminoisobutyryl) have been probed in CDCl3 solution by NMR methods using solvent perturbation of chemical shifts and radical broadening of NH resonances to delineate intramolecularly hydrogen bonded NH groups, Nuclear Overhauser effects (NOEs) provide additional information on preferred backbone conformations, The substituent at position 2 acts as a major conformational determinant, While a continuous 3(10) helical conformation is favoured for the peptide with Xxx = Ala, a multiple beta-turns conformation is supported by both NMR and CD data for the peptide with Xxx = D-Ala, In the peptide with Xxx = Gly CD and NMR data suggest that both 3(10) helical and multiple turns conformations are simultaneously populated, The results suggest that incorporation of D-amino acids and Aib residues into all L-sequences may prove useful in generating sequences containing multiple turns.

  DOI：

  10.1039/p29960002701

文献信息

• Conformational variability in short acyclic peptides. Stabilization of multiple β-turn structures in organic solvents
  作者：Satish Kumar Awasthi、Srinivasa Rao Raghothama、Padmanabhan Balaram

  DOI：10.1039/p29960002701

  日期：——

  The conformational characteristics of three hexapeptides Boc-Leu-Xxx-Val-Leu-Aib-Val-OMe (Xxx = Ala 1, D-Ala 2, Gly 3; Aib = alpha-aminoisobutyryl) have been probed in CDCl3 solution by NMR methods using solvent perturbation of chemical shifts and radical broadening of NH resonances to delineate intramolecularly hydrogen bonded NH groups, Nuclear Overhauser effects (NOEs) provide additional information on preferred backbone conformations, The substituent at position 2 acts as a major conformational determinant, While a continuous 3(10) helical conformation is favoured for the peptide with Xxx = Ala, a multiple beta-turns conformation is supported by both NMR and CD data for the peptide with Xxx = D-Ala, In the peptide with Xxx = Gly CD and NMR data suggest that both 3(10) helical and multiple turns conformations are simultaneously populated, The results suggest that incorporation of D-amino acids and Aib residues into all L-sequences may prove useful in generating sequences containing multiple turns.