(3R,6S,12S,15S)-15-tert-Butoxycarbonylamino-12-((S)-sec-butyl)-6-isobutyl-9-methylene-5,8,11,14-tetraoxo-1-thia-4,7,10,13-tetraaza-cyclohexadecane-3-carboxylic acid | 141697-87-2

• 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: (3R,6S,12S,15S)-15-tert-Butoxycarbonylamino-12-((S)-sec-butyl)-6-isobutyl-9-methylene-5,8,11,14-tetraoxo-1-thia-4,7,10,13-tetraaza-cyclohexadecane-3-carboxylic acid
• CAS: 141697-87-2
• 化学式: C₂₆H₄₃N₅O₈S
• 分子量: 585.722
• InChiKey: BIPDLRGOVJYMTL-UJCHZGTJSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.89
• 重原子数：
  40.0
• 可旋转键数：
  6.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.69
• 拓扑面积：
  192.03
• 氢给体数：
  6.0
• 氢受体数：
  8.0

反应信息

• 作为反应物：
  描述：

  (3R,6S,12S,15S)-15-tert-Butoxycarbonylamino-12-((S)-sec-butyl)-6-isobutyl-9-methylene-5,8,11,14-tetraoxo-1-thia-4,7,10,13-tetraaza-cyclohexadecane-3-carboxylic acid 在 1-羟基苯并三唑 、 1-(3-二甲基氨基丙基)-3-乙基碳二亚胺 、 三氟乙酸 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 0.5h， 生成 (3R,6S,12S,15S)-15-Amino-12-((S)-sec-butyl)-6-isobutyl-9-methylene-5,8,11,14-tetraoxo-1-thia-4,7,10,13-tetraaza-cyclohexadecane-3-carboxylic acid methylamide
  参考文献：
  名称：

  Effects of dehydroalanine on peptide conformations

  摘要：

  The conformational preferences of dehydroalanine were examined through a combined approach of X-ray diffraction, NMR spectroscopy, and molecular modeling. Monte Carlo simulated annealing was used in conjunction with X-ray diffraction data and semiempirical quantum mechanical calculations to determine appropriate parameters for modeling dehydroalanine with the DISCOVER consistent valence force field. The two molecules in the asymmetric unit of N-acetyldehydroalanine N'-methylamide were simulated in the crystalline environment using these optimized parameters. The rms deviations between simulation and experimental data for heavy atom bond lengths, bond angles, and torsions were 0.021 angstrom, 1.9-degrees, and 8.7-degrees, respectively. The dehydroalanine-containing ring A fragment of nisin and two analogs with either L- or D-alanine substituted for dehydroalanine were synthesized and examined by NMR spectroscopy. Using distance geometry followed by conformational energy minimization with our optimized parameters, families of conformations were determined for each molecule which satisfied the observed backbone NOE, J(alpha-N) coupling constants, and temperature coefficients. Dehydroalanine adopted a roughly planar conformation, with trans orientations for the phi and psi-torsions, and induced an inverse gamma-turn in the preceding residue. Similar effects have been observed for linear, dehydroalanine-containing peptides in solution and as crystals, suggesting that dehydroalanine exerts a powerful conformational influence independent of other constraints. The conformational preferences of the L- and D-Ala ring A analogs differed substantially from each other and from the ring A fragment.

  DOI：

  10.1021/ja00040a024
• 作为产物：
  描述：

  Boc-D-Ala-S(-Ile-Dha-Leu-)-Ala-OMe 在 sodium hydroxide 作用下， 以 1,4-二氧六环 为溶剂， 以55.2%的产率得到(3R,6S,12S,15S)-15-tert-Butoxycarbonylamino-12-((S)-sec-butyl)-6-isobutyl-9-methylene-5,8,11,14-tetraoxo-1-thia-4,7,10,13-tetraaza-cyclohexadecane-3-carboxylic acid
  参考文献：
  名称：

  Effects of dehydroalanine on peptide conformations

  摘要：

  The conformational preferences of dehydroalanine were examined through a combined approach of X-ray diffraction, NMR spectroscopy, and molecular modeling. Monte Carlo simulated annealing was used in conjunction with X-ray diffraction data and semiempirical quantum mechanical calculations to determine appropriate parameters for modeling dehydroalanine with the DISCOVER consistent valence force field. The two molecules in the asymmetric unit of N-acetyldehydroalanine N'-methylamide were simulated in the crystalline environment using these optimized parameters. The rms deviations between simulation and experimental data for heavy atom bond lengths, bond angles, and torsions were 0.021 angstrom, 1.9-degrees, and 8.7-degrees, respectively. The dehydroalanine-containing ring A fragment of nisin and two analogs with either L- or D-alanine substituted for dehydroalanine were synthesized and examined by NMR spectroscopy. Using distance geometry followed by conformational energy minimization with our optimized parameters, families of conformations were determined for each molecule which satisfied the observed backbone NOE, J(alpha-N) coupling constants, and temperature coefficients. Dehydroalanine adopted a roughly planar conformation, with trans orientations for the phi and psi-torsions, and induced an inverse gamma-turn in the preceding residue. Similar effects have been observed for linear, dehydroalanine-containing peptides in solution and as crystals, suggesting that dehydroalanine exerts a powerful conformational influence independent of other constraints. The conformational preferences of the L- and D-Ala ring A analogs differed substantially from each other and from the ring A fragment.

  DOI：

  10.1021/ja00040a024