N-butyl-phenylalaninamide | 1217886-75-3

• 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: N-butyl-phenylalaninamide
• 英文别名: N-Bu-Phe-NH2；(2S)-2-(butylamino)-3-phenylpropanamide
• CAS: 1217886-75-3
• 化学式: C₁₃H₂₀N₂O
• 分子量: 220.315
• InChiKey: FFLQMPFPTLQVTQ-LBPRGKRZSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2
• 重原子数：
  16
• 可旋转键数：
  7
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.46
• 拓扑面积：
  55.1
• 氢给体数：
  2
• 氢受体数：
  2

反应信息

• 作为产物：
  描述：

  L-苯丙氨酰胺 、 正丁醛 在 甲醇 、 sodium tetrahydroborate 作用下， 以 甲醇 为溶剂， 反应 0.25h， 以43.5%的产率得到N-butyl-phenylalaninamide
  参考文献：
  名称：

  Chemical Models of Peptide Formation in Translation

  摘要：

  Ribosomal incorporations of N-alkyl amino acids including proline are slower than incorporations of non-N-alkyl L-amino acids. The chemical reactivity hypothesis proposes that these results and the exclusion of nonproline N-alkyl amino acids from the genetic code are explained by intrinsic chemical reactivities of the amino and nucleophiles. However, there is little data on the reactivities relevant to physiological conditions. Here, we use nonenzymatic, aqueous-based, buffered reactions with formylmethionine-N-hydroxysuccinimide ester to model II amino acid nucleophiles in dipeptide formation. The relative rates in the nonenzymatic and translation systems correlate well. supporting the chemical reactivity hypothesis and arguing that peptide bond formation, not accommodation, is rate limiting, for natural Pro-tRNA(Pro) isoacceptors. The effects of N-substitution sterics, side chain sterics. Induction, and pK(a) were evaluated in the chemical model. The dominant factor affecting relative rates was found to he N-substitution sterics.

  DOI：

  10.1021/bi1000273

文献信息

• Chemical Models of Peptide Formation in Translation
  作者：R. Edward Watts、Anthony C. Forster

  DOI：10.1021/bi1000273

  日期：2010.3.16

  Ribosomal incorporations of N-alkyl amino acids including proline are slower than incorporations of non-N-alkyl L-amino acids. The chemical reactivity hypothesis proposes that these results and the exclusion of nonproline N-alkyl amino acids from the genetic code are explained by intrinsic chemical reactivities of the amino and nucleophiles. However, there is little data on the reactivities relevant to physiological conditions. Here, we use nonenzymatic, aqueous-based, buffered reactions with formylmethionine-N-hydroxysuccinimide ester to model II amino acid nucleophiles in dipeptide formation. The relative rates in the nonenzymatic and translation systems correlate well. supporting the chemical reactivity hypothesis and arguing that peptide bond formation, not accommodation, is rate limiting, for natural Pro-tRNA(Pro) isoacceptors. The effects of N-substitution sterics, side chain sterics. Induction, and pK(a) were evaluated in the chemical model. The dominant factor affecting relative rates was found to he N-substitution sterics.