tert-butyl N-[(2R)-1-[[(2S)-1-anilino-1-oxo-3-phenylpropan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]carbamate | 184956-21-6

• 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: tert-butyl N-[(2R)-1-[[(2S)-1-anilino-1-oxo-3-phenylpropan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]carbamate
• CAS: 184956-21-6
• 化学式: C₂₆H₃₅N₃O₄
• 分子量: 453.582
• InChiKey: KPXZYDVXRYQNQF-YADHBBJMSA-N

物化性质

• 沸点：
  693.8±55.0 °C(Predicted)
• 密度：
  1.131±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  4.29
• 重原子数：
  33.0
• 可旋转键数：
  9.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.42
• 拓扑面积：
  96.53
• 氢给体数：
  3.0
• 氢受体数：
  4.0

反应信息

• 作为反应物：
  描述：

  tert-butyl N-[(2R)-1-[[(2S)-1-anilino-1-oxo-3-phenylpropan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]carbamate 在 盐酸 作用下， 以 1,4-二氧六环 为溶剂， 以95%的产率得到
  参考文献：
  名称：

  Chymotrypsin inhibitory conformation induced by amino acid side chain–side chain intramolecular CH/π interaction

  摘要：

  Dipeptide amides H-D-Leu-Phe-NH-R have been found to assume a conformation induced by the CH/pi interaction and to inhibit chymotrypsin strongly. A series of benzyl amide derivatives H-D-Leu-Phe-NH-[CH2](n)-C6H5 (n = 0-4) have been assayed for chymotrypsin, They inhibit the enzyme in a competitive manner and the highest inhibition is achieved by the amide of n = 1 (K-1 3.6 x 10(-6) M), The activity enhancement is dependent upon the length of methylene chain, not upon the increase in molecular hydrophobicity, indicating the presence of an optimal distance between dipeptide backbone and C-terminal phenyl group for chymotrypsin inhibition, The C-terminal phenyl group has been found to interact with chymotrypsin stereospecifically, The R-isomer of H-D-Leu-Phe-NH-CH(CH3)-C6H5 is as active as the benzyl amide, while the S-isomer is about twenty-fold less active, When the fluorine atom is introduced at a para-position of the C-terminal phenyl group, the resulting dipeptide H-D-Leu-Phe-NH-CH2-C6H4F-p exhibits about six-times increased inhibitory activity (K-1 = 6.1 x 10(-7) M; this dipeptide is one of the most potent chymotrypsin inhibitors to date), H-1 NMR conformational analyses of these dipeptide amide derivatives show the CH/pi: interaction between D-Leu-isobutyl and Phe-phenyl as a key structural element for chymotrypsin inhibition, These structural examinations strongly suggest that in the inhibitory conformation the C-terminal phenyl group fits the chymotrypsin S-1 site, while the hydrophobic core constructed by D-Leu-Phe CH/pi interaction fits the chymotrypsin S-2 or S-1' site.

  DOI：

  10.1039/p19960002479
• 作为产物：
  描述：

  BOC-L-苯丙氨酸 生成 tert-butyl N-[(2R)-1-[[(2S)-1-anilino-1-oxo-3-phenylpropan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]carbamate
  参考文献：
  名称：

  Chymotrypsin inhibitory conformation induced by amino acid side chain–side chain intramolecular CH/π interaction

  摘要：

  Dipeptide amides H-D-Leu-Phe-NH-R have been found to assume a conformation induced by the CH/pi interaction and to inhibit chymotrypsin strongly. A series of benzyl amide derivatives H-D-Leu-Phe-NH-[CH2](n)-C6H5 (n = 0-4) have been assayed for chymotrypsin, They inhibit the enzyme in a competitive manner and the highest inhibition is achieved by the amide of n = 1 (K-1 3.6 x 10(-6) M), The activity enhancement is dependent upon the length of methylene chain, not upon the increase in molecular hydrophobicity, indicating the presence of an optimal distance between dipeptide backbone and C-terminal phenyl group for chymotrypsin inhibition, The C-terminal phenyl group has been found to interact with chymotrypsin stereospecifically, The R-isomer of H-D-Leu-Phe-NH-CH(CH3)-C6H5 is as active as the benzyl amide, while the S-isomer is about twenty-fold less active, When the fluorine atom is introduced at a para-position of the C-terminal phenyl group, the resulting dipeptide H-D-Leu-Phe-NH-CH2-C6H4F-p exhibits about six-times increased inhibitory activity (K-1 = 6.1 x 10(-7) M; this dipeptide is one of the most potent chymotrypsin inhibitors to date), H-1 NMR conformational analyses of these dipeptide amide derivatives show the CH/pi: interaction between D-Leu-isobutyl and Phe-phenyl as a key structural element for chymotrypsin inhibition, These structural examinations strongly suggest that in the inhibitory conformation the C-terminal phenyl group fits the chymotrypsin S-1 site, while the hydrophobic core constructed by D-Leu-Phe CH/pi interaction fits the chymotrypsin S-2 or S-1' site.

  DOI：

  10.1039/p19960002479

文献信息

• Late‐Stage Modification of Oligopeptides by Nickel‐Catalyzed Stereoselective Radical Addition to Dehydroalanine
  作者：Xiaoxu Qi、Subramanian Jambu、Yining Ji、Kevin M. Belyk、Nihar R. Panigrahi、Paramjit S. Arora、Neil A. Strotman、Tianning Diao

  DOI：10.1002/anie.202213315

  日期：2022.11.25

  Radical addition to the dehydroalanine (Dha) residue of a peptide could diversify the peptide sequence with noncanonical residues, but this strategy is currently limited by the lack of control over the stereochemistry. This work addresses this important challenge by applying chiral nickel catalysts to control the stereoselective radical addition to Dha on oligopeptides.

  对肽的脱氢丙氨酸 (Dha) 残基进行自由基添加可以使具有非规范残基的肽序列多样化，但该策略目前由于缺乏对立体化学的控制而受到限制。这项工作通过应用手性镍催化剂来控制寡肽上 Dha 的立体选择性自由基加成，解决了这一重要挑战。