N-benzyloxycarbonyl-O-(tert-butyl)-L-tyrosine p-nitrophenyl ester | 74293-19-9

• 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-benzyloxycarbonyl-O-(tert-butyl)-L-tyrosine p-nitrophenyl ester
• 英文别名: Cbz-Tyr(t-Bu)-ONp；Z-Tyr(tBu)-ONp；(4-nitrophenyl) (2S)-3-[4-[(2-methylpropan-2-yl)oxy]phenyl]-2-(phenylmethoxycarbonylamino)propanoate
• CAS: 74293-19-9
• 化学式: C₂₇H₂₈N₂O₇
• 分子量: 492.529
• InChiKey: BWXUCVPJRZCJKD-DEOSSOPVSA-N

物化性质

• 沸点：
  663.6±55.0 °C(Predicted)
• 密度：
  1.243±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  5.7
• 重原子数：
  36
• 可旋转键数：
  11
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.26
• 拓扑面积：
  120
• 氢给体数：
  1
• 氢受体数：
  7

反应信息

• 作为反应物：
  描述：

  N-benzyloxycarbonyl-O-(tert-butyl)-L-tyrosine p-nitrophenyl ester 在 palladium on activated charcoal 咪唑 、 氢气 、 三氟乙酸 作用下， 以 二氯甲烷 、 乙二醇甲醚 为溶剂， -10.0~25.0 ℃ 、101.33 kPa 条件下， 反应 49.0h， 生成 1-O-(L-tyrosyl)-α-D-glucopyranose trifluoroacetate
  参考文献：
  名称：

  Synthesis and reactions of d-glucopyranosyl esters of phenylalanine and tyrosine: a study of the diazomethanecatalysed 1→2 acyl migration of the N-acylated α-d anomers

  摘要：

  DOI：

  10.1016/s0008-6215(00)85315-x
• 作为产物：
  描述：

  对硝基苯酚 、 O-(叔丁基)-N-[(苯甲氧基)羰基]-L-酪氨酸 在 N,N'-二环己基碳二亚胺 作用下， 以 乙酸乙酯 为溶剂， 以70%的产率得到N-benzyloxycarbonyl-O-(tert-butyl)-L-tyrosine p-nitrophenyl ester
  参考文献：
  名称：

  Synthesis and reactions of d-glucopyranosyl esters of phenylalanine and tyrosine: a study of the diazomethanecatalysed 1→2 acyl migration of the N-acylated α-d anomers

  摘要：

  DOI：

  10.1016/s0008-6215(00)85315-x

文献信息

• Development of Potent and Selective Phosphinic Peptide Inhibitors of Angiotensin-Converting Enzyme 2
  作者：Andreas Mores、Magdalini Matziari、Fabrice Beau、Philippe Cuniasse、Athanasios Yiotakis、Vincent Dive

  DOI：10.1021/jm701275z

  日期：2008.4.1

  Arimotensin-converting enzyme 2 (ACE2), a recently identified human homologue of angiotensin-converting enzyme, is a zinc metallocarboxypeptidase which may play a unique role in cardiovascular and renal function. Here we report the discovery of potent and selective inhibitors of ACE2, which have been identified by evaluating a series of phosphinic di- and tripeptides of the general formula: Z-Xaa(PO2-CH2)YaaOH and Ac-Zaa-Xaa(PO2-CH2)YaaOH. The most potent inhibitor in this series is a tripeptide that displays a K-i value of 0.4 nM toward ACE2 and is 3 orders of magnitude less potent toward carboxypeptidase A. Phosphinic tripeptides exhibit high potency exclusively when the Xaa position is occupied by a pseudoproline. A model of interaction between one inhibitor of this series and ACE2 suggests that the critical role played by a proline in inhibitors, but also for substrates hydrolysis, may rely on the presence of Tyr(510) in the ACE2 active site.
• KEGLEVIC, D.;GOLES, D.;VALENTEKOVIC, S.;PONGRACIC, M.
  作者：KEGLEVIC, D.、GOLES, D.、VALENTEKOVIC, S.、PONGRACIC, M.

  DOI：——

  日期：——