methyl (2S)-2-[[(4R)-4-[(2-methylpropan-2-yl)oxycarbonylamino]-3-oxo-5-phenylpentanoyl]amino]-3-phenylpropanoate | 1450615-23-2

• 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: methyl (2S)-2-[[(4R)-4-[(2-methylpropan-2-yl)oxycarbonylamino]-3-oxo-5-phenylpentanoyl]amino]-3-phenylpropanoate
• CAS: 1450615-23-2
• 化学式: C₂₆H₃₂N₂O₆
• 分子量: 468.55
• InChiKey: PCPJGKINWCFPDZ-RTWAWAEBSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4
• 重原子数：
  34
• 可旋转键数：
  13
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.38
• 拓扑面积：
  111
• 氢给体数：
  2
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  methyl (2S)-2-[[(4R)-4-[(2-methylpropan-2-yl)oxycarbonylamino]-3-oxo-5-phenylpentanoyl]amino]-3-phenylpropanoate 在 盐酸 作用下， 以 乙酸乙酯 为溶剂， 生成
  参考文献：
  名称：

  Novel β-dicarbonyl derivatives as inhibitors of aminopeptidase N (APN)

  摘要：

  Most zinc metalloproteases are over-expressed in tumor cells and play a critical role in the genesis, development, and metastasis of tumors. Novel zinc binding groups (ZBGs) represent a novel strategy to obtain optimal potency and selectivity for zinc metalloproteases inhibitors. Here we described the design, synthesis, and biological studies of novel p-dicarbonyl derivatives as aminopeptidase N (APN/CD13) inhibitors. The results demonstrated that some compounds exhibited moderate to good inhibitory activities against APN with compound 5c being the most potent, suggesting that 5c could serve as new lead for the future APN inhibitor development. The results further confirm our design rationale of P-dicarbonyl moiety as a new ZBG, which may provide a new direction for the design and discovery of zinc metalloproteases inhibitors as new anti-tumor agents. Crown Copyright (C) 2013 Published by Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2013.06.058
• 作为产物：
  描述：

  Boc-D-苯丙氨酸 在 4-二甲氨基吡啶 、 盐酸-N-乙基-Nˊ-(3-二甲氨基丙基)碳二亚胺 作用下， 以 二氯甲烷 、 乙腈 为溶剂， 反应 2.0h， 生成 methyl (2S)-2-[[(4R)-4-[(2-methylpropan-2-yl)oxycarbonylamino]-3-oxo-5-phenylpentanoyl]amino]-3-phenylpropanoate
  参考文献：
  名称：

  Novel β-dicarbonyl derivatives as inhibitors of aminopeptidase N (APN)

  摘要：

  Most zinc metalloproteases are over-expressed in tumor cells and play a critical role in the genesis, development, and metastasis of tumors. Novel zinc binding groups (ZBGs) represent a novel strategy to obtain optimal potency and selectivity for zinc metalloproteases inhibitors. Here we described the design, synthesis, and biological studies of novel p-dicarbonyl derivatives as aminopeptidase N (APN/CD13) inhibitors. The results demonstrated that some compounds exhibited moderate to good inhibitory activities against APN with compound 5c being the most potent, suggesting that 5c could serve as new lead for the future APN inhibitor development. The results further confirm our design rationale of P-dicarbonyl moiety as a new ZBG, which may provide a new direction for the design and discovery of zinc metalloproteases inhibitors as new anti-tumor agents. Crown Copyright (C) 2013 Published by Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2013.06.058

文献信息

• Novel β-dicarbonyl derivatives as inhibitors of aminopeptidase N (APN)
  作者：Chunhua Ma、Xiaoguang Li、Xuewu liang、Kang Jin、Jiangying Cao、Wenfang Xu

  DOI：10.1016/j.bmcl.2013.06.058

  日期：2013.9

  Most zinc metalloproteases are over-expressed in tumor cells and play a critical role in the genesis, development, and metastasis of tumors. Novel zinc binding groups (ZBGs) represent a novel strategy to obtain optimal potency and selectivity for zinc metalloproteases inhibitors. Here we described the design, synthesis, and biological studies of novel p-dicarbonyl derivatives as aminopeptidase N (APN/CD13) inhibitors. The results demonstrated that some compounds exhibited moderate to good inhibitory activities against APN with compound 5c being the most potent, suggesting that 5c could serve as new lead for the future APN inhibitor development. The results further confirm our design rationale of P-dicarbonyl moiety as a new ZBG, which may provide a new direction for the design and discovery of zinc metalloproteases inhibitors as new anti-tumor agents. Crown Copyright (C) 2013 Published by Elsevier Ltd. All rights reserved.