N-tBOC-L-Ala-L-Ala-L-Phe-1-anthraquinonylhydrazide | 530103-32-3

• 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-tBOC-L-Ala-L-Ala-L-Phe-1-anthraquinonylhydrazide
• 英文别名: tert-butyl N-[(2S)-1-[[(2S)-1-[[(2S)-1-[2-(9,10-dioxoanthracen-1-yl)hydrazinyl]-1-oxo-3-phenylpropan-2-yl]amino]-1-oxopropan-2-yl]amino]-1-oxopropan-2-yl]carbamate
• CAS: 530103-32-3
• 化学式: C₃₄H₃₇N₅O₇
• 分子量: 627.697
• InChiKey: LQLANUPHFBFGEA-DYLHXGEVSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.05
• 重原子数：
  46.0
• 可旋转键数：
  10.0
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.29
• 拓扑面积：
  171.8
• 氢给体数：
  5.0
• 氢受体数：
  8.0

反应信息

• 作为反应物：
  描述：

  N-tBOC-L-Ala-L-Ala-L-Phe-1-anthraquinonylhydrazide 在 氢溴酸 、 溶剂黄146 作用下， 反应 1.0h， 以98%的产率得到L-Ala-L-Ala-L-Phe-1-anthraquinonylhydrazide hydrobromide
  参考文献：
  名称：

  Tripeptide Probes for Tripeptidyl Protease I Production via Gene Transfer

  摘要：

  Tripeptides derived from 5-chloroanthraquinone hydrazide and anthraquinone hydrazide have been prepared as potential reagents to probe cellular expression of tripeptidyl protease I (TPP-I). Attempted chemical synthesis of Gly-L-Pro-L-Ala-chloroanthraquinone hydrazide, a compound that had been reported to serve as a substrate for this enzyme, was complicated by formation of a pyrazoloquinone. In contrast, formation of pyrazoloquinones was not observed during coupling reactions with anthraquinone hydrazide, and several tripeptide derivatives of this compound were prepared. The most attractive probe for TPP-I activity in tests with mouse kidney tissue sections proved to be Gly-L-Pro-L-Ser anthraquinone hydrazide.

  DOI：

  10.1021/jm020525x
• 作为产物：
  描述：

  1-氯蒽醌 在 N-甲基吗啉 、 吡啶 、 盐酸 、 氢溴酸 、 一水合肼 、 溶剂黄146 作用下， 以 四氢呋喃 、 1,4-二氧六环 为溶剂， 反应 50.0h， 生成 N-tBOC-L-Ala-L-Ala-L-Phe-1-anthraquinonylhydrazide
  参考文献：
  名称：

  Tripeptide Probes for Tripeptidyl Protease I Production via Gene Transfer

  摘要：

  Tripeptides derived from 5-chloroanthraquinone hydrazide and anthraquinone hydrazide have been prepared as potential reagents to probe cellular expression of tripeptidyl protease I (TPP-I). Attempted chemical synthesis of Gly-L-Pro-L-Ala-chloroanthraquinone hydrazide, a compound that had been reported to serve as a substrate for this enzyme, was complicated by formation of a pyrazoloquinone. In contrast, formation of pyrazoloquinones was not observed during coupling reactions with anthraquinone hydrazide, and several tripeptide derivatives of this compound were prepared. The most attractive probe for TPP-I activity in tests with mouse kidney tissue sections proved to be Gly-L-Pro-L-Ser anthraquinone hydrazide.

  DOI：

  10.1021/jm020525x

文献信息

• Tripeptide Probes for Tripeptidyl Protease I Production via Gene Transfer
  作者：MeeKyoung Kim、Qinwen Mao、Beverly L. Davidson、David F. Wiemer

  DOI：10.1021/jm020525x

  日期：2003.4.1

  Tripeptides derived from 5-chloroanthraquinone hydrazide and anthraquinone hydrazide have been prepared as potential reagents to probe cellular expression of tripeptidyl protease I (TPP-I). Attempted chemical synthesis of Gly-L-Pro-L-Ala-chloroanthraquinone hydrazide, a compound that had been reported to serve as a substrate for this enzyme, was complicated by formation of a pyrazoloquinone. In contrast, formation of pyrazoloquinones was not observed during coupling reactions with anthraquinone hydrazide, and several tripeptide derivatives of this compound were prepared. The most attractive probe for TPP-I activity in tests with mouse kidney tissue sections proved to be Gly-L-Pro-L-Ser anthraquinone hydrazide.