N-tBOC-L-Ala-1-anthraquinonylhydrazide | 530103-17-4

• 分子结构分类: 有机化合物 - 苯类化合物 - 蒽
• 英文名称: N-tBOC-L-Ala-1-anthraquinonylhydrazide
• 英文别名: tert-butyl N-[(2S)-1-[2-(9,10-dioxoanthracen-1-yl)hydrazinyl]-1-oxopropan-2-yl]carbamate
• CAS: 530103-17-4
• 化学式: C₂₂H₂₃N₃O₅
• 分子量: 409.442
• InChiKey: LXLLEFKSBZRIEK-LBPRGKRZSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.82
• 重原子数：
  30.0
• 可旋转键数：
  4.0
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.27
• 拓扑面积：
  113.6
• 氢给体数：
  3.0
• 氢受体数：
  6.0

反应信息

• 作为反应物：
  描述：

  N-tBOC-L-Ala-1-anthraquinonylhydrazide 在 盐酸 作用下， 以 1,4-二氧六环 为溶剂， 反应 1.0h， 以98%的产率得到L-Ala-1-anthraquinonylhydrazide hydrochloride
  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 、 一水合肼 作用下， 以 四氢呋喃 为溶剂， 反应 16.0h， 生成 N-tBOC-L-Ala-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.
• EDC-mediated condensations of 1-chloro-5-hydrazino-9,10-anthracenedione, 1-hydrazino-9,10-anthracenedione, and the corresponding anthrapyrazoles
  作者：MeeKyoung Kim、David F Wiemer

  DOI：10.1016/j.tetlet.2004.04.041

  日期：2004.6

  The EDC-mediated condensation of 1-chloro-5-hydrazino-9,10-anthracenedione afforded an N-1 acyl anthrapyrazole instead of the expected hydrazide. The regiochemistry of the N-acyl substituent was assigned on the basis of an extensive set of NMR experiments, and identification of this isomer Suggests a reaction sequence based on initial acylation and Subsequent cyclization. In contrast, the parallel reaction of 1-hydrazino-9,10-anthracenedione proceeded to afford the expected hydrazide. (C) 2004 Elsevier Ltd. All rights reserved.