dimethyl 3-tert-butoxycarbonylamino-1,2,3,4-tetrahydronaphthalene-2-phosphonate | 913394-34-0

• 分子结构分类: 有机化合物 - 苯类化合物 - 茚满类
• 英文名称: dimethyl 3-tert-butoxycarbonylamino-1,2,3,4-tetrahydronaphthalene-2-phosphonate
• CAS: 913394-34-0
• 化学式: C₁₇H₂₆NO₅P
• 分子量: 355.371
• InChiKey: MKAZLYGZTWCOPO-UHFFFAOYSA-N

反应信息

• 作为反应物：
  描述：

  dimethyl 3-tert-butoxycarbonylamino-1,2,3,4-tetrahydronaphthalene-2-phosphonate 在 氢溴酸 、 溶剂黄146 作用下， 反应 2.0h， 以70%的产率得到3-amino-1,2,3,4-tetrahydronaphthalene-2-phosphonic acid hydrobromide
  参考文献：
  名称：

  Synthesis and structure activity relationships of novel non-peptidic metallo-aminopeptidase inhibitors

  摘要：

  Racemic derivatives of 3-amino-2-tetralone were synthesised and evaluated for their ability to inhibit metallo-aminopeptidase activities. New compounds substituted in position 2 by methyl ketone, substituted oximes or hydroxamic acids as well as heterocyclic derivatives were evaluated against representative members of zinc-dependent aminopeptidases: leucine aminopeptidase (E.C. 3.4.11.1), aminopeptidase-N(E.C. 3.4.11.2), Aeronumas proteolytica aminopeptidase (E.C. 3.4.11.10), and the aminopeptidase activity of leukotriene A(4) hydrolase (E.C. 3.3.2.6). Several compounds showed K-i values in the low micromolar range against the 'one-zinc' aminopeptidases, while most of them were rather poor inhibitors of the 'two-zinc' enzymes. This interesting selectivity profile may guide the design of new, specific inhibitors of target mammalian aminopeptidases with one active site zinc. (c) 2006 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2006.06.050
• 作为产物：
  描述：

  dimethyl 3-tert-butoxycarbonylamino-3,4-dihydronaphthalene-2-phosphonate 在 platinum(IV) oxide 氢气 作用下， 以 甲醇 为溶剂， 反应 48.0h， 以100%的产率得到dimethyl 3-tert-butoxycarbonylamino-1,2,3,4-tetrahydronaphthalene-2-phosphonate
  参考文献：
  名称：

  Synthesis and structure activity relationships of novel non-peptidic metallo-aminopeptidase inhibitors

  摘要：

  Racemic derivatives of 3-amino-2-tetralone were synthesised and evaluated for their ability to inhibit metallo-aminopeptidase activities. New compounds substituted in position 2 by methyl ketone, substituted oximes or hydroxamic acids as well as heterocyclic derivatives were evaluated against representative members of zinc-dependent aminopeptidases: leucine aminopeptidase (E.C. 3.4.11.1), aminopeptidase-N(E.C. 3.4.11.2), Aeronumas proteolytica aminopeptidase (E.C. 3.4.11.10), and the aminopeptidase activity of leukotriene A(4) hydrolase (E.C. 3.3.2.6). Several compounds showed K-i values in the low micromolar range against the 'one-zinc' aminopeptidases, while most of them were rather poor inhibitors of the 'two-zinc' enzymes. This interesting selectivity profile may guide the design of new, specific inhibitors of target mammalian aminopeptidases with one active site zinc. (c) 2006 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2006.06.050