Your browser doesn't support javascript.
loading
4-amino-5-aryl-6-arylethynylpyrimidines: structure-activity relationships of non-nucleoside adenosine kinase inhibitors.
Matulenko, Mark A; Paight, Ernest S; Frey, Robin R; Gomtsyan, Arthur; DiDomenico, Stanley; Jiang, Meiqun; Lee, Chih-Hung; Stewart, Andrew O; Yu, Haixia; Kohlhaas, Kathy L; Alexander, Karen M; McGaraughty, Steve; Mikusa, Joseph; Marsh, Kennan C; Muchmore, Steven W; Jakob, Clarissa L; Kowaluk, Elizabeth A; Jarvis, Michael F; Bhagwat, Shripad S.
Afiliación
  • Matulenko MA; Neuroscience Research, Global Pharmaceutical Research Abbott Laboratories, 100 Abbott Park Road, Abbott Park, IL 60064, USA. mark.a.matulenko@abbott.com
Bioorg Med Chem ; 15(4): 1586-605, 2007 Feb 15.
Article en En | MEDLINE | ID: mdl-17197188
A series of non-nucleoside adenosine kinase (AK) inhibitors is reported. These inhibitors originated from the modification of 5-(3-bromophenyl)-7-(6-morpholin-4-ylpyridin-3-yl)pyrido[2,3-d]pyrimidin-4-ylamine (ABT-702). The identification of a linker that would approximate the spatial arrangement found between the pyrimidine ring and the aryl group at C(7) in ABT-702 was a key element in this modification. A search of potential linkers led to the discovery of an acetylene moiety as a suitable scaffold. It was hypothesized that the aryl acetylenes, ABT-702, and adenosine bound to the active site of AK (closed form) in a similar manner with respect to the orientation of the heterocyclic base. Although potent acetylene analogs were discovered based on this assumption, an X-ray crystal structure of 5-(4-dimethylaminophenyl)-6-(6-morpholin-4-ylpyridin-3-ylethynyl)pyrimidin-4-ylamine (16a) revealed a binding orientation contrary to adenosine. In addition, this compound bound tightly to a unique open conformation of AK. The structure-activity relationships and unique ligand orientation and protein conformation are discussed.
Asunto(s)
Buscar en Google
Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Pirimidinas / Adenosina Quinasa Límite: Animals Idioma: En Revista: Bioorg Med Chem Asunto de la revista: BIOQUIMICA / QUIMICA Año: 2007 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Reino Unido
Buscar en Google
Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Pirimidinas / Adenosina Quinasa Límite: Animals Idioma: En Revista: Bioorg Med Chem Asunto de la revista: BIOQUIMICA / QUIMICA Año: 2007 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Reino Unido