RESUMO
Drug discovery in universities is usually associated with research on drug targets and mechanisms, but more recently there have been efforts to progress from target studies to proof of concept by applying commercially focussed medicinal chemistry. This creates more opportunities for novel interactions and partnering models between academic groups and pharmaceutical companies. We present a review of coordinated, multi-institutional drug discovery operations within academia that are engaging with industry nationally and internationally and describe how the Drug Discovery Portal at the University of Strathclyde enhances the possibilities for academic drug discovery.
Assuntos
Química Farmacêutica/métodos , Desenho de Fármacos , Descoberta de Drogas/métodos , Comportamento Cooperativo , Sistemas de Liberação de Medicamentos , Indústria Farmacêutica/organização & administração , Preparações Farmacêuticas/química , Projetos de Pesquisa , Escócia , UniversidadesRESUMO
The Drug Discovery Portal (DDP) is a research initiative based at the University of Strathclyde in Glasgow, Scotland. It was initiated in 2007 by a group of researchers with expertise in virtual screening. Academic research groups in the university working in drug discovery programmes estimated there was a historical collection of physical compounds going back 50 years that had never been adequately catalogued. This invaluable resource has been harnessed to form the basis of the DDP library, and has attracted a high-percentage uptake from the Universities and Research Groups internationally. Its unique attributes include the diversity of the academic database, sourced from synthetic, medicinal and phytochemists working an academic laboratories and the ability to link biologists with appropriate chemical expertise through a target-matching virtual screening approach, and has resulted in seven emerging hit development programmes between international contributors.
Assuntos
Descoberta de Drogas/métodos , Bases de Dados Factuais , Desenho de Fármacos , Descoberta de Drogas/educação , Estrutura Molecular , Projetos de Pesquisa , Escócia , Tecnologia Farmacêutica/educação , UniversidadesRESUMO
A new series of non-peptidic, mono-acid protein tyrosine phosphatase 1B (PTP1B) inhibitors has been identified by structure-based design. Compounds with 2-(indol-3-yl)- and 2-phenyl-3,3,3-trifluoro-2-hydroxypropionic acid core units targeted at the enzyme's primary site and a hydrophobic chlorophenylthiazole extension in its 2 degrees site exhibit 3-60microM IC(50)s for PTP1B inhibition in an Sf9 cell-based assay.
