变构调节
化学
药物发现
恶性疟原虫
小分子
天冬氨酸氨甲酰转移酶
立体化学
亲缘关系
结合位点
药理学
生物化学
疟疾
酶
生物
免疫学
作者
Chao Wang,Bidong Zhang,Arne Krüger,Xiaochen Du,Lidia Visser,Alexander Dömlingꝉ,Carsten Wrenger,Matthew R. Groves
摘要
The discovery and development of new drugs against malaria remain urgent. Aspartate transcarbamoylase (ATC) has been suggested to be a promising target for antimalarial drug development. Here, we describe a series of small-molecule inhibitors of P. falciparum ATC with low nanomolar binding affinities that selectively bind to a previously unreported allosteric pocket, thereby inhibiting ATC activation. We demonstrate that the buried allosteric pocket is located close to the traditional ATC active site and that reported compounds maintain the active site of PfATC in its low substrate affinity/low activity conformation. These compounds inhibit parasite growth in blood stage cultures at single digit micromolar concentrations, whereas limited effects were seen against human normal lymphocytes. To our knowledge, this series represent the first PfATC-specific allosteric inhibitors.
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