| Literature DB >> 24012183 |
Benjamin P Fauber1, Peter S Dragovich, Jinhua Chen, Laura B Corson, Charles Z Ding, Charles Eigenbrot, Anthony M Giannetti, Thomas Hunsaker, Sharada Labadie, Yichin Liu, Yingchun Liu, Shiva Malek, David Peterson, Keith Pitts, Steve Sideris, Mark Ultsch, Erica VanderPorten, Jing Wang, BinQing Wei, Ivana Yen, Qin Yue.
Abstract
A 2-amino-5-aryl-pyrazine was identified as an inhibitor of human lactate dehydrogenase A (LDHA) via a biochemical screening campaign. Biochemical and biophysical experiments demonstrated that the compound specifically interacted with human LDHA. Structural variation of the screening hit resulted in improvements in LDHA biochemical inhibition and pharmacokinetic properties. A crystal structure of an improved compound bound to human LDHA was also obtained and it explained many of the observed structure-activity relationships.Entities:
Keywords: Lactate dehydrogenase; Pyrazine; Tumor metabolism; X-ray crystal structure
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Year: 2013 PMID： 24012183 DOI： 10.1016/j.bmcl.2013.08.060
Source DB: PubMed Journal: Bioorg Med Chem Lett ISSN： 0960-894X Impact factor: 2.823