Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10587566 | Bioorganic & Medicinal Chemistry Letters | 2013 | 7 Pages |
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.
Related Topics
Physical Sciences and Engineering
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Organic Chemistry
Authors
Benjamin P. Fauber, 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,