![High-throughput virtual screening of novel dihydropyrimidine monastrol analogs reveals robust structure-activity relationship to kinesin Eg5 binding thermodynamics](/rails/active_storage/representations/proxy/eyJfcmFpbHMiOnsibWVzc2FnZSI6IkJBaHBBbklHIiwiZXhwIjpudWxsLCJwdXIiOiJibG9iX2lkIn19--d6c6de458558e4bad89fd55e0c9fc19a0e0453ff/eyJfcmFpbHMiOnsibWVzc2FnZSI6IkJBaDdCem9MWm05eWJXRjBTU0lJY0c1bkJqb0dSVlE2QzNKbGMybDZaVWtpRFRZd01IZzJNREErQmpzR1ZBPT0iLCJleHAiOm51bGwsInB1ciI6InZhcmlhdGlvbiJ9fQ==--33b2b080106a274a4ca568f8742d366d42f20c14/Figure_1.png)
As cancer continues to take millions of lives worldwide, the need to create effective therapeutics for the disease persists. The kinesin Eg5 assembly motor protein is a promising target for cancer therapeutics as inhibition of this protein leads to cell cycle arrest. Monastrol, a small dihydropyrimidine-based molecule capable of inhibiting the kinesin Eg5 function, has attracted the attention of medicinal chemists with its potency, affinity, and specificity to the highly targeted loop5/α2/α3 allosteric binding pocket. In this work, we employed high-throughput virtual screening (HTVS) to identify potential small molecule Eg5 inhibitors from a designed set of novel dihydropyrimidine analogs structurally similar to monastrol.
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