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A Myosin V Inhibitor Based on Privileged Chemical Scaffolds

Authors


  • This research was supported by the NIH (GM71772 and GM65933 to T.M.K.; GM071688 and GM071688-03S1 to E.M.D.L.C.). T.M.K. is a Scholar of the Leukemia and Lymphoma Society. H.F.C. was supported by an NIH predoctoral fellowship (F31 DC009143) and, in part, by a grant from the Yale Institute for Quantum Engineering (awarded to E.M.D.L.C.). E.M.D.L.C. is an American Heart Association Established Investigator (0940075N) and an NSF CAREER Award recipient (MCB-0546353). We thank Dr. Benjamin H. Kwok and Dr. Alexander Kelly for providing us with recombinant PLK1 and Aurora kinase.

Abstract

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Switching the motor off: Privileged chemical scaffolds were used as a starting point for the development of a specific chemical inhibitor 1 of myosin V, a key motor protein required for intracellular transport (see picture; ADP=adenosine diphosphate, ATP=adenosine triphosphate). The potency of 1, which does not compete directly with nucleotide binding, is comparable to that of other known motor-protein inhibitors used as probes in chemical biology.

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