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Significance Kinesin motor proteins are central to cellular processes and considered good drug targets, but very few reported kinesin inhibitors exhibit potential as drugs. Adociasulfates uniquely inhibit kinesins by competing with microtubules for binding. A declining interest in these compounds resulted from a report of large aggregates of adociasulfate-2 responsible for kinesin inhibition, poor cell permeability, and broad kinesin inhibition, limiting potential therapeutic applications. In this study, we show that kinesin inhibition is likely a 1:1 interaction and does not involve aggregates. We suggest a means by which cell permeability may be improved and show that adociasulfates inhibit kinesin-1 and -5 families of motors to a significantly different extent. These results collectively bring adociasulfates back to the foreground of chemical biology.

Single-molecule inhibition of human kinesin by adociasulfate-13 and -14 from the spongeCladocroce aculeata