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. Author manuscript; available in PMC: 2012 Aug 17.
Published in final edited form as: J Am Chem Soc. 2011 Jul 21;133(32):12386–12389. doi: 10.1021/ja204561q

Figure 2.

Figure 2

(a) Chemical structure of an ATP-competitive kinesin-5 inhibitor and analogs generated for SILIC. (b) Potency of compounds 1, 2 and 3 in inhibiting kinesin-5 activity, as examined using a steady-state microtubule-stimulated ATP hydrolysis assay. (c) In the presence of MgATP (1 mM) and DMSO, homotetrameric kinesin-5 drives microtubule gliding at an average rate of 19.6 ± 4.5 nm/s (left panel, n > 25). 1 (50nM) inhibits this activity (right panel, n > 30). Scale bar is 2μm.