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. Author manuscript; available in PMC: 2013 Jul 1.
Published in final edited form as: ChemMedChem. 2012 May 23;7(7):1286–1294. doi: 10.1002/cmdc.201200104

Table 1.

Biochemical and computational data of compounds tested

Compound R1 R2 R3 R4 IC50
(μM)		 Glide 5.7
XP GScore		 ΔΔGb
(kcal/mol)
1 H F H H 12 ± 1 −7.10
2 H F H OH 4 ± 1 −8.40 −0.55 ± 0.15
3 Cl F H H 18 ± 5 −6.85 3.6 ± 0.16
4 H F H OCH3 19 ± 6 −7.00 −1.25 ± 0.4
5 OH F H H 32 ± 4 −7.97 −1.3 ± 0.27
6 H F H Cl 32 ± 18 −7.04 0.12 ± 0.12
7 H H H Cl 181 ± 85 −7.92 −0.65 ± 0.13
8 H F Cl H 238 ± 91 −6.95 1.9 ± 0.14
9 OCH3 F H H no inhib. −8.46 3.3 ± 0.5
10 H Cl H H no inhib. −7.66 3.9 ± 0.15
11 H H Cl H no inhib. −7.66 2.5± 0.17
15 H H H H n/a n/a −0.53 ± 0.09

IC50 values were determined from the actin polymerization assay. Glide docking scores were calculated with the XP scoring function. Differences in free energies of binding, ΔΔGb, were calculated from the free energy perturbation calculations.