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. Author manuscript; available in PMC: 2012 May 26.
Published in final edited form as: J Med Chem. 2011 May 2;54(10):3581–3594. doi: 10.1021/jm200288r

Table 4.

Binding Affinities at hD2R, hD3R and Chimeric Receptors for Compound 8d

IABN Compound 8d

graphic file with name nihms290427t31.jpg D2 Wild type 0.03 ± 0.004 9,163 ± 3731
graphic file with name nihms290427t32.jpg Chimera A 0.05 ± 0.009 2,369 ± 945
graphic file with name nihms290427t33.jpg Chimera B 0.02 ± 0.004 13.9 ± 1.8
graphic file with name nihms290427t34.jpg Chimera C 0.02 ± 0.006 20.8 ± 3.0
graphic file with name nihms290427t35.jpg Chimera D 0.01 ± 0.003 11.5 ± 2.1
graphic file with name nihms290427t36.jpg Chimera E 0.03 ± 0.001 1.7 ± 0.1
graphic file with name nihms290427t37.jpg Chimera F 0.03 ± 0.011 2.9 ± 0.3
graphic file with name nihms290427t38.jpg D2/D3 E2 loop 0.08 ± 0.007 245 ± 37
graphic file with name nihms290427t39.jpg D3/D2 E2 loop 0.03 ± 0.004 31.5 ± 3.0
graphic file with name nihms290427t40.jpg D3 Wild type 0.04 ± 0.003 5.4 ± 0.6

All of the dissociation constants are expressed as nM and are the mean± S.E.M. For IABN Kd values were obtained by Scatchard analysis of direct binding studies and values for the other compounds are Ki values obtained from competitive radioligand binding analysis. The number of independent experiments performed to obtain the mean values is n ≥ 3 for the chimeric receptors. For the binding of 125I-IABN to D2R wild type n = 10 and for the D3R wild type n = 13. For the binding of 8d to D2R wild type n = 7 and for the D3R wild type n = 5.