A series of apomorphine ((-)-1, APO)-derived analogues ((+/-)-3, (-)-4-(-)-6) were designed and synthesized by hybridizing APO with a privileged 2-aminothiazole functionality which was lent from the orally available anti-parkinsonian drug, pramipexole (2). Among these hybridized compounds, catecholic aporphine (-)-6 shows good affinity at the D(2) receptor with K(i) of 328nM, slightly less potent (3-fold), but more selective against the D(1) receptor than that of the parent compound, APO. Although possessing reduced affinity at the D(2) receptor, aporphines 15 and 18 show significant potency at both the D(1) and 5-HT(1A) receptors. The former compound is equipotent at both receptors (K(i): 116 and 151nM, respectively), while the latter is 8-fold more potent at the D(1) (K(i): 78nM) than at the 5-HT(1A) receptors (K(i): 640nM). These results indicate that the catechol fragment is critical for the D(2) receptor binding of the anti-parkinsonian drug, APO ((-)-1), but not necessary for binding at the D(1) and 5-HT(1A) receptors.