A series of hetero ring (X) substitued chalcone derivatives with farnesyl protein transferase (FPTase) inhibition activities (pI_(50)) values determined in vitro is analyzed by modified Free-Wilson (F-W) and Hansch method for quantitative structure activity relationship (QSARs). On the basis of F-W analysis on the FPTase inhibitory activity of a training set of the compounds, none of the (X)-substituents were not contribute the activity. But the net charge of α carbon atom is contribute the activity than that of β carbon atom. And the relative orders of the (Y)-substituents on the activity are ortho$gt;meta$gt;para-substituents. According to Hansch approach, the activities would depend largely on the optimal, (R_(opt)=-0.35) resonance effect with ortho substituted (I_o$gt;0) electron donating group (R$lt;0) and STERIMOL parameter, B₁ constant. The inhibition activity between hetro ring substituents have been a proportioned with each others and none substituent(H), 45 showed the highest FPTase inhibition (pI_(50))=4.30) activity.