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The minimal topological difference (MTD) method is used to describe quantitative structure-activity relationships (OSAR) for the progesterone-receptor binding affinity including 59 proge-stational steroids. Multiple correlation coefficients of r = 0.962 and r = 0.955 are obtained by use of the MTD variable and a measure of hydrophobicity for the series of progesterone and ethisterone derivatives, respectively. Hydrophobic effects are found to strongly influence receptor binding. In accordance with the hydrogen bonding concept, the optimized MTD receptor maps indicate cavity vertices in the regions of oxygen functions at C3 and in the 17β position. Receptor wall vertices are attributed in the areas of 4, 10β, and 13β substituents of 4-en-3-one steroids while 17α side chains additionally contain receptor cavity vertices. A comparison of corresponding receptor maps suggests in accord with X-ray crystal structure data that progesterone and ethisterone derivatives are bound in somewhat different orientations relative to the receptor surface.

MTD Calculations on Quantitative Structure-Activity Relationships of Steroids Binding to the Progesterone Receptor