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THE CORRELATION OF STEROID PARTITION COEFFICIENTS WITH BINDING AFFINITIES TO THE RAT CYTOPLASMIC ANDROGEN RECEPTOR, RAT ANDROGEN‐BINDING PROTEIN, AND HUMAN TESTOSTERONE ESTRADIOL‐BINDING GLOBULIN

The binding affinity of a steroid to a protein binding site is regulated by spatial requirements as well as electronic and energetic factors, such as hydrogen bonding and hydrophobic properties. Because high entropy (calculated from free energy of binding I-:<) is associated with hydrophobic interactions, the objectives of this study were to determine the partition coefficient (PC) for a number of steroids and correlate them with the binding affinities to rat cytoplasmic androgen receptor (CR) , human testosterone estradiol-binding globulin (h-TeBG) , and rat androgen-binding protein (ABP) .