Summary
Binding of some selected steroids and anabolic agents to bovine sex-hormone binding
globulin (SHBG)* was investigated. SHBG binding affinities, relative to the reference hormone 5α-dihydrotestosterone,
were estimated for the compounds. The results demonstrate that binding of steroid
hormones to SHBG is facilitated by the 17β-hydroxyl group, possibly involving hydrogen
binding, and by the methyl group at C-19 of the steroid moiety. Structural modifications
at C-17 of a steroid molecule involving esterification, epimerization or reduction
of the 17β-hydroxyt group, or introduction of a bulky 17α group have the effect of
decreasing the SHBG binding affinity of the steroid molecule.
Key-Words:
SHBG
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Steroids
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Anabolic Agents
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Binding Affinity
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Bioavailability
