Structure activity relationship study of known inhibitors of the enzyme 5 alpha-reductase (5AR).
Preliminary results of a modelling study of both steroidal and non-steroidal inhibitors of 5 alpha-reductase (5AR) are described in order to elucidate the essential structural requirements needed for the design of novel non-steroidal inhibitors. The study suggests that: (i) there is a requirement for groups to mimic the C(3) = O of the steroid substrate A-ring; (ii) the area of the active site about the C(17)-OH position of the substrate does not appear to possess hydrogen bonding groups and is unrestricted.
Ahmed
S
S
School of Applied Chemistry, Kingston University, Surrey. CH_S534@KINGSTON.AC.UK
Denison
S
S
D042944:Cholestenone 5 alpha-Reductase; D004791:Enzyme Inhibitors / Q000737:chemistry* / Q000494:pharmacology*; D006860:Hydrogen Bonding; D015394:Molecular Structure; D010088:Oxidoreductases / Q000037:antagonists & inhibitors*; D013329:Structure-Activity Relationship
D004791:Enzyme Inhibitors; D010088:Oxidoreductases; D042944:Cholestenone 5 alpha-Reductase