Binding of alkylphenols and alkylated non-phenolics to rainbow trout (Oncorhynchus mykiss) hepatic estrogen receptors.
Alkylphenols are well-known endocrine disrupters, mediating effects through the estrogen receptor (ER). In the present work, the interaction of alkylphenols and alkylated non-phenolics with hepatic rainbow trout (Oncorhynchus mykiss) estrogen receptors (rtERs) was determined. The role of alkyl chain length and branching, substituent position, number of alkylated groups, and the requirement of a phenolic ring structure was assessed. The results showed that the rtERs bound most alkylphenols, although with 20,000 to 2 million times lower affinity than the endogenous estrogen 17beta-estradiol. Mono-substituted alkylphenols with moderate (C4-C6) and long (C8 and C12) alkyl chain length in the para position exhibited the highest affinity for the rtERs. Substitution with multiple alkyl groups, presence of substituents in the ortho- and meta-position, and lack of a hydroxyl group on the benzene ring reduced the binding affinity. The rtERs resembled the reported binding specificity of the human ER for alkylphenols, although some exceptions were identified.
Tollefsen
Knut-Erik
KE
Norwegian Institute for Water Research, Gaustadallèen 21, N-0349 Oslo, Norway. knut.erik.tollefsen@niva.no
Julie Nilsen
Anja
A
D000814:Aniline Compounds / Q000378:metabolism; D000818:Animals; D001547:Benzaldehydes / Q000378:metabolism; D001555:Benzene Derivatives / Q000378:metabolism; D001565:Benzoates / Q000378:metabolism; D001667:Binding, Competitive; D052244:Endocrine Disruptors / Q000378:metabolism; D005260:Female; D008099:Liver / Q000378:metabolism; D017686:Oncorhynchus mykiss; D010636:Phenols / Q000378:metabolism*; D011960:Receptors, Estrogen / Q000378:metabolism*; D013329:Structure-Activity Relationship
D000814:Aniline Compounds; D001547:Benzaldehydes; D001555:Benzene Derivatives; D001565:Benzoates; D052244:Endocrine Disruptors; D010636:Phenols; D011960:Receptors, Estrogen; C034290:4-tert-butylbenzoic acid