Binding of alkylphenols and alkylated non-phenolics to the rainbow trout (Oncorhynchus mykiss) plasma sex steroid-binding protein.
Alkylphenols are well-known endocrine disrupters, mediating effects through the estrogen receptor (ER). Although the estrogenic properties of the alkylphenols are well documented, alternative mechanisms of action are poorly described. In the present work, the interaction of a range of alkyl-substituted phenols and alkyl-substituted non-phenolics with the rainbow trout (Oncorhynchus mykiss) sex steroid-binding protein (rtSBP) were determined by competitive ligand-binding studies. The role of alkyl chain length and branching, substituent position, number of alkylated groups, and the requirement of a phenolic ring structure were assessed. The results showed that the rtSBP binds to most chemical structures tested, although the highest affinity was obtained for mono-substituted alkylphenols with a chain length of four to eight methyl groups. Interestingly, rtSBP binding was also observed for non-phenolic compounds such as 4-t-butylcyclohexanol and 4-t-butylnitrobenzene suggesting that the rtSBP has a broad binding specificity for alkylphenols and alkylated non-phenolics.
Tollefsen
K-E
KE
Norwegian Institute for Water Research (NIVA), PO Box 173 Kjelsaas, N-0411 Oslo, Norway. knut.erik.tollefsen@niva.no
D000478:Alkylation; D000818:Animals; D001665:Binding Sites; D052244:Endocrine Disruptors / Q000737:chemistry / Q000378:metabolism*; D005260:Female; D017686:Oncorhynchus mykiss / Q000502:physiology*; D010636:Phenols / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D012738:Sex Hormone-Binding Globulin / Q000378:metabolism*; D013329:Structure-Activity Relationship; D014874:Water Pollutants, Chemical / Q000737:chemistry / Q000378:metabolism*
D052244:Endocrine Disruptors; D010636:Phenols; D012738:Sex Hormone-Binding Globulin; D014874:Water Pollutants, Chemical; C474055:octylphenol; C025256:nonylphenol; C006862:butylphen