Pons M, Bignon E, Crastes de Paulet A, Gilbert J, Ojasoo T, Raynaud J P
INSERM U58, Montpellier, France.
J Steroid Biochem. 1990 Aug 14;36(5):391-7. doi: 10.1016/0022-4731(90)90079-8.
The relative binding affinities of a series of twelve para-hydroxylated triphenylethylenes (TPEs) for the estradiol receptor (ER) of calf uterus cytosol were measured by a competition method. The results obtained under equilibrium conditions support the hypothesis of the additivity of the energies corresponding to each of the hydrogen-bond type interactions of di- or tri-hydroxylated TPEs with the estradiol binding site of ER and strongly suggest that, whichever ring is hydroxylated, the orientation of the TPE in the steroid binding site is always the same. A hydroxyl group in a given position always interacts with the same location within the site. Mono-hydroxylation of the highly hydrophobic non-substituted TPE skeleton led to a large increase in relative binding affinity for ER which could be explained by a dual mechanism whereby the interaction specific to the hydroxyl is accompanied by a temperature- or time-dependent binding process that is not related to the hydroxylation position.
采用竞争法测定了一系列12种对羟基化三苯乙烯（TPEs）对小牛子宫细胞质雌二醇受体（ER）的相对结合亲和力。在平衡条件下获得的结果支持了二羟基或三羟基化TPEs与ER的雌二醇结合位点的每种氢键型相互作用所对应的能量具有加和性的假说，并强烈表明，无论哪个环被羟基化，TPE在类固醇结合位点的取向总是相同的。给定位置的羟基总是与该位点内的相同位置相互作用。高度疏水的未取代TPE骨架的单羟基化导致对ER的相对结合亲和力大幅增加，这可以用双重机制来解释，即羟基特异性相互作用伴随着与羟基化位置无关的温度或时间依赖性结合过程。
