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- W2012134800 abstract "To determine the importance of electrostatic interactions for agonist binding to the nicotinic acetylcholine receptor (AChR), we examined the affinity of the fluorescent agonist dansyl-C6-choline for the AChR. Increasing ionic strength decreased the binding affinity in a noncompetitive manner and increased the Hill coefficient of binding. Small cations did not compete directly for dansyl-C6-choline binding. The sensitivity to ionic strength was reduced in the presence of proadifen, a noncompetitive antagonist that desensitizes the receptor. Moreover, at low ionic strength, the dansyl-C6-choline affinities were similar in the absence or presence of proadifen, a result consistent with the receptor being desensitized at low ionic strength. Similar ionic strength effects were observed for the binding of the noncompetitive antagonist [3H]ethidium when examined in the presence and absence of agonist to desensitize the AChR. Therefore, ionic strength modulates binding affinity through at least two mechanisms: by influencing the conformation of the AChR and by electrostatic effects at the binding sites. The results show that charge-charge interactions regulate the desensitization of the receptor. Analysis of dansyl-C6-choline binding to the desensitized conformation using the Debye-Hückel equation was consistent with the presence of five to nine negative charges within 20 Å of the acetylcholine binding sites." @default.
- W2012134800 created "2016-06-24" @default.
- W2012134800 creator A5002600946 @default.
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- W2012134800 date "2000-03-01" @default.
- W2012134800 modified "2023-10-18" @default.
- W2012134800 title "Electrostatic Interactions Regulate Desensitization of the Nicotinic Acetylcholine Receptor" @default.
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- W2012134800 doi "https://doi.org/10.1016/s0006-3495(00)76687-2" @default.
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