Sensitivity Increase in Nicotinic Acetylcholine Receptor Binding in Fiber OpticWave Guide

摘要

Ligand binding studies with nicotinic acetylcholine receptor on the fiber opticbiosensor indicate K (sub i) values for antagonists were similar to those obtained in membrane binding assays. The agonists appear much less potent. This may be due to the inability of the receptor to make appropriate conformational changes necessary for agonist binding. Spacer arms may give the receptor the conformational freedom required. To test whether the spacer arms increase the conformational freedom of the immobilized receptors, receptors were tethered to the surface of the fiber with the antibodies specific for the receptor but did not block the binding sites of the receptor. Receptor binding of agonists on tethered receptors was at least one order of magnitude lower than values previously reported.