m-Azido-phencyclidine covalently labels the rat brain PCP receptor, a putative K channel.
The Journal of neuroscience : the official journal of the Society for Neuroscience December 1, 1986 R G Sorensen, M P Blaustein
Phencyclidine (PCP) binds with high affinity to a specific receptor in rat brain membranes, which is likely a voltage-gated, noninactivating potassium channel. Several potassium channel blockers, including aminopyridines and tetraalkylamines, displace PCP from this binding site, supporting the hypothesis. A photolabile PCP analog, m-azido-PCP, binds reversibly to two classes of sites on rat brain synaptic membranes: a high-affinity site (dissociation constant 0.14 ± 0.01 µM) and a low-affinity site (255 ± 55 µM). The high-affinity site corresponds to the PCP receptor. The rank order of potency for displacing PCP from this site among aminopyridines is 4-AP ≈ 3,4-diAP > 2-AP ≫ 3-AP; among tetraalkylamines it is TBA > TEA ≫ TMA.