Abstract
This essay discusses the different affinities of acetylcholine and nicotine for muscle-type acetylcholine receptors (nAChRs) due to their different chemical structures and binding mechanisms. Muscle-type nAChRs are pentameric receptors composed of five protein subunits, with the alpha subunit directly interacting with acetylcholine or nicotine. Acetylcholine binds to muscle-type nAChRs through key functional groups, including the carbonyl group and the quaternary ammonium cation, and specific interactions with tyrosine, serine, and tryptophan residues. Nicotine binds to muscle-type nAChRs through weaker interactions with the pyridine and pyrrolidine rings, as well as with polar or charged residues in the binding site. The strengths of the hydrogen bonds and pi-cation interactions involved in acetylcholine and nicotine binding are relatively weak.
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