Protein ligand interactions 7 halogenated pyridinium salts as inhibitors of acetylcholinesterase from Electrophorus electricus.
The interaction of halo-quaternary pyridinium hydrochloride salts on acetylcholinesterase (AChE, E.C.3.1.1.7) has been investigated. Kinetic analysis has shown that they reflect a non-competitive inhibition with Ki values in the range 8-13 microM and 5-34 microM for chloro- and bromo-substituted salts respectively. Spectrophotometry was used to study the binding of the ligands with the enzyme and Scatchard analysis used to calculate the respective dissociation constants (Kd) and the number of binding sites. The substitution position of the halogen on the pyridine ring also influenced the binding capacity and the Ki values.
Whiteley
C G
CG
Department of Biochemistry and Microbiology, Rhodes University, Grahamstown, South Africa.
Ngwenya
D S
DS
D000110:Acetylcholinesterase / Q000378:metabolism*; D000122:Acetylthiocholine / Q000378:metabolism; D000818:Animals; D001665:Binding Sites; D002800:Cholinesterase Inhibitors / Q000378:metabolism* / Q000494:pharmacology; D004593:Electrophorus; D007700:Kinetics; D008024:Ligands; D008956:Models, Chemical; D011725:Pyridines / Q000378:metabolism* / Q000494:pharmacology; D012492:Salts / Q000378:metabolism / Q000494:pharmacology
D002800:Cholinesterase Inhibitors; D008024:Ligands; D011725:Pyridines; D012492:Salts; D000122:Acetylthiocholine; D000110:Acetylcholinesterase