Acetylcholinesterase inhibition structure-activity relationships

Kang SY, Lee KY, Sung SH, Park MJ, Kim YC, Coumarins isolated from Angelica gigas inhibit acetylcholinesterase Structure-activity relationships, f Nat Prod 64 683-685,2001. 

Ali HM, Sharaf EHA, Hikal MS. Selectivity, acetylcholinesterase inhibition kinetics and quantitative structure-activity relationships of a series of N-(2-oxido-l,3,2-benzodioxa-phosphol-2-yl) amino acid ethyl or diethyl esters. Pest Biochem Physiol 2005 83 58-65. 

Lin G, Lai CY, Liao WC. Molecular recognition by acetylcholinesterase at the peripheral anionic site Structure-activity relationships for inhibitions by aryl carbamates. Bioorg Med Chem 1999 7 2683-9. 

Su C-T, Wang P-H, Liu R-F et al. (1986). Kinetic studies and structure-activity relationships of bispyridinium oximes as reactivators of acetylcholinesterase inhibited by organophosphorus compounds. Fund Appl Toxicol, 6, 506-524. 

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Carbamates - Structure activity relationships have been studied with respect to toxicity and anticholinesterase activity. 9 The mechanism of acetylcholinesterase inhibition by the carbamates is not entirely clear. 

The great majority of insecticides are nerve poisons. The target for most of them is an enzyme called acetylcholinesterase (AChE). We will describe the enzyme and its inhibition in some detail because there are no other enzymes for which we know so much about the relationship between its structure and its activity. The cholinesterase-inhibiting insecticides, the warfare gases, and the target enzyme have been the objects of intense study by scientists for many years. 

A review of the literature of the distribution, function and structure of acetylcholinesterase is too voluminous for the scope of this article, and the reader is referred elsewhere [1]. Cholinesterase enzyme is a protein, and a dietary deficiency of protein can result in lower cholinesterase activity in liver microsomes and serum of rats. Cholinesterase inhibition by parathion and by Banol (6-chloro-3,4-xylyl methylcarbamate) (Upjohn) is more at lower dietary levels of casein than at higher levels, thus confirming that the toxicity of these enzyme inhibitors is greater at lower dietary protein levels [13]. This observation indicates that a causal relationship exists between amino-acid intake and cholinesterase activity. 

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