| Title : Change in the mode of inhibition of acetylcholinesterase by (4- nitrophenyl)sulfonoxyl derivatives of conformationally constrained choline analogues - Savle_1998_Chem.Res.Toxicol_11_19 |
| Author(s) : Savle PS , Medhekar RA , Kelley EL , May JG , Watkins SF , Fronczek FR , Quinn DM , Gandour RD |
| Ref : Chemical Research in Toxicology , 11 :19 , 1998 |
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Abstract :
A chiral, five-step synthesis of 2-(hydroxymethyl)-2,4-dimethylmorpholine (12) from (R)- and (S)-2-methylglycidols gives an overall yield of 63%. Morpholines (R)- and (S)-12 are converted into 2-(azidomethyl)-2,4-dimethylmorpholine (15) via 2,4-dimethyl-2-[[(4-nitrophenyl)sulfonoxy]methyl]morpholine (14). The tertiary morpholines 12, 14, and 15 are quaternarized to afford 2-(hydroxymethyl)-2,4,4-trimethylmorpholinum iodide (2), 2,4,4-trimethyl-2-[[(4-nitrophenyl)sulfonoxy]methyl]morpholinium iodide (3), and 2-(azidomethyl)-2,4,4-trimethylmorpholinium iodide (4), respectively, which all inhibit acetylcholinesterase (AChE). These morpholinium inhibitors are compared with conformationally constrained aryl hemicholinium AChE inhibitors. Enantiomers of 2 and 4 are reversible competitive inhibitors of AChE, with values of Ki = 360 +/- 30 microM for (S)-2, 650 +/- 90 microM for (R)-2, 450 +/- 70 microM for (S)-4, and 560 +/- 30 microM for (R)-4, respectively. Enantiomers of 3 are noncompetitive inhibitors of AChE with values of Ki = 19.0 +/- 0.9 microM for (S)-3 and 50 +/- 2 microM for (R)-3, respectively. AChE shows a 2-fold chiral discrimination in the case of inhibition by 2 and 3. Inhibition also changes from competitive to noncompetitive when (3-hydroxyphenyl)-N,N,N-trimethylammonium iodide (18) [Ki = 0.21 +/- 0.06 microM; Lee, B. H., Stelly, T. C., Colucci, W. J., Garcia, J. G., Gandour, R. D., and Quinn, D. M. (1992) Chem. Res. Toxicol. 5, 411-418] is converted into [3-[(4-nitrophenyl)sulfonoxy]phenyl]-N,N,N-trimethylammonium iodide (5), Ki = 6.0 +/- 0.5 microM. These results indicate that the 4-nitrobenzenesulfonyl group controls the mode of inhibition. |
| PubMedSearch : Savle_1998_Chem.Res.Toxicol_11_19 |
| PubMedID: 9477222 |
Savle PS, Medhekar RA, Kelley EL, May JG, Watkins SF, Fronczek FR, Quinn DM, Gandour RD (1998)
Change in the mode of inhibition of acetylcholinesterase by (4- nitrophenyl)sulfonoxyl derivatives of conformationally constrained choline analogues
Chemical Research in Toxicology
11 :19
Savle PS, Medhekar RA, Kelley EL, May JG, Watkins SF, Fronczek FR, Quinn DM, Gandour RD (1998)
Chemical Research in Toxicology
11 :19