Design and activity of cationic fullerene derivatives as inhibitors of acetylcholinesterase |
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Authors: | Pastorin Giorgia Marchesan Silvia Hoebeke Johan Da Ros Tatiana Ehret-Sabatier Laurence Briand Jean-Paul Prato Maurizio Bianco Alberto |
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Institution: | Institute of Molecular and Cellular Biology, UPR 9021 CNRS, Strasbourg, France. |
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Abstract: | Four different regioisomers of cationic bis-N,N-dimethylfulleropyrrolidinium salts have been prepared and evaluated as inhibitors of the enzymatic activity of acetylcholinesterase. These fullerene-based derivatives were found to be noncompetitive inhibitors of acetylthiocholine hydrolysis. Molecular modelling was used to describe the possible interactions between the fullerene cage and the amino acids surrounding the cavity of the enzyme. The cationic C(60) derivatives used in this study represent a new class of molecules potentially able to modulate the enzymatic activity of acetylcholinesterase. |
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