Design and activity of cationic fullerene derivatives as inhibitors of acetylcholinesterase

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...

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Published inOrganic & biomolecular chemistry Vol. 4; no. 13; p. 2556
Main Authors Pastorin, Giorgia, Marchesan, Silvia, Hoebeke, Johan, Da Ros, Tatiana, Ehret-Sabatier, Laurence, Briand, Jean-Paul, Prato, Maurizio, Bianco, Alberto
Format Journal Article
LanguageEnglish
Published England 01.01.2006
Subjects
Acetylcholinesterase - drug effects
Binding Sites
Cations
Cholinesterase Inhibitors - chemistry
Cholinesterase Inhibitors - pharmacology
Drug Design
Fullerenes - chemistry
Fullerenes - pharmacology
Models, Molecular
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Summary: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.
ISSN:1477-0520
1477-0539
DOI:10.1039/b604361e