title: Design and activity of cationic fullerene derivatives as inhibitors of acetylcholinesterase.
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.
authors.affiliation: Institute of Molecular and Cellular Biology, UPR 9021 CNRS, Strasbourg, France.
authors.forename: Giorgia
authors.initials: G
authors.lastname: Pastorin
authors.forename: Silvia
authors.initials: S
authors.lastname: Marchesan
authors.forename: Johan
authors.initials: J
authors.lastname: Hoebeke
authors.forename: Tatiana
authors.initials: T
authors.lastname: Da Ros
authors.forename: Laurence
authors.initials: L
authors.lastname: Ehret-Sabatier
authors.forename: Jean-Paul
authors.initials: JP
authors.lastname: Briand
authors.forename: Maurizio
authors.initials: M
authors.lastname: Prato
authors.forename: Alberto
authors.initials: A
authors.lastname: Bianco
mesh_terms: D000110:Acetylcholinesterase / Q000187:drug effects*; D001665:Binding Sites; D002412:Cations; D002800:Cholinesterase Inhibitors / Q000737:chemistry* / Q000494:pharmacology*; D015195:Drug Design; D037741:Fullerenes / Q000737:chemistry* / Q000494:pharmacology*; D008958:Models, Molecular
chemical_list: D002412:Cations; D002800:Cholinesterase Inhibitors; D037741:Fullerenes; D000110:Acetylcholinesterase