@article{pastorin_design_2006,
title = {Design and activity of cationic fullerene derivatives as inhibitors of acetylcholinesterase},
author = {Giorgia Pastorin and Silvia Marchesan and Johan Hoebeke and Tatiana Da Ros and Laurence Ehret-Sabatier and Jean-Paul Briand and Maurizio Prato and Alberto Bianco},
doi = {10.1039/b604361e},
issn = {1477-0520},
year = {2006},
date = {2006-07-01},
journal = {Organic & Biomolecular Chemistry},
volume = {4},
number = {13},
pages = {2556--2562},
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.},
keywords = {Acetylcholinesterase, Binding Sites, Cations, Cholinesterase Inhibitors, Drug Design, Fullerenes, I2CT, Models, Molecular, Team-Bianco},
pubstate = {published},
tppubtype = {article}
}
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.