@article {269,
	title = {Molecular modelling approaches to the design of acetylcholinesterase inhibitors: new challenges for the treatment of Alzheimer{\textquoteright}s disease},
	journal = {Current pharmaceutical design},
	volume = {10},
	year = {2004},
	month = {2004///},
	pages = {3131 - 3140},
	abstract = {The interest for acetylcholinesterase as a target for the palliative treatment of Alzheimer{\textquoteright}s disease has been renewed in the last years owing to the evidences that support the role of this enzyme in accelerating the aggregation and deposition of the beta-amyloid peptide. A large amount of structural information on the acetylcholinesterase enzyme and of its complexes with inhibitors acting at the catalytic site, the peripheral binding site, or both is now available. Based on that, molecular modelling studies can be intensively used to decipher the molecular determinants that mediate the relationship between chemical structure and inhibitory potency. In turn, this knowledge can be exploited to design new compounds leading to more effective cholinergic strategies. At this point, inhibitors able to interact at the peripheral binding site are of particular relevance, as they might disrupt the interactions between the enzyme acetylcholinesterase and the beta-amyloid peptide. Therefore, these compounds might not only ameliorate the cholinergic deficit, but also be capable of slowing down the progression of the disease.},
	keywords = {Alzheimer Disease/drug therapy; Animals; Binding Sites; Cholinesterase Inhibitors/chemical synthesis/chemistry/therapeutic use; Drug Design; Humans; Models, Chemical; Molecular Structure; Structure-Activity Relationship},
	author = {Munoz-Muriedas,J. and Lopez,J. M. and M. Orozco and F. J. Luque}
}
