Three-dimensional structures of the complexes between the Abeta(1-42) fragments Abeta(1-11), Abeta(10-20), Abeta(12-28), and Abeta(22-35) and the alpha7 nicotinic receptor were obtained with the aid of the ESCHER program. Furthermore, short high-temperature molecular dynamics simulations in vacuo were employed to relax the complexes and allow the peptides to accommodate in the binding site. The final models have shown that Abeta peptides do bind on the same site, which is delineated by loop C of one subunit and the loops 6274 and G of the adjacent subunit on the receptor. This finding is supported by previous experimental and theoretical data, and should help one to obtain a better and more detailed structural information about the activity of the Abeta peptides and their repercussion in the disorders at molecular level, which are characteristic of the Alzheimer's disease. (C) 2004 Elsevier Inc. All rights reserved.