Conformational transition of Aβ42 inhibited by a mimetic peptide. A molecular modeling study using QM/MM calculations and QTAIM analysis
- Barrera Guisasola, Exequiel Ernesto
- Gutierrez, Lucas Joel
- Salcedo, Rodrigo Emiliano
- Garibotto, Francisco Matías
- Andujar, Sebastian Antonio
- Enriz, Ricardo Daniel
- Rodríguez, Ana M.
DOIAbstract
The main pathogenic event in Alzheimer's disease is believed to be the aggregation of the amyloid β-peptides into toxic aggregates. In a previous work we designed a mimetic peptide possessing a significant aggregation modulating effect by means of a molecular modeling study, using a pentameric model as a molecular target. Considerable experimental evidence indicates that oligomers as small as dimers have been involved in this disease. Therefore, an alternative therapeutic strategy might be to block the oligomerization at a monomeric level. To this end, using an Aβ42 monomeric model, we explored the capacity and mechanism of our mimetic peptides to stabilize the α-helical conformation while preventing the formation of β-sheet structures. Lon...
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