Peptides and proteins tend to aggregate under appropriate conditions. The amyloid fibrils that are ubiquitously found among these structures are associated with major human diseases like Alzheimer's disease, type 11 diabetes, and various prion diseases. Lately, it has been observed that even very short peptides like tetra and pentapeptides can form ordered amyloid structures. Here, we present aggregation studies of three such small polypeptide systems, namely, the two amyloidogenic peptides DFNKF and FF, and a control (nonamyloidogenic) one, the AGAIL. The respective aggregation process is studied by all-atom Molecular Dynamics simulations, which allow to shed light on the fine details of the association and aggregation process. Our analysis suggests that naturally aggregating systems exhibit significantly diverse overall cluster shape properties and specific intermolecular interactions. Additional analysis was also performed on the previously studied NFGAIL system.
Flock, D., Rossetti, G., Daidone, I., Amadei, A., & Di Nola, A. (2006). Aggregation of small peptides studied by molecular dynamics simulations. PROTEINS, 65(4), 914-921.
|Tipologia:||Articolo su rivista|
|Citazione:||Flock, D., Rossetti, G., Daidone, I., Amadei, A., & Di Nola, A. (2006). Aggregation of small peptides studied by molecular dynamics simulations. PROTEINS, 65(4), 914-921.|
|Settore Scientifico Disciplinare:||Settore CHIM/02 - Chimica Fisica|
|Revisione (peer review):||Sì, ma tipo non specificato|
|Digital Object Identifier (DOI):||http://dx.doi.org/10.1002/prot.21168|
|Stato di pubblicazione:||Pubblicato|
|Data di pubblicazione:||2006|
|Titolo:||Aggregation of small peptides studied by molecular dynamics simulations|
|Autori:||Flock, D; Rossetti, G; Daidone, I; Amadei, A; Di Nola, A|
|Appare nelle tipologie:||01 - Articolo su rivista|