|Title||Aggregation of disease-related peptides.|
|Publication Type||Journal Article|
|Year of Publication||2020|
|Authors||Nguyen PH, Sterpone F, Derreumaux P|
|Journal||Prog Mol Biol Transl Sci|
Protein misfolding and aggregation of amyloid proteins is the fundamental cause of more than 20 diseases. Molecular mechanisms of the self-assembly and the formation of the toxic aggregates are still elusive. Computer simulations have been intensively used to study the aggregation of amyloid peptides of various amino acid lengths related to neurodegenerative diseases. We review atomistic and coarse-grained simulations of short amyloid peptides aimed at determining their transient oligomeric structures and the early and late aggregation steps.
|Alternate Journal||Prog Mol Biol Transl Sci|