title: Quantitative prediction of amyloid fibril growth of short peptides from simulations: calculating association constants to dissect side chain importance.
abstract: Quantitative prediction of the fibril growth properties of different peptides is conducted with a molecular dynamics approach. Association constants of small peptides used as a model for amyloid formation are calculated, and the results show very good agreement with experiments. Also the free-energy differences associated with two important interactions that characterize fibril growth, namely cross-beta-sheet and lateral interactions, are obtained. These two interactions show different dependencies on the physicochemical properties of the side chains, explaining the variation in fibril morphologies between different peptides.
authors.affiliation: Delft University of Technology, Julianalaan 136, 2628 BL Delft, The Netherlands. m.g.wolf@tudelft.nl
authors.forename: Maarten G
authors.initials: MG
authors.lastname: Wolf
authors.forename: Jaap A
authors.initials: JA
authors.lastname: Jongejan
authors.forename: Jon D
authors.initials: JD
authors.lastname: Laman
authors.forename: Simon W
authors.initials: SW
authors.lastname: de Leeuw
mesh_terms: D000682:Amyloid / Q000737:chemistry*; D003198:Computer Simulation; D010455:Peptides / Q000737:chemistry*; D011336:Probability
chemical_list: D000682:Amyloid; D010455:Peptides