title: The role of aromaticity, exposed surface, and dipole moment in determining protein aggregation rates.
abstract: The mechanisms by which peptides and proteins form ordered aggregates are not well understood. Here we focus on the physicochemical properties of amino acids that favor ordered aggregation and suggest a parameter-free model that is able to predict the change of aggregation rates over a large set of natural sequences. Furthermore, the results of the parameter-free model correlate well with the aggregation propensities of a set of peptides designed by computer simulations.
authors.affiliation: Department of Biochemistry, University of Zurich, CH-8057, Zurich, Switzerland.
authors.forename: Gian Gaetano
authors.initials: GG
authors.lastname: Tartaglia
authors.forename: Andrea
authors.initials: A
authors.lastname: Cavalli
authors.forename: Riccardo
authors.initials: R
authors.lastname: Pellarin
authors.forename: Amedeo
authors.initials: A
authors.lastname: Caflisch
mesh_terms: D000544:Alzheimer Disease / Q000378:metabolism; D000596:Amino Acids / Q000737:chemistry* / Q000378:metabolism; D000818:Animals; D003198:Computer Simulation; D006801:Humans; D011328:Prions / Q000737:chemistry / Q000378:metabolism; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D013816:Thermodynamics
chemical_list: D000596:Amino Acids; D011328:Prions; D011506:Proteins