Kinetics and mechanical stability of the fibril state control fibril formation time of polypeptide chains: A computational study.
| Autor: | Kouza M; Faculty of Chemistry, University of Warsaw, Pasteura 1, 02-093 Warsaw, Poland., Co NT; Institute of Physics, Polish Academy of Sciences, Lotnikow 32/46, 02-668 Warsaw, Poland., Li MS; Institute of Physics, Polish Academy of Sciences, Lotnikow 32/46, 02-668 Warsaw, Poland., Kmiecik S; Faculty of Chemistry, University of Warsaw, Pasteura 1, 02-093 Warsaw, Poland., Kolinski A; Faculty of Chemistry, University of Warsaw, Pasteura 1, 02-093 Warsaw, Poland., Kloczkowski A; Battelle Center for Mathematical Medicine, The Research Nationwide Children's Hospital, 575 Children's Crossroad, Columbus, Ohio 43215, USA., Buhimschi IA; Department of Pediatrics, The Ohio State University College of Medicine, Columbus, Ohio 43215, USA. |
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| Jazyk: | angličtina |
| Zdroj: | The Journal of chemical physics [J Chem Phys] 2018 Jun 07; Vol. 148 (21), pp. 215106. |
| DOI: | 10.1063/1.5028575 |
| Abstrakt: | Fibril formation resulting from protein misfolding and aggregation is a hallmark of several neurodegenerative diseases such as Alzheimer's and Parkinson's diseases. Despite much progress in the understanding of the protein aggregation process, the factors governing fibril formation rates and fibril stability have not been fully understood. Using lattice models, we have shown that the fibril formation time is controlled by the kinetic stability of the fibril state but not by its energy. Having performed all-atom explicit solvent molecular dynamics simulations with the GROMOS43a1 force field for full-length amyloid beta peptides Aβ |
| Databáze: | MEDLINE |
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