Amyloid Polymorphism in the Protein Folding and Aggregation Energy Landscape
- PMID: 29446868
- DOI: 10.1002/anie.201713416
Amyloid Polymorphism in the Protein Folding and Aggregation Energy Landscape
Abstract
Protein folding involves a large number of steps and conformations in which the folding protein samples different thermodynamic states characterized by local minima. Kinetically trapped on- or off-pathway intermediates are metastable folding intermediates towards the lowest absolute energy minima, which have been postulated to be the natively folded state where intramolecular interactions dominate, and the amyloid state where intermolecular interactions dominate. However, this view largely neglects the rich polymorphism found within amyloid species. We review the protein folding energy landscape in view of recent findings identifying specific transition routes among different amyloid polymorphs. Observed transitions such as twisted ribbon→crystal or helical ribbon→nanotube, and forbidden transitions such helical ribbon↛crystal, are discussed and positioned within the protein folding and aggregation energy landscape. Finally, amyloid crystals are identified as the ground state of the protein folding and aggregation energy landscape.
Keywords: amyloids; energy landscapes; polymorphism; protein aggregation; protein folding.
© 2018 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.
Similar articles
-
Energy Landscapes of Protein Aggregation and Conformation Switching in Intrinsically Disordered Proteins.J Mol Biol. 2021 Oct 1;433(20):167182. doi: 10.1016/j.jmb.2021.167182. Epub 2021 Aug 3. J Mol Biol. 2021. PMID: 34358545 Review.
-
Surveying the Energy Landscapes of Aβ Fibril Polymorphism.J Phys Chem B. 2018 Dec 13;122(49):11414-11430. doi: 10.1021/acs.jpcb.8b07364. Epub 2018 Oct 1. J Phys Chem B. 2018. PMID: 30215519 Free PMC article.
-
Conformational Variability of Amyloid-β and the Morphological Diversity of Its Aggregates.Molecules. 2022 Jul 26;27(15):4787. doi: 10.3390/molecules27154787. Molecules. 2022. PMID: 35897966 Free PMC article. Review.
-
A Simple Principle for Understanding the Combined Cellular Protein Folding and Aggregation.Curr Protein Pept Sci. 2020;21(1):3-21. doi: 10.2174/1389203720666190725114550. Curr Protein Pept Sci. 2020. PMID: 31345145 Review.
-
AlphaFold and the amyloid landscape.J Mol Biol. 2021 Oct 1;433(20):167059. doi: 10.1016/j.jmb.2021.167059. Epub 2021 May 21. J Mol Biol. 2021. PMID: 34023402 Review.
Cited by
-
Multiscale Structural Elucidation of Peptide Nanotubes by X-Ray Scattering Methods.Front Bioeng Biotechnol. 2021 Mar 29;9:654339. doi: 10.3389/fbioe.2021.654339. eCollection 2021. Front Bioeng Biotechnol. 2021. PMID: 33855016 Free PMC article. Review.
-
Peptide backbone modifications of amyloid β (1-40) impact fibrillation behavior and neuronal toxicity.Sci Rep. 2021 Dec 9;11(1):23767. doi: 10.1038/s41598-021-03091-4. Sci Rep. 2021. PMID: 34887476 Free PMC article.
-
Inhibition of Amyloid Aggregation and Toxicity with Janus Iron Oxide Nanoparticles.Chem Mater. 2021 Aug 24;33(16):6484-6500. doi: 10.1021/acs.chemmater.1c01947. Epub 2021 Aug 3. Chem Mater. 2021. PMID: 34887621 Free PMC article.
-
Emergence of a short peptide based reductase via activation of the model hydride rich cofactor.Nat Commun. 2024 May 28;15(1):4515. doi: 10.1038/s41467-024-48930-w. Nat Commun. 2024. PMID: 38802430 Free PMC article.
-
Green Ambient-Dried Aerogels with a Facile pH-Tunable Surface Charge for Adsorption of Cationic and Anionic Contaminants with High Selectivity.Biomacromolecules. 2022 Nov 14;23(11):4934-4947. doi: 10.1021/acs.biomac.2c01142. Epub 2022 Nov 1. Biomacromolecules. 2022. PMID: 36318480 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
