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Aggregation of an Amyloidogenic Peptide on Gold Surfaces
Solid surfaces have been shown to affect the aggregation and assembly of many biomolecular systems. One important example is the formation of protein fibrils, which can occur on a range of biological and synthetic surfaces. The rate of fibrillation depends on both the protein structure and the surfa...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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MDPI
2023
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10452923/ https://www.ncbi.nlm.nih.gov/pubmed/37627326 http://dx.doi.org/10.3390/biom13081261 |
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author | Cheung, David L. |
author_facet | Cheung, David L. |
author_sort | Cheung, David L. |
collection | PubMed |
description | Solid surfaces have been shown to affect the aggregation and assembly of many biomolecular systems. One important example is the formation of protein fibrils, which can occur on a range of biological and synthetic surfaces. The rate of fibrillation depends on both the protein structure and the surface chemistry, with the different molecular and oligomer structures adopted by proteins on surfaces likely to be crucial. In this paper, the aggregation of the model amyloidogenic peptide, A [Formula: see text] (16–22), corresponding to a hydrophobic segment of the amyloid beta protein on a gold surface is studied using molecular dynamics simulation. Previous simulations of this peptide on gold surfaces have shown that it adopts conformations on surfaces that are quite different from those in bulk solution. These simulations show that this then leads to significant differences in the oligomer structures formed in solution and on gold surfaces. In particular, oligomers formed on the surface are low in beta-strands so are unlike the structures formed in bulk solution. When oligomers formed in solution adsorb onto gold surfaces they can then restructure themselves. This can then help explain the inhibition of A [Formula: see text] (16–22) fibrillation by gold surfaces and nanoparticles seen experimentally. |
format | Online Article Text |
id | pubmed-10452923 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-104529232023-08-26 Aggregation of an Amyloidogenic Peptide on Gold Surfaces Cheung, David L. Biomolecules Article Solid surfaces have been shown to affect the aggregation and assembly of many biomolecular systems. One important example is the formation of protein fibrils, which can occur on a range of biological and synthetic surfaces. The rate of fibrillation depends on both the protein structure and the surface chemistry, with the different molecular and oligomer structures adopted by proteins on surfaces likely to be crucial. In this paper, the aggregation of the model amyloidogenic peptide, A [Formula: see text] (16–22), corresponding to a hydrophobic segment of the amyloid beta protein on a gold surface is studied using molecular dynamics simulation. Previous simulations of this peptide on gold surfaces have shown that it adopts conformations on surfaces that are quite different from those in bulk solution. These simulations show that this then leads to significant differences in the oligomer structures formed in solution and on gold surfaces. In particular, oligomers formed on the surface are low in beta-strands so are unlike the structures formed in bulk solution. When oligomers formed in solution adsorb onto gold surfaces they can then restructure themselves. This can then help explain the inhibition of A [Formula: see text] (16–22) fibrillation by gold surfaces and nanoparticles seen experimentally. MDPI 2023-08-18 /pmc/articles/PMC10452923/ /pubmed/37627326 http://dx.doi.org/10.3390/biom13081261 Text en © 2023 by the author. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Cheung, David L. Aggregation of an Amyloidogenic Peptide on Gold Surfaces |
title | Aggregation of an Amyloidogenic Peptide on Gold Surfaces |
title_full | Aggregation of an Amyloidogenic Peptide on Gold Surfaces |
title_fullStr | Aggregation of an Amyloidogenic Peptide on Gold Surfaces |
title_full_unstemmed | Aggregation of an Amyloidogenic Peptide on Gold Surfaces |
title_short | Aggregation of an Amyloidogenic Peptide on Gold Surfaces |
title_sort | aggregation of an amyloidogenic peptide on gold surfaces |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10452923/ https://www.ncbi.nlm.nih.gov/pubmed/37627326 http://dx.doi.org/10.3390/biom13081261 |
work_keys_str_mv | AT cheungdavidl aggregationofanamyloidogenicpeptideongoldsurfaces |