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Lysozyme Amyloid Fibril Structural Variability Dependence on Initial Protein Folding State
Amyloid fibril formation is associated with several amyloidoses, including neurodegenerative Alzheimer’s or Parkinson’s diseases. The process of such fibrillar structure formation is still not fully understood, with new mechanistic insights appearing on a regular basis. This, in turn, has limited th...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9141980/ https://www.ncbi.nlm.nih.gov/pubmed/35628230 http://dx.doi.org/10.3390/ijms23105421 |
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author | Mikalauskaite, Kamile Ziaunys, Mantas Smirnovas, Vytautas |
author_facet | Mikalauskaite, Kamile Ziaunys, Mantas Smirnovas, Vytautas |
author_sort | Mikalauskaite, Kamile |
collection | PubMed |
description | Amyloid fibril formation is associated with several amyloidoses, including neurodegenerative Alzheimer’s or Parkinson’s diseases. The process of such fibrillar structure formation is still not fully understood, with new mechanistic insights appearing on a regular basis. This, in turn, has limited the development of potential anti-amyloid compounds, with only a handful of effective cures or treatment modalities available. One of the multiple amyloid aggregation factors that requires further examination is the ability of proteins to form multiple, structurally distinct aggregates, based on the environmental conditions. In this work, we examine how the initial folding state affects the fibrilization of lysozyme—an amyloidogenic protein, often used in protein aggregation studies. We show that there is a correlation between the initial state of the protein and the aggregate formation lag time, rate of elongation, resulting aggregate structural variability and dye-binding properties, as well as formation lag time and rate of elongation. |
format | Online Article Text |
id | pubmed-9141980 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-91419802022-05-28 Lysozyme Amyloid Fibril Structural Variability Dependence on Initial Protein Folding State Mikalauskaite, Kamile Ziaunys, Mantas Smirnovas, Vytautas Int J Mol Sci Article Amyloid fibril formation is associated with several amyloidoses, including neurodegenerative Alzheimer’s or Parkinson’s diseases. The process of such fibrillar structure formation is still not fully understood, with new mechanistic insights appearing on a regular basis. This, in turn, has limited the development of potential anti-amyloid compounds, with only a handful of effective cures or treatment modalities available. One of the multiple amyloid aggregation factors that requires further examination is the ability of proteins to form multiple, structurally distinct aggregates, based on the environmental conditions. In this work, we examine how the initial folding state affects the fibrilization of lysozyme—an amyloidogenic protein, often used in protein aggregation studies. We show that there is a correlation between the initial state of the protein and the aggregate formation lag time, rate of elongation, resulting aggregate structural variability and dye-binding properties, as well as formation lag time and rate of elongation. MDPI 2022-05-12 /pmc/articles/PMC9141980/ /pubmed/35628230 http://dx.doi.org/10.3390/ijms23105421 Text en © 2022 by the authors. 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 Mikalauskaite, Kamile Ziaunys, Mantas Smirnovas, Vytautas Lysozyme Amyloid Fibril Structural Variability Dependence on Initial Protein Folding State |
title | Lysozyme Amyloid Fibril Structural Variability Dependence on Initial Protein Folding State |
title_full | Lysozyme Amyloid Fibril Structural Variability Dependence on Initial Protein Folding State |
title_fullStr | Lysozyme Amyloid Fibril Structural Variability Dependence on Initial Protein Folding State |
title_full_unstemmed | Lysozyme Amyloid Fibril Structural Variability Dependence on Initial Protein Folding State |
title_short | Lysozyme Amyloid Fibril Structural Variability Dependence on Initial Protein Folding State |
title_sort | lysozyme amyloid fibril structural variability dependence on initial protein folding state |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9141980/ https://www.ncbi.nlm.nih.gov/pubmed/35628230 http://dx.doi.org/10.3390/ijms23105421 |
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