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Investigation of serum amyloid a within animal species focusing on the 1-25 amino acid region
AA amyloidosis, characterized by the misfolding of serum amyloid A (SAA) protein, is the most common amyloid protein disorder across multiple species. SAA is a positive-acute phase protein synthesized by the liver in response to inflammation or stress, and it normally associates with high-density li...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Taylor & Francis
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10614707/ https://www.ncbi.nlm.nih.gov/pubmed/37800590 http://dx.doi.org/10.1080/01652176.2023.2267605 |
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author | Horgan, Natalie G. Moore, Kendall B. E. Fortin, Jessica S. |
author_facet | Horgan, Natalie G. Moore, Kendall B. E. Fortin, Jessica S. |
author_sort | Horgan, Natalie G. |
collection | PubMed |
description | AA amyloidosis, characterized by the misfolding of serum amyloid A (SAA) protein, is the most common amyloid protein disorder across multiple species. SAA is a positive-acute phase protein synthesized by the liver in response to inflammation or stress, and it normally associates with high-density lipoprotein at its N-terminus. In this study, we focused on the 1-25 amino acid (aa) region of the complete 104 aa SAA sequence to examine the aggregation propensity of AA amyloid. A library comprising eight peptides from different species was assembled for analysis. To access the aggregation propensity of each peptide region, a bioinformatic study was conducted using the algorithm TANGO. Congo red (CR) binding assays, Thioflavin T (ThT) assays, and transmission electron microscopy (TEM) were utilized to evaluate whether the synthesized peptides formed amyloid-like fibrils. All synthetic SAA 1-25 congeners resulted in amyloid-like fibrils formation (per CR and/or ThT staining and TEM detection) at the exception of the ferret SAA1-25 fragment, which generated plaque-like materials by TEM. Ten residues were preserved among SAA 1-25 congeners resulting in amyloid-like fibrils, i.e. F6, E9, A10, G13, D16, M17, A20, Y21, D23, and M24. Amino acid residues highlighted by this study may have a role in increasing the propensity for amyloid-like fibril formation. This study put an emphasis on region 1-25 in the mechanism of SAA1 misfolding. |
format | Online Article Text |
id | pubmed-10614707 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Taylor & Francis |
record_format | MEDLINE/PubMed |
spelling | pubmed-106147072023-10-31 Investigation of serum amyloid a within animal species focusing on the 1-25 amino acid region Horgan, Natalie G. Moore, Kendall B. E. Fortin, Jessica S. Vet Q Research Article AA amyloidosis, characterized by the misfolding of serum amyloid A (SAA) protein, is the most common amyloid protein disorder across multiple species. SAA is a positive-acute phase protein synthesized by the liver in response to inflammation or stress, and it normally associates with high-density lipoprotein at its N-terminus. In this study, we focused on the 1-25 amino acid (aa) region of the complete 104 aa SAA sequence to examine the aggregation propensity of AA amyloid. A library comprising eight peptides from different species was assembled for analysis. To access the aggregation propensity of each peptide region, a bioinformatic study was conducted using the algorithm TANGO. Congo red (CR) binding assays, Thioflavin T (ThT) assays, and transmission electron microscopy (TEM) were utilized to evaluate whether the synthesized peptides formed amyloid-like fibrils. All synthetic SAA 1-25 congeners resulted in amyloid-like fibrils formation (per CR and/or ThT staining and TEM detection) at the exception of the ferret SAA1-25 fragment, which generated plaque-like materials by TEM. Ten residues were preserved among SAA 1-25 congeners resulting in amyloid-like fibrils, i.e. F6, E9, A10, G13, D16, M17, A20, Y21, D23, and M24. Amino acid residues highlighted by this study may have a role in increasing the propensity for amyloid-like fibril formation. This study put an emphasis on region 1-25 in the mechanism of SAA1 misfolding. Taylor & Francis 2023-10-06 /pmc/articles/PMC10614707/ /pubmed/37800590 http://dx.doi.org/10.1080/01652176.2023.2267605 Text en © 2023 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group. https://creativecommons.org/licenses/by/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. The terms on which this article has been published allow the posting of the Accepted Manuscript in a repository by the author(s) or with their consent. |
spellingShingle | Research Article Horgan, Natalie G. Moore, Kendall B. E. Fortin, Jessica S. Investigation of serum amyloid a within animal species focusing on the 1-25 amino acid region |
title | Investigation of serum amyloid a within animal species focusing on the 1-25 amino acid region |
title_full | Investigation of serum amyloid a within animal species focusing on the 1-25 amino acid region |
title_fullStr | Investigation of serum amyloid a within animal species focusing on the 1-25 amino acid region |
title_full_unstemmed | Investigation of serum amyloid a within animal species focusing on the 1-25 amino acid region |
title_short | Investigation of serum amyloid a within animal species focusing on the 1-25 amino acid region |
title_sort | investigation of serum amyloid a within animal species focusing on the 1-25 amino acid region |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10614707/ https://www.ncbi.nlm.nih.gov/pubmed/37800590 http://dx.doi.org/10.1080/01652176.2023.2267605 |
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