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Serotonin Promotes Serum Albumin Interaction with the Monomeric Amyloid β Peptide
Prevention of amyloid β peptide (Aβ) deposition via facilitation of Aβ binding to its natural depot, human serum albumin (HSA), is a promising approach to preclude Alzheimer’s disease (AD) onset and progression. Previously, we demonstrated the ability of natural HSA ligands, fatty acids, to improve...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8199245/ https://www.ncbi.nlm.nih.gov/pubmed/34072751 http://dx.doi.org/10.3390/ijms22115896 |
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author | Litus, Ekaterina A. Kazakov, Alexey S. Deryusheva, Evgenia I. Nemashkalova, Ekaterina L. Shevelyova, Marina P. Nazipova, Aliya A. Permyakova, Maria E. Raznikova, Elena V. Uversky, Vladimir N. Permyakov, Sergei E. |
author_facet | Litus, Ekaterina A. Kazakov, Alexey S. Deryusheva, Evgenia I. Nemashkalova, Ekaterina L. Shevelyova, Marina P. Nazipova, Aliya A. Permyakova, Maria E. Raznikova, Elena V. Uversky, Vladimir N. Permyakov, Sergei E. |
author_sort | Litus, Ekaterina A. |
collection | PubMed |
description | Prevention of amyloid β peptide (Aβ) deposition via facilitation of Aβ binding to its natural depot, human serum albumin (HSA), is a promising approach to preclude Alzheimer’s disease (AD) onset and progression. Previously, we demonstrated the ability of natural HSA ligands, fatty acids, to improve the affinity of this protein to monomeric Aβ by a factor of 3 (BBRC, 510(2), 248–253). Using plasmon resonance spectroscopy, we show here that another HSA ligand related to AD pathogenesis, serotonin (SRO), increases the affinity of the Aβ monomer to HSA by a factor of 7/17 for Aβ(40)/Aβ(42), respectively. Meanwhile, the structurally homologous SRO precursor, tryptophan (TRP), does not affect HSA’s affinity to monomeric Aβ, despite slowdown of the association and dissociation processes. Crosslinking with glutaraldehyde and dynamic light scattering experiments reveal that, compared with the TRP-induced effects, SRO binding causes more marked changes in the quaternary structure of HSA. Furthermore, molecular docking reveals distinct structural differences between SRO/TRP complexes with HSA. The disintegration of the serotonergic system during AD pathogenesis may contribute to Aβ release from HSA in the central nervous system due to impairment of the SRO-mediated Aβ trapping by HSA. |
format | Online Article Text |
id | pubmed-8199245 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-81992452021-06-14 Serotonin Promotes Serum Albumin Interaction with the Monomeric Amyloid β Peptide Litus, Ekaterina A. Kazakov, Alexey S. Deryusheva, Evgenia I. Nemashkalova, Ekaterina L. Shevelyova, Marina P. Nazipova, Aliya A. Permyakova, Maria E. Raznikova, Elena V. Uversky, Vladimir N. Permyakov, Sergei E. Int J Mol Sci Article Prevention of amyloid β peptide (Aβ) deposition via facilitation of Aβ binding to its natural depot, human serum albumin (HSA), is a promising approach to preclude Alzheimer’s disease (AD) onset and progression. Previously, we demonstrated the ability of natural HSA ligands, fatty acids, to improve the affinity of this protein to monomeric Aβ by a factor of 3 (BBRC, 510(2), 248–253). Using plasmon resonance spectroscopy, we show here that another HSA ligand related to AD pathogenesis, serotonin (SRO), increases the affinity of the Aβ monomer to HSA by a factor of 7/17 for Aβ(40)/Aβ(42), respectively. Meanwhile, the structurally homologous SRO precursor, tryptophan (TRP), does not affect HSA’s affinity to monomeric Aβ, despite slowdown of the association and dissociation processes. Crosslinking with glutaraldehyde and dynamic light scattering experiments reveal that, compared with the TRP-induced effects, SRO binding causes more marked changes in the quaternary structure of HSA. Furthermore, molecular docking reveals distinct structural differences between SRO/TRP complexes with HSA. The disintegration of the serotonergic system during AD pathogenesis may contribute to Aβ release from HSA in the central nervous system due to impairment of the SRO-mediated Aβ trapping by HSA. MDPI 2021-05-31 /pmc/articles/PMC8199245/ /pubmed/34072751 http://dx.doi.org/10.3390/ijms22115896 Text en © 2021 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 Litus, Ekaterina A. Kazakov, Alexey S. Deryusheva, Evgenia I. Nemashkalova, Ekaterina L. Shevelyova, Marina P. Nazipova, Aliya A. Permyakova, Maria E. Raznikova, Elena V. Uversky, Vladimir N. Permyakov, Sergei E. Serotonin Promotes Serum Albumin Interaction with the Monomeric Amyloid β Peptide |
title | Serotonin Promotes Serum Albumin Interaction with the Monomeric Amyloid β Peptide |
title_full | Serotonin Promotes Serum Albumin Interaction with the Monomeric Amyloid β Peptide |
title_fullStr | Serotonin Promotes Serum Albumin Interaction with the Monomeric Amyloid β Peptide |
title_full_unstemmed | Serotonin Promotes Serum Albumin Interaction with the Monomeric Amyloid β Peptide |
title_short | Serotonin Promotes Serum Albumin Interaction with the Monomeric Amyloid β Peptide |
title_sort | serotonin promotes serum albumin interaction with the monomeric amyloid β peptide |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8199245/ https://www.ncbi.nlm.nih.gov/pubmed/34072751 http://dx.doi.org/10.3390/ijms22115896 |
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