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...
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MDPI AG
2021-05-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/22/11/5896 |
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| author | Ekaterina A. Litus Alexey S. Kazakov Evgenia I. Deryusheva Ekaterina L. Nemashkalova Marina P. Shevelyova Aliya A. Nazipova Maria E. Permyakova Elena V. Raznikova Vladimir N. Uversky Sergei E. Permyakov |
| author_facet | Ekaterina A. Litus Alexey S. Kazakov Evgenia I. Deryusheva Ekaterina L. Nemashkalova Marina P. Shevelyova Aliya A. Nazipova Maria E. Permyakova Elena V. Raznikova Vladimir N. Uversky Sergei E. Permyakov |
| author_sort | Ekaterina A. Litus |
| collection | DOAJ |
| 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<sub>40</sub>/Aβ<sub>42</sub>, 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. |
| first_indexed | 2024-03-10T10:52:00Z |
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| id | doaj.art-bd22e6b9c6eb4bdb811d289be5e5dbc3 |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-10T10:52:00Z |
| publishDate | 2021-05-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-bd22e6b9c6eb4bdb811d289be5e5dbc32023-11-21T22:12:09ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672021-05-012211589610.3390/ijms22115896Serotonin Promotes Serum Albumin Interaction with the Monomeric Amyloid β PeptideEkaterina A. Litus0Alexey S. Kazakov1Evgenia I. Deryusheva2Ekaterina L. Nemashkalova3Marina P. Shevelyova4Aliya A. Nazipova5Maria E. Permyakova6Elena V. Raznikova7Vladimir N. Uversky8Sergei E. Permyakov9Institute for Biological Instrumentation, Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences, Pushchino, 142290 Moscow, RussiaInstitute for Biological Instrumentation, Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences, Pushchino, 142290 Moscow, RussiaInstitute for Biological Instrumentation, Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences, Pushchino, 142290 Moscow, RussiaInstitute for Biological Instrumentation, Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences, Pushchino, 142290 Moscow, RussiaInstitute for Biological Instrumentation, Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences, Pushchino, 142290 Moscow, RussiaInstitute for Biological Instrumentation, Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences, Pushchino, 142290 Moscow, RussiaInstitute for Biological Instrumentation, Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences, Pushchino, 142290 Moscow, RussiaInstitute for Biological Instrumentation, Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences, Pushchino, 142290 Moscow, RussiaDepartment of Molecular Medicine and USF Health Byrd Alzheimer’s Research Institute, Morsani College of Medicine, University of South Florida, Tampa, FL 33612, USAInstitute for Biological Instrumentation, Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences, Pushchino, 142290 Moscow, RussiaPrevention 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<sub>40</sub>/Aβ<sub>42</sub>, 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.https://www.mdpi.com/1422-0067/22/11/5896Alzheimer’s diseasehuman serum albuminamyloid β peptideserotonintryptophansurface plasmon resonance |
| spellingShingle | Ekaterina A. Litus Alexey S. Kazakov Evgenia I. Deryusheva Ekaterina L. Nemashkalova Marina P. Shevelyova Aliya A. Nazipova Maria E. Permyakova Elena V. Raznikova Vladimir N. Uversky Sergei E. Permyakov Serotonin Promotes Serum Albumin Interaction with the Monomeric Amyloid β Peptide International Journal of Molecular Sciences Alzheimer’s disease human serum albumin amyloid β peptide serotonin tryptophan surface plasmon resonance |
| 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 | Alzheimer’s disease human serum albumin amyloid β peptide serotonin tryptophan surface plasmon resonance |
| url | https://www.mdpi.com/1422-0067/22/11/5896 |
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