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Condition-Dependent Coordination and Peroxidase Activity of Hemin-Aβ Complexes
The peroxidase activity of hemin-peptide complexes remains a potential factor in oxidative damage relevant to neurodegeneration. Here, we present the effect of temperature, ionic strength, and pH relevant to pathophysiological conditions on the dynamic equilibrium between high-spin and low-spin hemi...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7662341/ https://www.ncbi.nlm.nih.gov/pubmed/33143109 http://dx.doi.org/10.3390/molecules25215044 |
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author | Bacchella, Chiara Brewster, James T. Bähring, Steffen Dell’Acqua, Simone Root, Harrison D. Thiabaud, Gregory D. Reuther, James F. Monzani, Enrico Sessler, Jonathan L. Casella, Luigi |
author_facet | Bacchella, Chiara Brewster, James T. Bähring, Steffen Dell’Acqua, Simone Root, Harrison D. Thiabaud, Gregory D. Reuther, James F. Monzani, Enrico Sessler, Jonathan L. Casella, Luigi |
author_sort | Bacchella, Chiara |
collection | PubMed |
description | The peroxidase activity of hemin-peptide complexes remains a potential factor in oxidative damage relevant to neurodegeneration. Here, we present the effect of temperature, ionic strength, and pH relevant to pathophysiological conditions on the dynamic equilibrium between high-spin and low-spin hemin-Aβ(40) constructs. This influence on peroxidase activity was also demonstrated using 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) and dopamine (DA) oxidation rate analyses with increasing ratios of Aβ(16) and Aβ(40) (up to 100 equivalents). Interaction and reactivity studies of aggregated Aβ(40)-hemin revealed enhanced peroxidase activity versus hemin alone. Comparison of the results obtained using Aβ(16) and Aβ(40) amyloid beta peptides revealed marked differences and provide insight into the potential effects of hemin-Aβ on neurological disease progression. |
format | Online Article Text |
id | pubmed-7662341 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-76623412020-11-14 Condition-Dependent Coordination and Peroxidase Activity of Hemin-Aβ Complexes Bacchella, Chiara Brewster, James T. Bähring, Steffen Dell’Acqua, Simone Root, Harrison D. Thiabaud, Gregory D. Reuther, James F. Monzani, Enrico Sessler, Jonathan L. Casella, Luigi Molecules Article The peroxidase activity of hemin-peptide complexes remains a potential factor in oxidative damage relevant to neurodegeneration. Here, we present the effect of temperature, ionic strength, and pH relevant to pathophysiological conditions on the dynamic equilibrium between high-spin and low-spin hemin-Aβ(40) constructs. This influence on peroxidase activity was also demonstrated using 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) and dopamine (DA) oxidation rate analyses with increasing ratios of Aβ(16) and Aβ(40) (up to 100 equivalents). Interaction and reactivity studies of aggregated Aβ(40)-hemin revealed enhanced peroxidase activity versus hemin alone. Comparison of the results obtained using Aβ(16) and Aβ(40) amyloid beta peptides revealed marked differences and provide insight into the potential effects of hemin-Aβ on neurological disease progression. MDPI 2020-10-30 /pmc/articles/PMC7662341/ /pubmed/33143109 http://dx.doi.org/10.3390/molecules25215044 Text en © 2020 by the authors. 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 (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Bacchella, Chiara Brewster, James T. Bähring, Steffen Dell’Acqua, Simone Root, Harrison D. Thiabaud, Gregory D. Reuther, James F. Monzani, Enrico Sessler, Jonathan L. Casella, Luigi Condition-Dependent Coordination and Peroxidase Activity of Hemin-Aβ Complexes |
title | Condition-Dependent Coordination and Peroxidase Activity of Hemin-Aβ Complexes |
title_full | Condition-Dependent Coordination and Peroxidase Activity of Hemin-Aβ Complexes |
title_fullStr | Condition-Dependent Coordination and Peroxidase Activity of Hemin-Aβ Complexes |
title_full_unstemmed | Condition-Dependent Coordination and Peroxidase Activity of Hemin-Aβ Complexes |
title_short | Condition-Dependent Coordination and Peroxidase Activity of Hemin-Aβ Complexes |
title_sort | condition-dependent coordination and peroxidase activity of hemin-aβ complexes |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7662341/ https://www.ncbi.nlm.nih.gov/pubmed/33143109 http://dx.doi.org/10.3390/molecules25215044 |
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