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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...

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Autores principales: 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
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
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.
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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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