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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| Format: | Article |
| Language: | English |
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MDPI AG
2020-10-01
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| Series: | Molecules |
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| Online Access: | https://www.mdpi.com/1420-3049/25/21/5044 |
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| author | Chiara Bacchella James T. Brewster Steffen Bähring Simone Dell’Acqua Harrison D. Root Gregory D. Thiabaud James F. Reuther Enrico Monzani Jonathan L. Sessler Luigi Casella |
| author_facet | Chiara Bacchella James T. Brewster Steffen Bähring Simone Dell’Acqua Harrison D. Root Gregory D. Thiabaud James F. Reuther Enrico Monzani Jonathan L. Sessler Luigi Casella |
| author_sort | Chiara Bacchella |
| collection | DOAJ |
| 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<sub>40</sub> 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<sub>16</sub> and Aβ<sub>40</sub> (up to 100 equivalents). Interaction and reactivity studies of aggregated Aβ<sub>40</sub>-hemin revealed enhanced peroxidase activity versus hemin alone. Comparison of the results obtained using Aβ<sub>16</sub> and Aβ<sub>40</sub> amyloid beta peptides revealed marked differences and provide insight into the potential effects of hemin-Aβ on neurological disease progression. |
| first_indexed | 2024-03-10T15:12:45Z |
| format | Article |
| id | doaj.art-33fc3ebe28194fffa7663bf54a5c8cb0 |
| institution | Directory Open Access Journal |
| issn | 1420-3049 |
| language | English |
| last_indexed | 2024-03-10T15:12:45Z |
| publishDate | 2020-10-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Molecules |
| spelling | doaj.art-33fc3ebe28194fffa7663bf54a5c8cb02023-11-20T19:11:04ZengMDPI AGMolecules1420-30492020-10-012521504410.3390/molecules25215044Condition-Dependent Coordination and Peroxidase Activity of Hemin-Aβ ComplexesChiara Bacchella0James T. Brewster1Steffen Bähring2Simone Dell’Acqua3Harrison D. Root4Gregory D. Thiabaud5James F. Reuther6Enrico Monzani7Jonathan L. Sessler8Luigi Casella9Department of Chemistry, University of Pavia, Via Taramelli 12, 27100 Pavia, ItalyDepartment of Chemistry, The University of Texas at Austin, 105 East 24th, Street-Stop A5300, Austin, TX 78712-1224, USADepartment of Physics, Chemistry, and Pharmacy, University of Southern Denmark, Campusvej 55, DK-5230 Odense, DenmarkDepartment of Chemistry, University of Pavia, Via Taramelli 12, 27100 Pavia, ItalyDepartment of Chemistry, The University of Texas at Austin, 105 East 24th, Street-Stop A5300, Austin, TX 78712-1224, USADepartment of Chemistry, The University of Texas at Austin, 105 East 24th, Street-Stop A5300, Austin, TX 78712-1224, USADepartment of Chemistry, The University of Texas at Austin, 105 East 24th, Street-Stop A5300, Austin, TX 78712-1224, USADepartment of Chemistry, University of Pavia, Via Taramelli 12, 27100 Pavia, ItalyDepartment of Chemistry, The University of Texas at Austin, 105 East 24th, Street-Stop A5300, Austin, TX 78712-1224, USADepartment of Chemistry, University of Pavia, Via Taramelli 12, 27100 Pavia, ItalyThe 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<sub>40</sub> 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<sub>16</sub> and Aβ<sub>40</sub> (up to 100 equivalents). Interaction and reactivity studies of aggregated Aβ<sub>40</sub>-hemin revealed enhanced peroxidase activity versus hemin alone. Comparison of the results obtained using Aβ<sub>16</sub> and Aβ<sub>40</sub> amyloid beta peptides revealed marked differences and provide insight into the potential effects of hemin-Aβ on neurological disease progression.https://www.mdpi.com/1420-3049/25/21/5044central nervous systemneurodegenerationAlzheimer’s diseaseheminperoxidase |
| spellingShingle | Chiara Bacchella James T. Brewster Steffen Bähring Simone Dell’Acqua Harrison D. Root Gregory D. Thiabaud James F. Reuther Enrico Monzani Jonathan L. Sessler Luigi Casella Condition-Dependent Coordination and Peroxidase Activity of Hemin-Aβ Complexes Molecules central nervous system neurodegeneration Alzheimer’s disease hemin peroxidase |
| 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 | central nervous system neurodegeneration Alzheimer’s disease hemin peroxidase |
| url | https://www.mdpi.com/1420-3049/25/21/5044 |
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