Condition-Dependent Coordination and Peroxidase Activity of Hemin-Aβ Complexes

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

doi:10.3390/molecules25215044

Molecules (Oct 2020)

Condition-Dependent Coordination and Peroxidase Activity of Hemin-Aβ Complexes

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

Affiliations

Chiara Bacchella: Department of Chemistry, University of Pavia, Via Taramelli 12, 27100 Pavia, Italy
James T. Brewster: Department of Chemistry, The University of Texas at Austin, 105 East 24th, Street-Stop A5300, Austin, TX 78712-1224, USA
Steffen Bähring: Department of Physics, Chemistry, and Pharmacy, University of Southern Denmark, Campusvej 55, DK-5230 Odense, Denmark
Simone Dell’Acqua: Department of Chemistry, University of Pavia, Via Taramelli 12, 27100 Pavia, Italy
Harrison D. Root: Department of Chemistry, The University of Texas at Austin, 105 East 24th, Street-Stop A5300, Austin, TX 78712-1224, USA
Gregory D. Thiabaud: Department of Chemistry, The University of Texas at Austin, 105 East 24th, Street-Stop A5300, Austin, TX 78712-1224, USA
James F. Reuther: Department of Chemistry, The University of Texas at Austin, 105 East 24th, Street-Stop A5300, Austin, TX 78712-1224, USA
Enrico Monzani: Department of Chemistry, University of Pavia, Via Taramelli 12, 27100 Pavia, Italy
Jonathan L. Sessler: Department of Chemistry, The University of Texas at Austin, 105 East 24th, Street-Stop A5300, Austin, TX 78712-1224, USA
Luigi Casella: Department of Chemistry, University of Pavia, Via Taramelli 12, 27100 Pavia, Italy

DOI: https://doi.org/10.3390/molecules25215044
Journal volume & issue: Vol. 25, no. 21
p. 5044

Abstract

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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-Aβ40 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 Aβ16 and Aβ40 (up to 100 equivalents). Interaction and reactivity studies of aggregated Aβ40-hemin revealed enhanced peroxidase activity versus hemin alone. Comparison of the results obtained using Aβ16 and Aβ40 amyloid beta peptides revealed marked differences and provide insight into the potential effects of hemin-Aβ on neurological disease progression.

Published in Molecules

ISSN: 1420-3049 (Online)
Publisher: MDPI AG
Country of publisher: Switzerland
LCC subjects: Science: Chemistry: Organic chemistry
Website: http://www.mdpi.com/journal/molecules

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