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*

*Kontaktforfatter for dette arbejde

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Abstrakt

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.
OriginalsprogEngelsk
Artikelnummer5044
TidsskriftMolecules
Vol/bind25
Udgave nummer21
Antal sider13
ISSN1420-3049
DOI
StatusUdgivet - 30. okt. 2020

Bibliografisk note

Peer-reviewed<br/>https://www.mdpi.com/1420-3049/25/21/5044<br/>

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