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.
Condition-Dependent Coordination and Peroxidase Activity of Hemin-Aβ Complexes
Bacchella C.;Dell'Acqua S.;Monzani E.;Casella L.
2020-01-01
Abstract
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.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
