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

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

Institut for Fysik, Kemi og Farmaci

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › peer review

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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.

Originalsprog	Engelsk
Artikelnummer	5044
Tidsskrift	Molecules
Vol/bind	25
Udgave nummer	21
Antal sider	13
ISSN	1420-3049
DOI	https://doi.org/10.3390/molecules25215044
Status	Udgivet - 30. okt. 2020

Bibliografisk note

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

Dokumenter og links

10.3390/molecules25215044Licens: CC BY

Open Access VersionForlagets udgivne version, 1,59 MBLicens: CC BY
134772.cif

Citationsformater

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title = "Condition-Dependent Coordination and Peroxidase Activity of Hemin-Aβ Complexes",

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.",

author = "Chiara Bacchella and Brewster, {James T.} and Steffen B{\"a}hring and Simone Dell{\textquoteright}Acqua and Root, {Harrison D.} and Thiabaud, {Gregory D.} and Reuther, {James F.} and Enrico Monzani and Sessler, {Jonathan L.} and Luigi Casella",

note = "Peer-reviewed https://www.mdpi.com/1420-3049/25/21/5044 ",

year = "2020",

month = oct,

day = "30",

doi = "10.3390/molecules25215044",

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T1 - Condition-Dependent Coordination and Peroxidase Activity of Hemin-Aβ Complexes

AU - Bacchella , Chiara

AU - Brewster, James T.

AU - Bähring, Steffen

AU - Dell’Acqua, Simone

AU - Root, Harrison D.

AU - Thiabaud , Gregory D.

AU - Reuther , James F.

AU - Monzani , Enrico

AU - Sessler, Jonathan L.

AU - Casella, Luigi

N1 - Peer-reviewed https://www.mdpi.com/1420-3049/25/21/5044

PY - 2020/10/30

Y1 - 2020/10/30

N2 - 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.

AB - 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.

U2 - 10.3390/molecules25215044

DO - 10.3390/molecules25215044

M3 - Journal article

C2 - 33143109

SN - 1420-3049

VL - 25

JO - Molecules

JF - Molecules

IS - 21

M1 - 5044

ER -

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

Abstract

Bibliografisk note

Dokumenter og links

Fingeraftryk

Citationsformater