Dataset Information

Condition-Dependent Coordination and Peroxidase Activity of Hemin-A? 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-A?40 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 A?16 and A?40 (up to 100 equivalents). Interaction and reactivity studies of aggregated A?40-hemin revealed enhanced peroxidase activity versus hemin alone. Comparison of the results obtained using A?16 and A?40 amyloid beta peptides revealed marked differences and provide insight into the potential effects of hemin-A? on neurological disease progression.

SUBMITTER: Bacchella C

PROVIDER: S-EPMC7662341 | biostudies-literature | 2020 Oct

REPOSITORIES: biostudies-literature

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

Bacchella Chiara C Brewster James T JT Bähring Steffen S Dell'Acqua Simone S Root Harrison D HD Thiabaud Gregory D GD Reuther James F JF Monzani Enrico E Sessler Jonathan L JL Casella Luigi L

Molecules (Basel, Switzerland) 20201030 21

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 ...[more]

PMID: 33143109

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Project description:Accurately detecting dynamic changes in bioactive small molecules in real-time is very challenging. In this study, a hemin-based peptide assembly was rationally designed for the colorimetric detection of active small molecules. Hemin-functionalized peptide nanotubes were obtained through the direct incubation of hemin (hemin@PNTs) and peptide nanotubes (PNTs) or were coassembled with the heptapeptide Ac-KLVFFAL-NH2 via electrostatic, π-π stacking, and hydrophobic interactions (hemin-PNTs). This new substance is significant because it exhibits the benefits of both hemin and PNTs as well as some special qualities. First, hemin-PNTs exhibited higher intrinsic peroxidase-like activity, which, in the presence of H2O2, could catalyze the oxidation of the substrate 3,3',5,5'-tetramethylbenzidine (TMB) to yield a typical blue solution after 10 min at 25 ℃. Second, hemin-PNTs showed significantly higher activity than that of hemin, PNTs alone, or hemin@PNTs. Hemin-PNTs with a 20.0% hemin content may cooperate to improve catalytic activity. The catalytic activity was dependent on the reaction temperature, pH, reaction time, and H2O2 concentration. The nature of the TMB-catalyzed reaction may arise from the production of hydroxyl radicals. Fluorescence analysis was used to demonstrate the catalytic mechanism. According to this investigation, a new highly selective and sensitive colorimetric technique for detecting glutathione (GSH), L-cysteine, and glucose was established. The strategy demonstrated excellent sensitivity for GSH in the range of 1 to 30 μM with a 0.51 μM detection limit. Importantly, this glucose detection technique, which employs glucose oxidase and hemin-PNTs, is simple and inexpensive, with a 0.1 μM to 1.0 mM linear range and a 15.2 μM detection limit. Because of their low cost and high catalytic activity, hemin-PNTs are an excellent choice for biocatalysts in a diverse range of potential applications, including applications in clinical diagnostics, environmental chemistry, and biotechnology.

Dataset Information

Condition-Dependent Coordination and Peroxidase Activity of Hemin-A? Complexes.

Publications

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

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