Activation of catalase by pioglitazone: Multiple spectroscopic methods combined with molecular docking studies

Yekta, Reza; Dehghan, Gholamreza; Rashtbari, Samaneh; Moosavi-Movahedi, Ali Akbar

doi:10.1002/jmr.2648

Cited by 37 publications

(9 citation statements)

References 36 publications

(77 reference statements)

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“…The fluorescence spectrum of standard CAT showed an emission band with a maximum intensity at 334.5 nm, in accordance with data from the literature. 45,46 In contrast, the negative control (denatured CAT) showed a weak fluorescence emission characterized by the absence of the band at 334 nm. Compared to the positive control, solutions of CAT released from the particles exhibited emission peaks with decreased intensity but a similar band shape, indicating that the tertiary structure of the protein was mainly preserved.…”

Section: ■ Results and Discussionmentioning

confidence: 97%

Solid Lipid Microparticles for Oral Delivery of Catalase: Focus on the Protein Structural Integrity and Gastric Protection

et al. 2020

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Protein inactivation either during the production process or along the gastrointestinal tract is the major problem associated with the development of oral delivery systems for biological drugs. This work presents an evaluation of the structural integrity and the biological activity of a model protein, catalase, after its encapsulation in glyceryl trimyristate-based solid lipid microparticles (SLMs) obtained by the spray congealing technology. Circular dichroism and fluorescence spectroscopies were used to assess the integrity of catalase released from SLMs. The results confirmed that no conformational change occurred during the production process and both the secondary and tertiary structures were retained. Catalase is highly sensitive to temperature and undergoes denaturation above 60 °C; nevertheless, spray congealing allowed the retention of most biological activity due to the loading of the drug at the solid state, markedly reducing the risk of denaturation. Catalase activity after exposure to simulated gastric conditions (considering both acidic pH and the presence of gastric digestive hydrolases) ranged from 35 to 95% depending on the carrier: increasing of both the fatty acid chain length and the degree of substitution of the glyceride enhanced residual enzyme activity. SLMs allowed the protein release in a simulated intestinal environment and were not cytotoxic against HT29 cells. In conclusion, the encapsulation of proteins into SLMs by spray congealing might be a promising strategy for the formulation of nontoxic and inexpensive oral biotherapeutic products.

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Section: ■ Results and Discussionmentioning

confidence: 97%

Solid Lipid Microparticles for Oral Delivery of Catalase: Focus on the Protein Structural Integrity and Gastric Protection

et al. 2020

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“…The fluorescence quenching data follow the Stern‐Volmer equation :

\frac{F_{0}}{F} = 1 + k_{q} τ_{0} ([], Q) = 1 + K_{sv} ([], Q),

where F 0 and F are the fluorescence intensities of N,S‐CDs in the absence and presence of the quencher (BHb) , k q is the rate constant of quenching, K sv is the Stern‐Volmer quenching constant, and [ Q ] is the quencher concentration. The Stern‐Volmer plot shown in Figure 4B fits a linear equation in the concentration range of 1.49–6.96 μmol L −1 ( R 2 = 0.9886) with K sv = 5.18 × 10 5 and k q =6.47 × 10 13 M −1 s −1 , respectively.…”

Section: Resultsmentioning

confidence: 99%

Nitrogen and sulfur co‐doped carbon nanodots toward bovine hemoglobin: A fluorescence quenching mechanism investigation

Wang

Xiang

Milcovich

et al. 2018

J of Molecular Recognition

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A deep understanding of the molecular interactions of carbon nanodots with biomacromolecules is essential for wider applications of carbon nanodots both in vitro and in vivo. Herein, nitrogen and sulfur co-doped carbon dots (N,S-CDs) with a quantum yield of 16% were synthesized by a 1-step hydrothermal method. The N,S-CDs exhibited a good dispersion, with a graphite-like structure, along with the fluorescence lifetime of approximately 7.50 ns. Findings showed that the fluorescence of the N,S-CDs was effectively quenched by bovine hemoglobin as a result of the static fluorescence quenching. The mentioned quenching mechanism was investigated by the Stern-Volmer equation, temperature-dependent quenching, and fluorescence lifetime measurements. The binding constants, number of binding sites, and the binding average distance between the energy donor N,S-CDs and acceptor bovine hemoglobin were calculated as well. These findings will provide for valuable insights on the future bioapplications of N,S-CDs.

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“…1 . The review of the literature shows that catalase binds with other compounds and simvastatin binds only to inhibitors of HMG-CoA reductase in particular ( Yekta et al., 2017 ; Huo et al., 2020 ; Shahraki et al., 2020 ; Nazir et al., 2018 ). However, the binding of simvastatin with catalase has never been reported earlier.…”

Section: Discussionmentioning

confidence: 99%

Simvastatin ameliorates oxidative stress levels in HepG2 cells and hyperlipidemic rats

Verma

Makwana

Paliwal

et al. 2022

Current Research in Pharmacology and Drug Discovery

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Simvastatin is an established anti-hyperlipidemic drug and few studies have indicated its role in the mitigation of oxidative stress. However, a systematic study considering molecular binding/interaction of simvastatin with anti-oxidant enzymes followed by confirmational in vitro and in vivo studies have never been done. We investigated the molecular binding of simvastatin with multiple anti-oxidant enzymes and assessed their levels after the treatment of simvastatin in vitro and in vivo . This study is the first to show the molecular binding of simvastatin to catalase through molecular docking analysis. Moreover, the anti-oxidative properties of simvastatin have not been studied in Lipopolysaccharide (LPS) induced oxidative stress in HepG2 cells. We found that simvastatin effectively attenuated oxidative stress in LPS induced HepG2 cells and high-fat diet (HFD) fed hyperlipidemic rats by increasing the levels of antioxidant enzymes. The activity of catalase and superoxide dismutase (SOD) both increased significantly in oxidatively stressed HepG2 cells after the treatment with simvastatin (10 μM, 24 h). In addition to this, he original cell morphology of oxidatively stressed cells was restored by simvastatin, and an increase in antioxidant enzymes, catalase (0.08 U/cells to 0.12 U/cells), and SOD (0.57 U/cells to 0.74 U/cells) was also noted in HepG2 cells. Furthermore, a significant increase in the antioxidant enzymes such as Catalase, SOD, and reduced glutathione (GSH) was noted after simvastatin treatment in the HFD model. Moreover, we also observed degradation of by-products of lipid peroxidation thiobarbituric acid reactive substances (TBARs), nitric oxide (NO), and protein carbonyl levels. This indicates that simvastatin enhances anti-oxidant enzyme activities and can be repurposed for the treatment of oxidative stress in liver diseases in humans after extensive clinical trials.

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Activation of catalase by pioglitazone: Multiple spectroscopic methods combined with molecular docking studies

Cited by 37 publications

References 36 publications

Solid Lipid Microparticles for Oral Delivery of Catalase: Focus on the Protein Structural Integrity and Gastric Protection

Solid Lipid Microparticles for Oral Delivery of Catalase: Focus on the Protein Structural Integrity and Gastric Protection

Nitrogen and sulfur co‐doped carbon nanodots toward bovine hemoglobin: A fluorescence quenching mechanism investigation

Simvastatin ameliorates oxidative stress levels in HepG2 cells and hyperlipidemic rats

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