Study on the interaction between salicylic acid and catalase by spectroscopic methods

Wu, Yunhua

doi:10.1016/j.jpba.2007.03.016

Cited by 18 publications

(7 citation statements)

References 21 publications

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“…The secondary structure was determined using SELCON3, software for protein secondary structure analysis. The protein secondary conformation was found to be 26.7% α‐helix, 20.7% β‐sheet, 24.6% β‐turns, and 28.7% random coil, respectively, which is in close agreement with the previous reports . By this method, it was found that upon complexation with MWCNTs (10 mg/L), the α‐helix content of the protein decreased from 26.7% to 25.1% with an increase in the β‐sheet from 20.7% to 23.4% (Table ).…”

Section: Resultssupporting

confidence: 89%

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Probing the Interaction of Mutiwalled Carbon Nanotubes and Catalase: Mutispectroscopic Approach

Sheng

Lü

et al. 2012

J Biochem & Molecular Tox

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In this study, the mechanism of the interaction between multiwalled carbon nanotubes (MWCNTs) and catalase was investigated by fluorescence, UV-vis, and circular dichroism (CD) spectroscopy under physiological conditions. The fluorescence quenching mechanism of catalase by MWCNTs was shown to be a static quenching procedure and was a result of the formation of a catalase-MWCNT complex. The secondary structure and conformation of the catalase adsorbed on MWCNTs was determined by CD and UV-vis spectroscopy, and the results indicate that the catalase in this complex is partially unfolded with its lost in α-helical content and obtainment in β-sheet content. Moreover, binding of MWCNTs to catalase inhibited the enzymatic activity, which may trigger some toxic effects and undesirable physiological consequences.

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Section: Resultssupporting

confidence: 89%

“…Our results suggest that binding of MWCNTs to catalase induced secondary structural changes and hydrogen‐bond network destruction . Several previous reports also indicate that conformational changes occur in catalase due to complexation with ligands .…”

Section: Resultssupporting

confidence: 69%

Probing the Interaction of Mutiwalled Carbon Nanotubes and Catalase: Mutispectroscopic Approach

Sheng

Lü

et al. 2012

J Biochem & Molecular Tox

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“…Characteristic information on the microenvironmental changes in the vicinity of fluorophores was investigated by synchronous fluorescence spectra. When Δλ is set at 15 nm, the fluorescence spectra give information for Tyr, and 60 nm for Trp . The synchronous fluorescence spectra of the HSA–keracyanin system are shown in Figure .…”

Section: Resultsmentioning

confidence: 99%

Separation and Identification of Anthocyanin Extracted from Mulberry Fruit and the Pigment Binding Properties toward Human Serum Albumin

Feng

Wang

Zhao

et al. 2014

J. Agric. Food Chem.

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Purple pigments were isolated from mulberry extracts using preparative high-speed countercurrent chromatography (HSCCC) and identified by ESI-MS/MS and high performance liquid chromatography (HPLC) techniques. The solvent system containing methyl tert-butyl ether, 1-butanol, acetonitrile, water, and trifluoroacetic acid (10:30:10:50:0.05; %, v/v) was developed in order to separate anthocyanins with different polarities. Cyanidin 3-O-(6″-O-α-rhamnopyranosyl-β-galactopyranoside) (also known as keracyanin) is the major component present in mulberry (41.3%). Other isolated pigments are cyanidin 3-O-(6″-O-α-rhamnopyranosyl-β-glucopyranoside) and petunidin 3-O-β-glucopyranoside. The binding characteristics of keracyanin with human serum albumin (HSA) were investigated by fluorescence and circular dichroism (CD) spectroscopy. Spectroscopic analysis reveals that HSA fluorescence quenched by keracyanin follows a static mode. Binding of keracyanin to HSA mainly depends on van der Waals force or H-bonds with average binding distance of 2.82 nm. The results from synchronous fluorescence, three-dimensional fluorescence, and CD spectra show that adaptive structure rearrangement and decrease of α-helical structure occur in the presence of keracyanin.

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“…The concentration of CAT was determined after resuspension in 10 mM HEPES (4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid) buffer using its absorbance at 280 nm, with ε = 246 000 cm −1 M −1 . 25 The concentration of the SOD solution was determined by measuring the Cu and Zn contents of the protein suspension in 10 mM HEPES (pH = 7.0) using an inductively coupled plasma spectrometer (Agilent, 7700x ICP-MS).…”

Section: Silver Nanoparticles and Proteinsmentioning

confidence: 99%

Interaction of silver nanoparticles with antioxidant enzymes

Liu

Worms

Slaveykova

2020

Environ. Sci.: Nano

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Oxidative stress is accepted as a key mechanism of silver nanoparticle (AgNP) toxicity in living organisms. Therefore, mechanistic studies related to the impact of AgNPs on the structure and function of antioxidant enzymes at the molecular level are essential for a comprehensive evaluation of their toxicity. By using a combination of spectroscopic, imaging and fractionation techniques, we explored the interactions between citrate-coated AgNPs (20 nm) and two key antioxidant enzymes: catalase (CAT) and superoxide dismutase (SOD). Both enzymes interacted with AgNPs by forming surface complexes. Only CAT was able to promote AgNP dissolution, without the impact of the released Ag ions on its heme cofactor. Instead, our results suggest that the formation of the AgNP-CAT complex induced conformation changes in the CAT, which resulted in an impairment of its enzymatic activity together with AgĲI) adsorption. By contrast, the formation of the AgNP-SOD complex has only a marginal influence on the protein conformation and has no impact on its metallic cofactors, and thus its enzymatic activity. Overall, the results showed that the changes in the protein conformation and the dissolution of AgNPs depended on the protein structure and could result in different degrees of enzymatic activity modulation.Excessive production of reactive oxygen species in cells by direct interaction with particles and/or dissolved species is currently accepted as one of the main mechanisms of cellular toxicity of engineered nanoparticles. Therefore, studies related to the impact of silver nanoparticles (AgNPs) on the structure and function of antioxidant enzymes at the molecular level are crucial for a comprehensive evaluation of their toxicity. This study suggests that the conformation changes of two key antioxidant enzymes, catalase and superoxide dismutase, and the dissolution of AgNPs depended on the protein structure and could result in different degrees of enzymatic activity modulation. This research provides a basis to understand how the functional properties of the key antioxidant enzymes may affect the stability of nanoparticles in a biological context and give insights into the role of these enzymes in the mechanism of NP-induced redox stress in vivo.

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Study on the interaction between salicylic acid and catalase by spectroscopic methods

Cited by 18 publications

References 21 publications

Probing the Interaction of Mutiwalled Carbon Nanotubes and Catalase: Mutispectroscopic Approach

Probing the Interaction of Mutiwalled Carbon Nanotubes and Catalase: Mutispectroscopic Approach

Separation and Identification of Anthocyanin Extracted from Mulberry Fruit and the Pigment Binding Properties toward Human Serum Albumin

Interaction of silver nanoparticles with antioxidant enzymes

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