Spectroscopic Investigations on the Interaction between Carbon Nanotubes and Catalase on Molecular Level

Guan, Jin; Dai, Jingping; Zhao, Xingchen; Liu, Chunhua; Gao, Canzhu; Liu, Rutao

doi:10.1002/jbt.21555

Cited by 14 publications

(6 citation statements)

References 35 publications

(47 reference statements)

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“…It has been reported that interaction of SWCNT with horseradish peroxidase and chicken egg white lysozyme doesn’t change on the protein structure 27 . The interaction of MWCNT with catalase revealed that the activity of protein was inhibited, and secondary and tertiary structures of protein were changed 28 . Also interaction of CNT with different proteins such as hydrolase and albumin had been investigated and relation of nanoparticle surface curvature and protein conformational changes had been studied 29 30 31 .…”

mentioning

confidence: 99%

Interaction of single and multi wall carbon nanotubes with the biological systems: tau protein and PC12 cells as targets

Zeinabad

Zarrabian

Saboury

et al. 2016

Sci Rep

124

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Subtle changes in the structure of nanoparticles influence their surface tension and corresponding interaction with cells and proteins. Here, the interaction of the single wall carbon nanotube (SWCNT) and multiwall carbon nanotube (MWCNT) with different surface tension with tau protein was evaluated using a variety of techniques including far and near circular dichroism, fluorescence spectroscopy, dynamic light scattering, Zeta potential, and TEM evaluation. Also the cytotoxicity of SWCNT and MWCNT on the PC12 cell line as a model of nervous system cell line was investigated by the MTT, LDH, acridine orange/ethidium bromide staining, flow cytometry, caspase 3 activity, cell and membrane potential assays. It was observed that SWCNT induced more structural changes of tau protein relative to MWCNT/tau protein interaction. It was also revealed that SWCNT and MWCNT impaired the viability and complexity of PC12 cells in different modes of cytotoxicity. Analysis of cellular outcomes indicated that MWCNT in comparison with SWCNT resulted in induction of necrotic modes of cell death, whereas apoptotic modes of cell death were activated in SWCNT-incubated cells. Together these findings suggest that surface tension may be used to determine how nanoparticle structure affects neurotoxicity and protein conformational changes.

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mentioning

confidence: 99%

Interaction of single and multi wall carbon nanotubes with the biological systems: tau protein and PC12 cells as targets

Zeinabad

Zarrabian

Saboury

et al. 2016

Sci Rep

124

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“…The strong absorption peak of pepsin decreased significantly and did not shift and the weak absorption peak showed a slight blue shift on addition of Dai or Gen. These results suggest that the microenvironment hydrophobicity of the amino acid residue increased , and a strong binding interaction between pepsin and Dai or Gen existed, which changed the conformation of pepsin.…”

Section: Resultsmentioning

confidence: 82%

Spectroscopy and molecular docking study on the interaction of daidzein and genistein with pepsin

Nan

Wang²,

Sun

et al. 2016

Luminescence

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The interaction of pepsin with daidzein (Dai) or genistein (Gen) was investigated using spectroscopic techniques under simulated physiological conditions. Dai and Gen can quench the fluorescence of pepsin and the quenching mechanism was a static process. The binding site number n and apparent binding constant K were measured at different temperatures. The thermodynamic parameters ΔΗ, ΔG and ΔS were calculated. The results indicated that van der Waals forces and hydrogen bond formation played major roles in the interaction of Dai or Gen with pepsin. The binding distance between pepsin and Dai or Gen was calculated according to energy transfer theory. The results of synchronous fluorescence spectra showed that the microenvironment and conformation of pepsin were changed. UV absorption and 3D fluorescence spectra showed that the binding interaction disturbed the microenvironment of amino acid residues and induced conformational changes in pepsin. Molecular docking results showed that Dai and Gen entered into the hydrophobic cavity of pepsin and two hydrogen bonds formed between Dai or Gen and pepsin. The results demonstrated that the interaction behavior between Dai and Gen with pepsin was slightly different, which denoted that the 5-hydroxyl group of Gen, to a certain extent, had an effect on ligand binding to proteins. Copyright © 2016 John Wiley & Sons, Ltd.

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“…In order to investigate the effect of the inner‐filter exists in the protein–ligand system, we carried out relevant experiment primarily. Inner‐filter effect has been observed and studied for a long time . Recorded fluorescence intensity is in general not proportional to the sample concentration owing to the absorption of the incident and emitted light passing through the sample to and from the point inside the cell where the emission is detected.…”

Section: Resultsmentioning

confidence: 99%

New Insights into the Toxicity ofn-Butanol to Trypsin: Spectroscopic and Molecular Docking Descriptions

Zhang

Sun

Song

et al. 2015

J Biochem Mol Toxicol

Self Cite

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n-Butanol has been widely used and its residue exists extensively in the environment. It could lead to conformational and functional changes of trypsin by forming a complex with it. Docking method and spectrographic technique were employed to the study of the complex of trypsin and n-butanol. The fluorescence results indicated that n-butanol can form a complex with trypsin and change the distance between tryptophan and fluorescence quenchers. The conformational changes of trypsin were proved by UV-visible absorption and synchronous fluorescence spectroscopy indicating that n-butanol had little effect on the conformation of trypsin at a low concentration while denatured and coagulated the trypsin at a high concentration. The binding site was displayed by molecular modeling, which gave information about distances and binding forces between n-butanol and trypsin. The results were in accordance with spectroscopic experiments. Besides, enzyme activity assay gave the dose-response relationship of n-butanol with trypsin.

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Spectroscopic Investigations on the Interaction between Carbon Nanotubes and Catalase on Molecular Level

Cited by 14 publications

References 35 publications

Interaction of single and multi wall carbon nanotubes with the biological systems: tau protein and PC12 cells as targets

Interaction of single and multi wall carbon nanotubes with the biological systems: tau protein and PC12 cells as targets

Spectroscopy and molecular docking study on the interaction of daidzein and genistein with pepsin

New Insights into the Toxicity ofn-Butanol to Trypsin: Spectroscopic and Molecular Docking Descriptions

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