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

Xu, Ming; Sheng, Zhonghua; Lü, Wenyu; Dai, Tianchun; Hou, Cailing

doi:10.1002/jbt.21454

Cited by 9 publications

(6 citation statements)

References 26 publications

(26 reference statements)

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“…Thus, there was a remarkable decrease of peak intensity at this range when vancomycin interacted with HSA. This phenomenon confirmed that the tertiary or secondary structure of HSA was altered by the drug and the hydrogen bonding was partially destroyed .…”

Section: Resultssupporting

confidence: 63%

Underlying the Mechanism of Vancomycin and Human Serum Albumin Interaction: A Biophysical Study

Wei

Wang

et al. 2013

J Biochem & Molecular Tox

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In the present study, the binding mechanism of vancomycin with human serum albumin (HSA) was determined. Upon addition of vancomycin to HSA, the fluorescence emission was quenched and the binding constant of vancomycin with HSA was found to be 6.05 × 10(3) M(-1) at 295 K, which corresponds to -2.16 × 10(4) J·mol(-1) of free energy. The conformation of HSA was altered upon binding of vancomycin with a decrease in α helix and an increase in β sheets and random coils, suggesting partial unfolding of the secondary structure. Molecular docking experiments found that vancomycin binds strongly with HSA at the hydrophobic pocket through hydrogen bonding and van der Waals interactions. An average binding distance of 4.71 nm has been determined on the basis of the Förster resonance energy theory. It was demonstrated that vancomycin binding to HSA causes protein structural changes.

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Section: Resultssupporting

confidence: 63%

Underlying the Mechanism of Vancomycin and Human Serum Albumin Interaction: A Biophysical Study

Wei

Wang

et al. 2013

J Biochem & Molecular Tox

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“…Thrombin had two absorption peaks at 215 nm and 275 nm. When the P9 solution was added to the thrombin solution, the peak at 215 nm was slightly blue-shifted (2 nm) and decreased in intensity, probably due to the interaction of P9 with thrombin, which resulted in the disorganization of the surroundings of amide bonds and the contraction of the C = O bonds in thrombin (Chen et al 2019;Xu et al 2012). The slight decrease of the absorption peak at 275 nm may be due to the binding of P9 to thrombin, which altered the structure of thrombin and resulted in the masking of the hydrophobic moiety of aromatic amino acids in thrombin, thus leading to the weakening of the absorption peak(Chen et al…”

Section: Interaction Assay Between Thrombin and Peptidementioning

confidence: 99%

Purification and Characterization of a Novel Anticoagulant Peptide from Protein Hydrolysate of Eupolyphaga sinensis Walker

Li,

Zhuang,

et al. 2024

Int J Pept Res Ther

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Eupolyphaga sinensis Walker (ESW), an animal drug in traditional Chinese medicine, has been used clinically for thousands of years for cardiovascular disease and osteoarthritis. Many studies of ESW have reported that it had have anti-in ammatory and anti-tumor activities due to the small-molecule ingredients. However, large-molecule compounds of ESW representing signi cant pharmacological effects such as anti-thrombotic, anti-cancer, and anti-in ammatory have not been revealed yet. Here, a novel anticoagulant peptide (P9) containing 9 amino acids was isolated from the hydrolysate of aqueous extracts of ESW. Further, P9 synthesized by solid-phase synthesis was able to prolong APTT and TT and bind to thrombin in a mixed mode. Molecular docking and spectroscopy demonstrated that P9 was able to inhibit thrombin activity by binding to the active site of thrombin and altering the secondary structure of thrombin. In an in vivo study, P9 was able to reduce the intensity of Phenylhydrazine (PHZ)-induced cardiac staining in thrombosed zebra sh with antithrombotic activity. The results suggest that peptides originated from ESW hydrolysates could exert an anticoagulant effect, which is likely to be a potential source of bioactive peptides with anticoagulant activity.

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“…Studies have shown that fluorescence of CAT is mainly generated from the emission of tryptophan (Trp), tyrosine (Tyr), and phenylala-nine (Phe) residues. [23,24] When binding with proteins, small molecules like Sudan dyes can change the microenvironment of aromatic amino acid residues and thus lead to the changes in the intrinsic fluorescence intensity of CAT. [8] Fluorescence enhancement and quenching means the enhancement or reduction of fluorescence intensity, respectively, which can be caused by Sudan dyes.…”

Section: Fluorescence and Synchronous Fluorescence Spectroscopymentioning

confidence: 99%

Comparison of the toxicity of the dyes Sudan II and Sudan IV to catalase

Hao

Pan

et al. 2017

J Biochem & Molecular Tox

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The mechanisms of the toxicity of Sudan dyes to the key antioxidant enzyme catalase (CAT) were investigated by spectroscopic methods, calorimetry techniques, enzyme activity assay, and molecular docking. Results showed that Sudan dyes bound to CAT through hydrophobic force, which changed the microenvironment of tryptophan and tyrosine residues, leading to a conformational alteration and shrinkage of the protein. Enzyme activity assay and molecular docking revealed that the activity of CAT was slightly inhibited in the presence of Sudan dyes. In comparison, the binding of Sudan II with CAT was slightly stronger than Sudan IV. Also, Sudan II and Sudan IV showed a different impact on the microenvironment of aromatic amino acid residues. But the dyes had very similar effects on conformation and activity of the protein. This work provides an essential reference for the evaluation of Sudan dyes' effects on body's antioxidant defense system and safe use of Sudan dyes.

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

Cited by 9 publications

References 26 publications

Underlying the Mechanism of Vancomycin and Human Serum Albumin Interaction: A Biophysical Study

Underlying the Mechanism of Vancomycin and Human Serum Albumin Interaction: A Biophysical Study

Purification and Characterization of a Novel Anticoagulant Peptide from Protein Hydrolysate of Eupolyphaga sinensis Walker

Comparison of the toxicity of the dyes Sudan II and Sudan IV to catalase

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