Interaction of malachite green with bovine serum albumin: Determination of the binding mechanism and binding site by spectroscopic methods

Zhang, Ye-Zhong; Zhou, Bo; Zhang, Xiaoping; Huang, Ping; Li, Chaohong; Liu, Yi

doi:10.1016/j.jhazmat.2008.07.132

Cited by 295 publications

(103 citation statements)

References 43 publications

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“…3 and the K sv and K q values were presented in Table 1. Generally, the quenching constant decreases with the increasing temperature for static quenching, whereas the contrary effect is measured for dynamic quenching [36]. As shown in Table 1, the Stern-Volmer dynamic quenching constant K sv decreased with the rinsing temperature, indicating that the probable quenching mechanism of fluorescence of HAase by flavonoids is not initiated by dynamic collision but complex formation.…”

Section: Fluorescence Quenchingmentioning

confidence: 89%

Molecular Interactions of Flavonoids to Hyaluronidase: Insights from Spectroscopic and Molecular Modeling Studies

Zeng

Yang

et al. 2015

J Fluoresc

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In the work described on this paper, the interactions between eight flavonoids and hyaluronidase (HAase), an important enzyme involved in a promoting inflammation pathway, were investigated by spectroscopic and molecular modeling methods. The results revealed that all flavonoids could interact with HAase to form flavonoid-HAase complexes. The binding parameters obtained from the data at different temperatures indicated that flavonoids could spontaneously bind with HAase mainly through electrostatic forces and hydrophobic interactions with one binding site. According to synchronous and three-dimensional fluorescence spectra and the molecular docking results, all flavonoids bound directly into the enzyme cavity site and the binding of flavonoid into the enzyme cavity influenced the microenvironment of the HAase activity site which led to the reduced enzyme activity. The present study provides direct evidence at a molecular level to understand the mechanism of inhibitory effect of flavonoid against HAase and explain the anti-inflammatory mechanism of the Traditional Chinese Medicines as anti-inflammatory drugs.

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Section: Fluorescence Quenchingmentioning

confidence: 89%

Molecular Interactions of Flavonoids to Hyaluronidase: Insights from Spectroscopic and Molecular Modeling Studies

Zeng

Yang

et al. 2015

J Fluoresc

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“…The group of albumin proteins has been used for the preparation of nanoparticles, microparticles and encapsulates due to its well-defined primary structure combined with the advantage of enabling surface modifications with dyes, antibodies, antigens, polysaccharides and proteins under stoichiometric conditions which provide stability to the structure (Weber et al 2000a;Lewis et al 2006;Zhang et al 2008Zhang et al , 2009Gebregeorgis et al 2013). Bovine serum albumin (BSA; MW 66,000) and cationised BSA (cBSA) are highly water-soluble containing numerous functional groups suitable for conjugation (Hermanson 2008).…”

Section: The Albumin-group Proteins As Wall Materials For Encapsulationmentioning

confidence: 99%

Food Nano- and Microconjugated Systems: The Case of Albumin–Capsaicin

Sánchez-Segura

García‐Armenta

Perea-Flores

et al. 2015

Food Nanoscience and Nanotechnology

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“…In contrast, the static quenching process depends on the formation of ground-state complexes, and the stability of the ground state complexes decreases with increasing temperature, so the static quenching constant decreases with rising temperature [12].…”

Section: Fluorescence Quenching Studiesmentioning

confidence: 94%

Biophysical studies of the interaction between a triazole derivative and bovine serum albumin by multi-spectroscopic and molecular modeling methods

Wang

et al. 2011

Sci. China Chem.

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The interaction between 3-thiol-4-(2,4-dichlorobenzylideneamino)-5-methyl-4H-1,2,4-triazole (CBTZ) and bovine serum albumin (BSA) under physiological conditions was investigated by fluorescence, UV-vis absorption and circular dichroism (CD) spectroscopy as well as molecular modeling methods. The result of fluorescence experiment indicates the static quenching as a result of the formation of the CBTZ-BSA complex. The binding constants (K a ) at different temperatures were calculated according to the modified Stern-Volmer equation. The enthalpy change (H) and entropy change (S) were determined based on the van′t Hoff equation. Both negative H and S indicated that van der Waals and hydrogen-bonding forces were the dominant intermolecular forces to stabilize the CBTZ-BSA complex. Site marker competitive replacement experiments demonstrated that binding of CBTZ to BSA primarily took place in sub-domain IIA (Sudlow's site I). The binding distance (r = 7.2 nm) between CBTZ and the tryptophan residue of BSA was estimated according to the theory of fluorescence resonance energy transfer (FRET). The conformational studies by circular dichroism (CD) and three-dimensional fluorescence spectroscopy showed that the presence of CBTZ induced minor changes of the secondary structure of BSA. Molecular modeling study further confirmed the binding mode obtained experimentally. triazole, bovine serum albumin, fluorescence quenching, binding site, molecular modeling

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Interaction of malachite green with bovine serum albumin: Determination of the binding mechanism and binding site by spectroscopic methods

Cited by 295 publications

References 43 publications

Molecular Interactions of Flavonoids to Hyaluronidase: Insights from Spectroscopic and Molecular Modeling Studies

Molecular Interactions of Flavonoids to Hyaluronidase: Insights from Spectroscopic and Molecular Modeling Studies

Food Nano- and Microconjugated Systems: The Case of Albumin–Capsaicin

Biophysical studies of the interaction between a triazole derivative and bovine serum albumin by multi-spectroscopic and molecular modeling methods

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