The investigation of the interaction between oxybutynin hydrochloride and bovine serum albumin by spectroscopic methods

Guo, Xingjia; Jing, Kui; Guo, Chuang; Jiang, Yuchun; Jiang, Tong; Han, Xiaowei

doi:10.1016/j.jlumin.2010.07.005

Cited by 25 publications

(8 citation statements)

References 22 publications

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“…The values of V and K sv at different temperatures (279, 296, and 310 K) are presented in Table 1. The result confirmed that the quenching mechanism was a static quenching initiated by the formation of the ground state Qy-BSA complex (Guo et al, 2010).…”

Section: Stern-volmer Analysissupporting

confidence: 70%

“…It is clear from this figure that the absorbance peak around 278 nm decreased with the addition of dye, indicating that Qy could bind to BSA to form the Qy-BSA complex. These results implied that the micro-environment around chromophores of BSA was changed upon addition of Qy (Guo et al, 2010;Meirong et al, 2011. The absorption peaks of these solutions showed moderate shifts towards shorter wavelength indicating that with the addition of Qy, the peptide strands of BSA molecules extended more and the hydrophobicity was decreased.…”

Section: Conformation Investigationmentioning

confidence: 92%

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Study on the interaction of food colourant quinoline yellow with bovine serum albumin by spectroscopic techniques

2012

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Section: Stern-volmer Analysissupporting

confidence: 70%

Section: Conformation Investigationmentioning

confidence: 92%

Study on the interaction of food colourant quinoline yellow with bovine serum albumin by spectroscopic techniques

2012

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“…Also the intensity of the two peaks changed with different concentrations of Cu(II)-ATA. As we all known, the dynamic quenching only affects the excited state of fluorophore and does not change the absorption spectrum, whereas the static quenching induces the change of absorption spectrum of fluorophore, so the result again confirmed that the quenching mechanism was a static quenching initiated by the formation of the groundstate Cu(II)-ATA-HSA complex [22,23].…”

Section: Resultssupporting

confidence: 69%

Exploring the copper(II)–aminotriazole complex-binding sites of human serum albumin

Yang

Zhang

et al. 2015

J Biol Inorg Chem

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The potential impact on human exposure to aminotriazole (ATA) and heavy metal in the environment becomes a concerning issue. In the current study, a water-soluble Cu(II)-aminotriazole complex [Cu(II)-ATA] was synthesized. To explore the binding mechanism of the complex with human serum albumin (HSA), their effects on conformation and activity of HSA by multispectroscopic approach and molecular modeling were investigated. Further fluorescent tests revealed that the quenching mechanism of HSA by Cu(II)-ATA was overall static. Meanwhile, the obtained binding constant and thermodynamic parameters on complex-HSA interaction showed that the types of interaction force of Cu(II)-ATA and HSA were hydrogen bonding, van der Waals and electrostatic. The analysis of three-dimensional fluorescence, circular dichroism and Fourier transform infrared spectroscopy showed that Cu(II)-ATA induced the changes in the secondary structure of HSA. Molecular docking simulation was performed and docking model suggested that the complex docked into HSA at subdomain IIA. Furthermore, amino group and attractive electrostatic interaction of Cu(II)-ATA greatly contributed to the hydrogen bonding, van der Waals and electrostatic interaction between Cu(II)-ATA and HSA, as confirmed by experimental data.

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“…And the intensity of the two peaks changed with different concentrations of BPF. As we all known, the dynamic quenching only affected the excited state of fluorophore and did not change the absorption spectrum, but the static quenching induced the change of absorption spectrum of fluorophore, so the result again confirmed that the quenching mechanism was a static quenching initiated by the formation of the ground state BPF-HSA complex [28,29]. …”

Section: Fluorescence Quenching Mechanismsupporting

confidence: 62%

Probing the binding of an endocrine disrupting compound-Bisphenol F to human serum albumin: Insights into the interactions of harmful chemicals with functional biomacromolecules

Pan

Xu²,

Yang

et al. 2014

Spectrochimica Acta Part A: Molecular and Biomolecular Spectros

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The investigation of the interaction between oxybutynin hydrochloride and bovine serum albumin by spectroscopic methods

Cited by 25 publications

References 22 publications

Study on the interaction of food colourant quinoline yellow with bovine serum albumin by spectroscopic techniques

Study on the interaction of food colourant quinoline yellow with bovine serum albumin by spectroscopic techniques

Exploring the copper(II)–aminotriazole complex-binding sites of human serum albumin

Probing the binding of an endocrine disrupting compound-Bisphenol F to human serum albumin: Insights into the interactions of harmful chemicals with functional biomacromolecules

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