2021
DOI: 10.1016/j.foodchem.2021.129771
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Exploring the mode of binding between butylated hydroxyanisole with bovine serum albumin: Multispectroscopic and molecular docking study

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Cited by 18 publications
(3 citation statements)
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“…Similar results were also reported showing that the fluorescence intensity of bovine serum albumin decreased with the addition of butylated hydroxyanisole, and a slight blue shift of 3 nm emerged which indicates that the microenvironment of bovine serum albumin had been changed by butylated hydroxyanisole [15]. The relative fluorescence quenching rates were 76.69 % and 85.04 % when BCL and JSD were added at the highest concentration to LOX respectively, which demonstrates that JSD quenched the intrinsic fluorescence of LOX more easily than BCL.…”
Section: Effect Of Bcl and Jsd On Fluorescence Emission Spectra Of Loxsupporting
confidence: 87%
“…Similar results were also reported showing that the fluorescence intensity of bovine serum albumin decreased with the addition of butylated hydroxyanisole, and a slight blue shift of 3 nm emerged which indicates that the microenvironment of bovine serum albumin had been changed by butylated hydroxyanisole [15]. The relative fluorescence quenching rates were 76.69 % and 85.04 % when BCL and JSD were added at the highest concentration to LOX respectively, which demonstrates that JSD quenched the intrinsic fluorescence of LOX more easily than BCL.…”
Section: Effect Of Bcl and Jsd On Fluorescence Emission Spectra Of Loxsupporting
confidence: 87%
“…The values of K a were approximately equal to 10 4 M −1 , which suggested moderate binding interactions between HSA and astilbin, since the binding affinity of chemicals with transport proteins could affect their biological activity. Generally, drugs with strong protein binding have long half-life, long duration time and slow work and elimination in plasma [ 32 ]. The values of n were close to 1, which suggested the presence of one binding site in HSA for astilbin.…”
Section: Resultsmentioning
confidence: 99%
“…Effect of CLE on the fluorescence spectra of BSA Steady-state and synchronous fluorescence spectroscopies have been used to explore the conformational changes of proteins interacting with small molecules (Cheng et al, 2022). BSA has a fluorescence emission peak at approximately 348 nm (Gu et al, 2021). In the presence of glucose, the fluorescence intensity of BSA decreased (Figure 2A) due to the changes in the microenvironment of tryptophan and tyrosine residues in BSA (Qin et al, 2021;Rahman & Khalil, 2022).…”
Section: 7mentioning
confidence: 99%