Study of the Interaction of Aglycon of Daunorubicin with Human Serum Albumin by Spectroscopy and Modeling

Cui, Fengling; Qin, Lixia; Zhang, Guisheng; Yao, Xiaojun; Lei, Beilei

doi:10.1002/mabi.200800105

Cited by 5 publications

(3 citation statements)

References 40 publications

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“…Static quenching involves the combination of a quencher and a protein, while dynamic quenching involves diffusion and collision . The difference is that the biomolecular quenching constant of the former decreases with an increase in temperature, whereas that of the latter increases . The biomolecular quenching constant can be calculated by the Stern–Volmer equation: F 0 / F = 1 + K q τ 0 [ Q ] = 1 + K sv [ Q ] where F 0 represents the endogenous fluorescence intensity of the protein, F represents the fluorescence intensity of the protein in the presence of the quencher, K q is the bimolecular quenching constant, τ 0 is the fluorescence lifetime of the protein (generally considered to be 10 –8 s), [Q] is the concentration of the quencher, and K sv is the Stern–Volmer quenching constant.…”

Section: Resultsmentioning

confidence: 99%

Interaction between a Commercial Mannoprotein and Cyanidin-3-O-glucoside-4-vinylphenol and Its Stability and Antioxidative Properties as a Novel Functional Pigment

Liu,

Li,

Zeng

et al. 2023

J. Agric. Food Chem.

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Hydroxyphenyl-pyranoanthocyanins, which are derived from anthocyanins and phenolic acids during the fermentation and aging of red wine, are prone to polymerization and precipitation, which largely limits their application and bioactivity research. In the present study, cyanidin-3-O-glucoside-4-vinylphenol (C3GVP), a hydroxyphenyl-pyranoanthocaynin, was prepared from C3G and p-coumaric acid, and mannoprotein (MP) was employed to improve its stability in various complex solvents by forming a stable anthocyanin–MP complex. We used scanning electron microscopy, ultraviolet–visible spectroscopy, Fourier-transform infrared spectroscopy, and circular dichroism spectroscopy to observe structural changes in C3GVP and MP. The results demonstrated that the intermolecular polymerization of C3GVP was mitigated and the secondary conformation of MP was changed slightly. Fluorescence spectroscopy and molecular docking indicated that C3GVP and MP interacted via hydrogen bonds and hydrophobic interactions. Importantly, the C3GVP–MP complex exhibited better thermal stability and antioxidant capacity than C3G.

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Section: Resultsmentioning

confidence: 99%

Interaction between a Commercial Mannoprotein and Cyanidin-3-O-glucoside-4-vinylphenol and Its Stability and Antioxidative Properties as a Novel Functional Pigment

Liu,

Li,

Zeng

et al. 2023

J. Agric. Food Chem.

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“…A comparison of this method with the BCG assay is listed in Table-2. The results of three serum samples are given in Table-2. Studies on binding constant of 3H-indole with human serum albumin: In order to study the binding constant in the system of 3H-indole and human serum albumin, the fluorescence quenching method was used [10][11][12][13][14][15] .…”

Section: Tolerance Of Foreign Substancesmentioning

confidence: 99%

Fluorometric Method for Microdetermination of Human Serum Albumin Using Substituted 3H-Indole Compound

Xu¹,

Qu²,

Han³

et al. 2014

Asian J. Chem.

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A simple, sensitive and reproducible fluorometric method for determining nanoamount of protein is developed. The method is based on the reaction between protein and 3H-indole compounds in aqueous solution. Under the optimized experimental conditions, there is little interference with amino acids and most metal ions. In the detection of total amount of proteins in human serum albumin, the values obtained by this method are close to those of the BCG method. The binding reaction mechanism between this compound and human serum albumin in aqueous solution was studied using fluorescence. Their binding constant is Ka = 8.51 × 10 5 L mol-1 and the binding site number is n = 1.2. It is confirmed that the combination is a single static queching process. According to the resonance energy transfer theory, the distance between the molecule and tryptophan of human serum albumin is 37.3 Å and the förster energy transfer is very efficient as high as 93.7 %.

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“…From the values of binding constant at three different temperatures (298 K, 301 K, and 311 K), the thermodynamic parameters, enthalpy change ( H Δ ○ ), are calculated by the Van't Hoff equation [19] : [20] . The results coincide with the molecular docking study.…”

Section: Binding Character Of Hsa and Acetylgliotoxinmentioning

confidence: 99%

Molecular docking and spectroscopic methods to probe the interaction of acetylgliotoxin and HSA

Zhang

Chen

Song

et al. 2010

Wuhan Univ. J. Nat. Sci.

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The interaction between acetylgliotoxin and human serum albumin (HSA) has been studied by spectroscopic method. Acetylgliotoxin quenches the intrinsic fluorescence of HSA in a static quenching procedure. The binding of acetylgliotoxin to HSA causes a slight conformational change of HSA. The binding constants at different temperatures as well as enthalpy change and entropy change, are calculated according to relevant fluorescent data and Van't Hoff equation. The hydrogen bond is a predominant intermolecular force for stabilizing the complex, which is in conformity with the results of molecular modeling study.

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Study of the Interaction of Aglycon of Daunorubicin with Human Serum Albumin by Spectroscopy and Modeling

Cited by 5 publications

References 40 publications

Interaction between a Commercial Mannoprotein and Cyanidin-3-O-glucoside-4-vinylphenol and Its Stability and Antioxidative Properties as a Novel Functional Pigment

Interaction between a Commercial Mannoprotein and Cyanidin-3-O-glucoside-4-vinylphenol and Its Stability and Antioxidative Properties as a Novel Functional Pigment

Fluorometric Method for Microdetermination of Human Serum Albumin Using Substituted 3H-Indole Compound

Molecular docking and spectroscopic methods to probe the interaction of acetylgliotoxin and HSA

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