Investigation of the interaction of aurantio‐obtusin with human serum albumin by spectroscopic and molecular docking methods

Liu, Jianming; Yan, Xuyang; Yue, Yuanyuan; Zhao, Shufang

doi:10.1002/bio.3378

Cited by 37 publications

(10 citation statements)

References 62 publications

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“…Figure shows HSA CD spectra in the absence and presence of CA (curves b and c). It can be seen that two negative bands of HSA were at 208 and 222 nm, which are attributed to π‐π*and n → π* electron transfer for the peptide bond of α‐helix . The addition of CA caused the obvious increase of two negative bands without any significant peak position shift since binding was performed.…”

Section: Resultsmentioning

confidence: 99%

“…According to equations and , the calculated results exhibited a reduction of α‐helix structures from 51.67% to 42.17% for HSA at the molar ratio HSA/CA of 1:1. The earlier results indicate that CA bound with amino acid residues of HSA and altered its conformation …”

Section: Resultsmentioning

confidence: 99%

“…It can be seen that two negative bands of HSA were at 208 and 222 nm, which are attributed to π-π*and n → π* electron transfer for the peptide bond of α-helix. [42,43] The addition of CA caused the obvious increase of two negative bands without any significant peak position shift since binding was performed. According to equations 1 and 2, the calculated results exhibited a reduction of αhelix structures from 51.67% to 42.17% for HSA at the molar ratio HSA/CA of 1:1.…”

Section: Synchronous Fluorescence Spectramentioning

confidence: 99%

“…The earlier results indicate that CA bound with amino acid residues of HSA and altered its conformation. [43] 3.6 | Molecular docking…”

Section: Synchronous Fluorescence Spectramentioning

confidence: 99%

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Exploration of interaction of canthaxanthin with human serum albumin by spectroscopic and molecular simulation methods

et al. 2017

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The interaction between the food colorant canthaxanthin (CA) and human serum albumin (HSA) in aqueous solution was explored by using fluorescence spectroscopy, three-dimensional fluorescence spectra, synchronous fluorescence spectra, UV-vis absorbance spectroscopy, circular dichroism (CD) spectra and molecular docking methods. The thermodynamic parameters calculated from fluorescence spectra data showed that CA could result in the HSA fluorescence quenching. From the K change with the temperature dependence, it was concluded that HSA fluorescence quenching triggered by CA is the static quenching and the number of binding sites is one. Furthermore, the secondary structure of HSA was changed with the addition of CA based on the results of synchronous fluorescence, three-dimensional fluorescence and CD spectra. Hydrogen bonds and van der Waals forces played key roles in the binding process of CA with HSA, which can be obtained from negative standard enthalpy (ΔH) and negative standard entropy (ΔS). Furthermore, the conclusions were certified by molecular docking studies and the binding mode was further analyzed with Discovery Studio. These conclusions can highlight the potential of the interaction mechanism of food additives and HSA.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Synchronous Fluorescence Spectramentioning

confidence: 99%

“…The earlier results indicate that CA bound with amino acid residues of HSA and altered its conformation. [43] 3.6 | Molecular docking…”

Section: Synchronous Fluorescence Spectramentioning

confidence: 99%

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Exploration of interaction of canthaxanthin with human serum albumin by spectroscopic and molecular simulation methods

et al. 2017

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“…At present, extensive studies using fluorescence spectroscopy on interactions between different types of proteins and pharmaceutical molecules have been reported, these included the study of FQS with human serum albumin using luminescence spectroscopy . Similar studies on the interaction between FQS and pepsin have been very infrequent.…”

Section: Introductionmentioning

confidence: 99%

Investigation of binding between fluoroquinolones and pepsin by fluorescence spectroscopy and molecular simulation

et al. 2019

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In this paper, the interactions of pepsin with fluoroquinolones, including norfloxacin (NFX) or ofloxacin (OFX), were investigated using fluorescence spectroscopy. The effects of NFX or OFX on pepsin showed that the molecular conformation of pepsin and the microenvironment of tryptophan residues were changed under mimicked physiological conditions. Static quenching was suggested as a factor. Quenching constants and binding constants were determined and thermodynamic parameters were calculated at three temperatures (25°C, 31°C and 37°C). Molecular interaction distances (binding distance r) were obtained. Binding was enthalpy driven and the process was spontaneous. Synchronous fluorescence, three-dimensional fluorescence spectroscopy and molecular simulation were used for analysis. Interactions were further tested using molecular modelling. Quenching and binding constants of NFX with pepsin were the highest when testing NFX/OFX/fleroxacin/gatifloxacin with pepsin combinations. NFX was the strongest quencher, and affinity of NFX for pepsin was higher than that of OFX/fleroxacin/gatifloxacin.

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Interactions of diclazuril enantiomers with serum albumins: Multi‐spectroscopic and molecular docking approaches

Chen

Guo

et al. 2022

J of Molecular Recognition

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In this work, multi‐spectroscopic and molecular docking methods have been conducted in the investigation of enantioselective interactions between diclazuril enantiomers and human/bovine serum albumins (HSA/BSA). The binding constants between serum albumins (SAs) and diclazuril enantiomers revealed that SAs exhibited stronger binding affinity for (R)‐diclazuril than (S)‐enantiomer. In addition, the fluorescence quenching of SAs induced by diclazuril enantiomers was ascribed to static quenching mechanism, in which hydrogen bonds and Van der Waals forces were the main interactions. According to the thermodynamic study, binding of diclazuril enantiomers and SAs was an exothermic process driven by enthalpy change. Then, circular dichroism spectroscopy of SAs with diclazuril enantiomers revealed that the SAs conformation had changed in the presence of diclazuril. Moreover, molecular docking technology was applied in exploration of interactions between SAs and diclazuril enantiomers. The docking energy between SAs and (R)‐diclazuril was larger than (S)‐diclazuril, which indicated that the affinity of SAs with (R)‐diclazuril was stronger than (S)‐enantiomer. This work may provide valuable information for explaining differences in pharmacokinetics and residue elimination of diclazuril enantiomers in living organisms.

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Investigation of the interaction of aurantio‐obtusin with human serum albumin by spectroscopic and molecular docking methods

Cited by 37 publications

References 62 publications

Exploration of interaction of canthaxanthin with human serum albumin by spectroscopic and molecular simulation methods

Exploration of interaction of canthaxanthin with human serum albumin by spectroscopic and molecular simulation methods

Investigation of binding between fluoroquinolones and pepsin by fluorescence spectroscopy and molecular simulation

Interactions of diclazuril enantiomers with serum albumins: Multi‐spectroscopic and molecular docking approaches

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