Different spectroscopic and molecular modeling studies on the interaction between cyanidin‐3‐O‐glucoside and bovine serum albumin

Anthocyanin is one of the flavonoid phytopigments with specific health benefits. The interaction between delphinidin-3-O-glucoside (D3G) and bovine serum albumin (BSA) was investigated by fluorescence spectroscopy, synchronous fluorescence spectroscopy, three-dimensional fluorescence spectroscopy, ultraviolet-visible absorption spectroscopy, circular dichroism spectroscopy and molecular modeling. D3G effectively quenched the intrinsic fluorescence of BSA via static quenching. The number of binding sites and binding constant Ka were determined, and the hydrogen bonds and van der Waals forces played major roles in stabilizing the D3G-BSA complex. The distance r between donor and acceptor was obtained as 2.81 nm according to Förster's theory. In addition, the effects of pH and metal ions on the binding constants were discussed. The results studied by synchronous fluorescence, three-dimensional fluorescence and circular dichroism experiments indicated that the secondary structures of the protein has been changed by the addition of D3G and the α-helix content of BSA decreased (from 56.1% to 52.4%). Furthermore, the study of site marker competitive experiments and molecular modeling indicated that D3G could bind to site I of BSA, which was in the large hydrophobic cavity of subdomain IIA.

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“…Tang et al . and Cahyana et al . also found that anthocyanins could quench the fluorescence intensity of BSA.…”

Section: Resultsmentioning

confidence: 88%

“… studied the interaction of delphinidin and HSA with multi‐spectral and Tang et al . researched the combination of cyanidin‐3‐ O ‐glucoside and BSA with different spectroscopic and molecular modeling techniques. Cahyana et al .…”

Section: Introductionmentioning

confidence: 99%

Combined multispectroscopic and molecular docking investigation on the interaction between delphinidin‐3‐O‐glucoside and bovine serum albumin

Zuo

Tang

et al. 2014

Luminescence

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“…The docking results demonstrate that the binding of C3G to bovine serum albumin was predominantly due to hydrogen bond interactions and hydrophobic and electrostatic forces. The secondary structure of the protein changed in the presence of C3G (Tang and others ).…”

Section: Food Compounds and Their Capacity To Stabilize Natural Pigmentsmentioning

confidence: 99%

“…BSA, bovine serum albumin; C3G, cyanidin‐3‐O‐glucoside.The binding of C3G to BSA is predominantly due to hydrogen bond interaction, and hydrophobic electrostatic forces. The secondary structure of protein changed in the presence of C3G (Tang and others ). Reproduced with permission granted by John Wiley and Sons, August 1, 2016.…”

Section: Food Compounds and Their Capacity To Stabilize Natural Pigmentsmentioning

confidence: 99%

Natural Pigments: Stabilization Methods of Anthocyanins for Food Applications

Cortez

Luna‐Vital

Margulis

et al. 2016

Comp Rev Food Sci Food Safe

404

214

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The production of natural food pigments continues to grow worldwide. The global market is expected to grow at a compound annual growth rate of 6.22%, by revenue, over the period 2015 to 2019. Pigments such as anthocyanins, carotenoids, betalains, and chlorophylls have been used to color foods. However, there are challenges related to color losses during food processing, storage, and commercialization due to a low stability of natural pigments compared to synthetic colorants. This review summarizes the most recent studies and patents aimed at enhancing anthocyanin stability in food systems. The stabilizing methods include additions of copigment compounds, such as polymers, phenolic compounds, and metals. In addition, the exclusion of O 2 during processing and storage, hard-panned candy coating methods for blue, green, and brown colors, and various encapsulation techniques were considered. Combining strategies and evaluating new materials capable of stabilizing anthocyanins will enhance their potential for use as value-added natural food pigments.

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“…To date, a lot of research has focused on interactions between anthocyanins and serum albumin . However, the interaction between P3G and BSA has not been discussed.…”

Section: Introductionmentioning

confidence: 99%

Study on the interaction between pelargonidin‐3‐O‐glucoside and bovine serum albumin using spectroscopic, transmission electron microscopy and molecular modeling techniques

Tang

2015

Luminescence

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The aim of this study is to evaluate the binding behavior between pelargonidin-3-O-glucoside (P3G) and bovine serum albumin (BSA) using multi-spectroscopic, transmission electron microscopy (TEM) and molecular docking methods under physiological conditions. Fluorescence spectroscopy and time-resolved fluorescence showed that the fluorescence of BSA could be quenched remarkably by P3G via a static quenching mechanism, and there is a single class of binding site on BSA. In addition, the thermodynamic functions ΔH and ΔS were -21.69 kJ/mol and 24.46 J/mol/K, indicating that an electrostatic interaction was a main acting force. The distance between BSA and P3G was 2.74 nm according to Förster's theory, illustrating that energy transfer occurred. In addition, the secondary structure of BSA changed with a decrease in the α-helix content from 66.2% to 64.0% as seen using synchronous fluorescence, UV/vis, circular dichroism and Fourier transform infrared spectroscopies, whereas TEM images showed that P3G led to BSA aggregation and fibrillation. Furthermore, site marker competitive experiments and molecular docking indicated that P3G could bind with subdomain IIA of BSA. The calculated results of the equilibrium fraction showed that the concentration of free P3G in plasma was high enough to be stored and transported from the circulatory system to its target sites to provide therapeutic effects.

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Different spectroscopic and molecular modeling studies on the interaction between cyanidin‐3‐O‐glucoside and bovine serum albumin

Cited by 20 publications

References 31 publications

Combined multispectroscopic and molecular docking investigation on the interaction between delphinidin‐3‐O‐glucoside and bovine serum albumin

Combined multispectroscopic and molecular docking investigation on the interaction between delphinidin‐3‐O‐glucoside and bovine serum albumin

Natural Pigments: Stabilization Methods of Anthocyanins for Food Applications

Study on the interaction between pelargonidin‐3‐O‐glucoside and bovine serum albumin using spectroscopic, transmission electron microscopy and molecular modeling techniques

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