A spectroscopic study of the interaction of the antioxidant naringin with bovine serum albumin

Roy, Atanu Singha; Tripathy, Debi Ranjan; Chatterjee, Angshuman; Dasgupta, Swagata

doi:10.4236/jbpc.2010.13017

Cited by 78 publications

(45 citation statements)

References 53 publications

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“…Glycosylation is attributed to the decrease in the hydrophobicity resulting in lower binding affinity. Naringin also binds with BSA under physiological conditions to the hydrophobic site I (subdomain IIA) of BSA (Singha Roy et al, 2010). The binding constants in order of 10 4 are similar to naringin HSA complex.…”

Section: Flavanone-sa Interactionmentioning

confidence: 95%

“…Fourier transform infrared (FT-IR) spectroscopy has long been used as a powerful method for investigating the secondary structures of proteins and their dynamics Singha Roy, Tripathy, Chatterjee, & Dasgupta, 2010;. Hydrogen bonding and the coupling between transition dipoles are the key factors that have a crucial role in governing the conformational sensitivity of the amide bands in the protein.…”

Section: Fourier Transform Infrared Spectroscopymentioning

confidence: 99%

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A review on structure–affinity relationship of dietary flavonoids with serum albumins

Pal

Saha

2013

Journal of Biomolecular Structure and Dynamics

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Flavonoids are a class of plant secondary metabolites and among thousands of flavonoids few are considered as dietary flavonoids. Serum albumin (SA), the most abundant protein in plasma, functions as the most important carrier of vital drugs, including dietary flavonoids. The binding affinity of dietary flavonoids to SA is demonstrated to be governed by structure-affinity relationship (SAR) and its bioavailability. The present review summarizes the interactions of flavonoids categorized as flavanol, flavonol, flavone, isoflavone, flavanones, and anthocyanidins with SAs (bovine serum albumin and human serum albumin) in light of SAR. The key findings are: (1) the position and degree of hydroxylation highly influence the affinity of flavonoids to SAs, (2) glycosylation decreases and substitution of methoxy group increases the affinity of flavonoids for SAs, (3) catechin gallates have higher binding affinity to SAs than catechins and gallocatechins, (4) inorganic metal ions modulate the binding affinity of flavonoids to SAs, and (5) hydrophobic interaction plays a major role in the interactions of all flavonoids with SAs.

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Section: Flavanone-sa Interactionmentioning

confidence: 95%

Section: Fourier Transform Infrared Spectroscopymentioning

confidence: 99%

A review on structure–affinity relationship of dietary flavonoids with serum albumins

Pal

Saha

2013

Journal of Biomolecular Structure and Dynamics

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“…Naringin affinity for proteins, enzymes, DNA, RNA or particular cell types, as well as its ability to penetrate the cell membrane determines its biological effects [6]. In vitro experiments have been carried out to verify naringin binding to human serum albumin (HSA) and bovine serum albumin (BSA), as well as transport by these proteins, which is pivotal in the design of new naringin-inspired drugs [7]–[8]. However, the practical application of naringin has been limited by its poor solubility and stability in lipidic environments.…”

Section: Introductionmentioning

confidence: 99%

Investigation of the Interaction of Naringin Palmitate with Bovine Serum Albumin: Spectroscopic Analysis and Molecular Docking

Zhang

et al. 2013

PLoS ONE

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BackgroundBovine serum albumin (BSA) contains high affinity binding sites for several endogenous and exogenous compounds and has been used to replace human serum albumin (HSA), as these two compounds share a similar structure. Naringin palmitate is a modified product of naringin that is produced by an acylation reaction with palmitic acid, which is considered to be an effective substance for enhancing naringin lipophilicity. In this study, the interaction of naringin palmitate with BSA was characterised by spectroscopic and molecular docking techniques.Methodology/Principal FindingsThe goal of this study was to investigate the interactions between naringin palmitate and BSA under physiological conditions, and differences in naringin and naringin palmitate affinities for BSA were further compared and analysed. The formation of naringin palmitate-BSA was revealed by fluorescence quenching, and the Stern-Volmer quenching constant (KSV) was found to decrease with increasing temperature, suggesting that a static quenching mechanism was involved. The changes in enthalpy (ΔH) and entropy (ΔS) for the interaction were detected at −4.11±0.18 kJ·mol−1 and −76.59±0.32 J·mol−1·K−1, respectively, which indicated that the naringin palmitate-BSA interaction occurred mainly through van der Waals forces and hydrogen bond formation. The negative free energy change (ΔG) values of naringin palmitate at different temperatures suggested a spontaneous interaction. Circular dichroism studies revealed that the α-helical content of BSA decreased after interacting with naringin palmitate. Displacement studies suggested that naringin palmitate was partially bound to site I (subdomain IIA) of the BSA, which was also substantiated by the molecular docking studies.Conclusions/SignificanceIn conclusion, naringin palmitate was transported by BSA and was easily removed afterwards. As a consequence, an extension of naringin applications for use in food, cosmetic and medicinal preparations may be clinically and practically significant, especially in the design of new naringin palmitate-inspired drugs.

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“…This indicates that the observed CD signal is only produced by BSA. The CD spectrum of BSA exhibits two negative bands in the ultraviolet region at 208 (π→π* transition) and 222 nm (n→π* transition), which is characteristic of the α-helical structure of a protein [20]. It can be seen from Figure 1 that the interaction of [bmim]BF 4 or [bmim]PF 6 with BSA caused a slight decrease in band intensity at all wavelengths of the far UV CD without any significant shift in the peak position.…”

Section: Circular Dichroism Studiesmentioning

confidence: 99%

Interaction of bovine serum albumi with two alkylimidazolium-based ionic liquids investigated by microcalorimetry and circular dichroism

Zhu¹,

Li²,

Zheng³

2011

JBPC

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The interactions of bovine serum albumin (BSA) with two alkylimidazolium-based ionic liquids, 1-butyl-3-methylimidazolium tetrafluoroborate ([bmim]BF 4 ) and 1-butyl-3-methylimidazolium hexafluorophosphate ([bmim]PF 6 ), in buffer solutions at pH 7.0 were investigated by isothermal titration calorimetry (ITC) and circular dichroism (CD). CD spectra showed that the two ionic liquids changed the secondary structure of BSA. Data process was based on the supposition that there were several independent types of binding sites on each BSA molecule for the two ligand molecules. The results obtained by using this supposition combined with Langmuir adsorption model showed that there were two types of such binding sites. One was the high affinity binding site, and the other was the low affinity binding site. The binding constants, changes in enthalpy, entropy and Gibbs free energy for the two types of binding were obtained, which showed that the two types of binding were driven by a favorable entropy increase. Furthermore, for either the ionic liquids, the number of the high affinity binding sites is much smaller than that of the low affinity ones. These results were interpreted with the molecular structure of BSA and the different substituent groups on imidazole ring of the two ionic liquid molecules.

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A spectroscopic study of the interaction of the antioxidant naringin with bovine serum albumin

Cited by 78 publications

References 53 publications

A review on structure–affinity relationship of dietary flavonoids with serum albumins

A review on structure–affinity relationship of dietary flavonoids with serum albumins

Investigation of the Interaction of Naringin Palmitate with Bovine Serum Albumin: Spectroscopic Analysis and Molecular Docking

Interaction of bovine serum albumi with two alkylimidazolium-based ionic liquids investigated by microcalorimetry and circular dichroism

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