Bioflavonoid (Hesperidin) Restrains Protein Oxidation and Advanced Glycation End Product Formation by Targeting AGEs and Glycolytic Enzymes

Khan, Mohd Shahnawaz; Rehman, Tabish; Ismael, Mohamed; Alajmi, Mohamed F.; Alruwaished, Ghaida I; Alokail, Majed S.

doi:10.1007/s12013-021-00997-8

Cited by 18 publications

(17 citation statements)

References 60 publications

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“…Quenching studies were carried out against the protein in the presence of both the natural compounds, using a spectrofluorometer (Jasco FP-750, JASCO Corporation, Tokyo, Japan). The protein (5 µM α-amylase) was excited at 295 nm, and the emission spectra were recorded at higher wavelengths between 300-400nm [32][33][34][35]. Caffeic acid (0-40 µM) and coumaric acid (0-30 µM) were titrated with the α-amylase at three different temperatures (25, 30 and 35 • C).…”

Section: Steady-state Fluorescencementioning

confidence: 99%

“…Figures 1B and 2B apparently show linear SV plots for caffeic acid-α-amylase and coumaric acid-α-amylase, respectively. Fluorescence quenching can be static or dynamic or a combination of both [34,35]. Temperature dependency of K sv reveals the type of quenching operative for a particular interaction, i.e., protein-ligand complex formation is driven by static or dynamic quenching.…”

Section: Intrinsic Fluorescencementioning

confidence: 99%

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Binding Studies of Caffeic and p-Coumaric Acid with α-Amylase: Multispectroscopic and Computational Approaches Deciphering the Effect on Advanced Glycation End Products (AGEs)

et al. 2022

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Alpha-amylase (α-amylase) is a key player in the management of diabetes and its related complications. This study was intended to have an insight into the binding of caffeic acid and coumaric acid with α-amylase and analyze the effect of these compounds on the formation of advanced glycation end-products (AGEs). Fluorescence quenching studies suggested that both the compounds showed an appreciable binding affinity towards α-amylase. The evaluation of thermodynamic parameters (ΔH and ΔS) suggested that the α-amylase-caffeic/coumaric acid complex formation is driven by van der Waals force and hydrogen bonding, and thus complexation process is seemingly specific. Moreover, glycation and oxidation studies were also performed to explore the multitarget to manage diabetes complications. Caffeic and coumaric acid both inhibited fructosamine content and AGE fluorescence, suggesting their role in the inhibition of early and advanced glycation end-products (AGEs). However, the glycation inhibitory potential of caffeic acid was more in comparison to p-coumaric acid. This high antiglycative potential can be attributed to its additional –OH group and high antioxidant activity. There was a significant recovery of 84.5% in free thiol groups in the presence of caffeic acid, while coumaric attenuated the slow recovery of 29.4% of thiol groups. In vitro studies were further entrenched by in silico studies. Molecular docking studies revealed that caffeic acid formed six hydrogen bonds (Trp 59, Gln 63, Arg 195, Arg 195, Asp 197 and Asp 197) while coumaric acid formed four H-bonds with Trp 59, Gln 63, Arg 195 and Asp 300. Our studies highlighted the role of hydrogen bonding, and the ligands such as caffeic or coumaric acid could be exploited to design antidiabetic drugs.

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Section: Steady-state Fluorescencementioning

confidence: 99%

Section: Intrinsic Fluorescencementioning

confidence: 99%

Binding Studies of Caffeic and p-Coumaric Acid with α-Amylase: Multispectroscopic and Computational Approaches Deciphering the Effect on Advanced Glycation End Products (AGEs)

et al. 2022

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“…The chemical structure of HES is shown in Figure 1 and its IUPAC name is ((S)-2,3-dihydro-5,7-dihydroxy-2-(3-hydroxy-4 methoxy-phenyl)-4H-1-benzopyran-4-one). Similar to most flavonoids, HES is also a natural antioxidant and has anti-inflammatory, anti-atherosclerotic, and anti-diabetic properties [14][15][16][17][18]. Several studies have reported that HES can ameliorates anxiety and depression-like behaviors by enhancing Glo-1 and activating the Nrf2/ARE pathway in the brain of diabetic rats and high glucose cultured SH-SY5Y cells [19].…”

Section: Introductionmentioning

confidence: 99%

Crystal Structure, Solubility, and Pharmacokinetic Study on a Hesperetin Cocrystal with Piperine as Coformer

et al. 2022

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Hesperetin (HES) is a key biological active ingredient in citrus peels, and is one of the natural flavonoids that attract the attention of researchers due to its numerous therapeutic bioactivities that have been identified in vitro. As a bioenhancer, piperine (PIP) can effectively improve the absorption of insoluble drugs in vivo. In the present study, a cocrystal of HES and PIP was successfully obtained through solution crystallization. The single-crystal structure was illustrated and comprehensive characterization of the cocrystal was conducted. The cocrystal was formed by two drug molecules at a molar ratio of 1:1, which contained O–H–O hydrogen bonds between the carbonyl and ether oxygen of PIP and the phenolic hydroxyl group of HES. In addition, a solubility experiment was performed on powder cocrystal in simulated gastrointestinal fluid, and the result revealed that the cocrystal improves the dissolution behavior of HES compared with that of the pure substance. Furthermore, HES’s bioavailability in the cocrystal was six times higher than that of pristine drugs. These results may provide an efficient oral formulation for HES.

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“…Because of its potential health benefits such as antihyperlipidemic, cardioprotective, antihypertensive, antidiabetic, and antioxidant activities, HES has attracted considerable attention for its potential application as a nutraceutical ingredient in foods ( 25 , 26 ). Previous studies have reported the interaction of HES with various proteins, including glutenin ( 23 ), HMG-CoA reductase enzyme ( 27 ), SARS-CoV2 spike protein ( 28 ) and digestive enzyme ( 29 ). The results of these researches suggest that HES exerts strong binding affinity to these proteins.…”

Section: Introductionmentioning

confidence: 99%

“…It is known that the interacting mechanism varies greatly depending on protein and phenolic type ( 13 , 14 ). For instance, previous studies suggest that the binding of HES to glutenin ( 23 ) was dominated by hydrogen bonding and hydrophobic forces, whereas the binding of HES to α-amylase was dominated by van der Waals forces and hydrogen bonding ( 29 ). Consequently, it is important to establish the binding mechanism for specific protein-phenolic pairs, as well as the impact of these interactions on the functionality of the complexes formed.…”

Section: Introductionmentioning

confidence: 99%

Impacts of hesperidin on whey protein functionality: Interacting mechanism, antioxidant capacity, and emulsion stabilizing effects

et al. 2023

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The objective of this work was to explore the possibility of improving the antioxidant capacity and application of whey protein (WP) through non-covalent interactions with hesperidin (HES), a citrus polyphenol with nutraceutical activity. The interaction mechanism was elucidated using several spectroscopic methods and molecular docking analysis. The antioxidant capacity of the WP-HES complexes was analyzed and compared to that of the proteins alone. Moreover, the resistance of oil-in-water emulsions formulated using the WP-HES complexes as antioxidant emulsifiers to changes in environmental conditions (pH, ion strength, and oxidant) was evaluated. Our results showed that HES was incorporated into a single hydrophobic cavity in the WP molecule, where it was mainly held by hydrophobic attractive forces. As a result, the microenvironments of the non-polar tyrosine and tryptophan residues in the protein molecules were altered after complexation. Moreover, the α-helix and β-sheet regions in the protein decreased after complexation, while the β-turn and random regions increased. The antioxidant capacity of the WP-HES complexes was greater than that of the proteins alone. Non-radiative energy transfer from WP to HES was detected during complex formation. Compared to WP alone, the WP-HES complexes produced emulsions with smaller mean droplet diameters, exhibited higher pH and salt stability, and had better oxidative stability. The magnitude of these effects increased as the HES concentration was increased. This research would supply valuable information on the nature of the interactions between WP and HES. Moreover, it may lead to the creation of dual-function antioxidant emulsifiers for application in emulsified food products.

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Bioflavonoid (Hesperidin) Restrains Protein Oxidation and Advanced Glycation End Product Formation by Targeting AGEs and Glycolytic Enzymes

Cited by 18 publications

References 60 publications

Binding Studies of Caffeic and p-Coumaric Acid with α-Amylase: Multispectroscopic and Computational Approaches Deciphering the Effect on Advanced Glycation End Products (AGEs)

Binding Studies of Caffeic and p-Coumaric Acid with α-Amylase: Multispectroscopic and Computational Approaches Deciphering the Effect on Advanced Glycation End Products (AGEs)

Crystal Structure, Solubility, and Pharmacokinetic Study on a Hesperetin Cocrystal with Piperine as Coformer

Impacts of hesperidin on whey protein functionality: Interacting mechanism, antioxidant capacity, and emulsion stabilizing effects

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