Synergistic interaction of Cu(II) with caffeic acid and chlorogenic acid in α-glucosidase inhibition.

BACKGROUND: Phenolic acids are widespread in foods and are beneficial to human health. However, the role of metal ions in influencing the binding of proteins with phenolic acids that contain the same parent nucleus structure remains unclear. This study investigated the inhibitory effect of caffeic acid (CA) and chlorogenic acid (CHA) on α-glucosidase and the biological effect of copper on this process. RESULTS: It was found that the esterification of CA with quinic acid could increase the fluorescence quenching, conformational change, and inhibitory effect of CHA on α-glucosidase. Copper ions reduced their fluorescence quenching and conformation-changing ability by binding to the neighboring phenolic hydroxyl group but also increased their ability to alter secondary structure and to inhibit α-glucosidase and in vitro anti-glycation. CONCLUSION: Overall, this study shows that the binding of copper ions to the phenolic hydroxyl group adjacent to CA and CHA synergistically inhibited α-glucosidase. The findings will offer a theoretical basis for investigating the properties of metal ions and phenolic acid in food chemistry and their potential applications in the prevention and treatment of diabetes mellitus. © 2023 Society of Chemical Industry.

Molecular insights into α-glucosidase inhibition and antiglycation properties affected by the galloyl moiety in (-)-epigallocatechin-3-gallate.

BACKGROUND: Diabetes mellitus poses a substantial threat to public health due to rising morbidity and mortality. α-Glucosidase is one of the key enzymes affecting diabetes. Herein, (-)-epigallocatechin-3-gallate (EGCG) and (-)-epigallocatechin (EGC) were applied to clarify the role of the galloyl moiety of tea polyphenols in the inhibition of glycation and α-glucosidase activity. The structure-activity relationship of the galloyl moiety in EGCG on α-glucosidase was investigated in terms of inhibition kinetics, spectroscopy, atomic force microscopy and molecular docking. A bovine serum protein-fructose model was employed to determine the effect of the galloyl moiety on glycation. RESULTS: The results indicated that the introduction of a galloyl moiety enhanced the capacity of EGCG to inhibit glycation and α-glucosidase activity. The IC50 value of EGC is approximately 2400 times higher than that of EGCG. Furthermore, the galloyl moiety in EGCG altered the microenvironment and secondary structure of α-glucosidase, resulting in a high binding affinity of EGCG to α-glucosidase. The binding constant of EGCG to α-glucosidase at 298 K is approximately 28 times higher than that of EGC. CONCLUSION: Overall, the galloyl moiety of EGCG plays a crucial role in inhibiting glycation and α-glucosidase activity, which helps to enhance the molecular understanding of the structure and function of the polyphenol galloyl moiety in the science of food and agriculture. © 2023 Society of Chemical Industry.

Comparison of binding sites and affinity of flavonol-Cu(II) complexes with the same parent nucleus: Synthesis, DFT prediction, and coordination pattern.

This study explores the coordination dynamics between dietary polyphenols, specifically kaempferol, quercetin, and myricetin, and Cu ions in aqueous environments. A novel synthesis method for flavonol-Cu(II) coordination compounds is introduced, effectively reducing interference from free metal ions. Our results reveal consistent binding patterns of Cu ions with flavonols (2:1 ratio of flavonol to Cu(II)), predominantly at the 4,5 sites. Various analytical techniques are used to validate these coordination ratios and sites. The binding affinity of the flavonols for Cu ions follows a descending sequence: myricetin > quercetin > kaempferol. Notably, coordination with Cu ions enhances the free-radical scavenging activities of these flavonols. These findings hold substantial importance for food chemistry, biology, and medicine, providing crucial insights into the way dietary flavonols form stable structures in environments similar to human body fluids and their interactions with metal ions, opening new possibilities for their application and understanding in diverse scientific domains.

Tannin complexation with metal ions and its implication on human health, environment and industry: An overview.

Tannins, also known as plant polyphenols (PPs), are secondary metabolites widely existing in higher plants and are a kind of natural renewable resource with wide distribution, variety and quantity. Tannin has become an important class of fine chemicals due to the easily modified molecular structure and the properties of antibacterial and antioxidant, combining with protein and complexing with metal ion. Besides being used for tanning leather, tannins are also widely used in wood adhesive, concrete water-reducing agents, oil drilling fluid viscosity-reducing agents, pharmaceutical, mineral processing, water treatment, gas desulfurization, metal anticorrosion, wood anticorrosion, printing and dyeing, liquor clarification, oil antioxidant, daily chemical products and other products preparation. There are two groups of tannins: condensed tannins (CTs) (flavonoid-derived proanthocyanidins) and hydrolysable tannins (HTs) (gallic acid ester-derived). Tannins can form complexes with metals through the ortho-dihydroxyphenolic group(s), especially with transition metals. The structure-activity relationships, stoichiometry, and origin of the insolubility of which were emphasized. Furthermore, this paper proposed an in-depth discussion of the associations of tannins-metal complexes in human health, environment and industries.

Effect of Metal Ions on the Interaction of Condensed Tannins with Protein.

A quantitative analysis of the precipitate effects of metal ions (Al3+, Fe2+, Cu2+, Zn2+) by bovine serum albumin (BSA) on two condensed tannins (CT) from sorghum and plum was presented in this study. The results showed that adding metal ions enhanced the precipitation of proteins by CT, depending on the type and concentration of the metal ions used in the reaction system. The presence of metal ions and precipitation results on the CT-protein complex showed that Al3+ and Fe2+ had a higher binding ability with CT and a weaker influence on the precipitation of the CT-protein complex than Cu2+ and Zn2+. However, when the initial reaction solution contained excessive amounts of BSA, the extra addition of metal ions had no significant effect on the amount of BSA precipitation. Reversely, adding Cu2+ or Zn2+ into the reaction solution increased the amount of precipitated BSA when the amount of CT was excessive. In addition, the amounts of CT from plum, rather than sorghum, generated more protein precipitate in the presence of Cu2+ or Zn2+, which may be due to the different binding modes between the metal ion and the CT-BSA complex. This study also proposed a model of the interaction between the metal ion and the CT-protein precipitate.

A spectroscopic and quantum chemical calculation method for the characterisation of metal ions complexed with propyl gallate and procyanidins.

The deprotonation mechanism for the phenolic hydroxyl and the complexing of metal ions with a commonly used food additive, propyl gallate (PG) were studied theoretically and experimentally. The interaction of procyanidins [PC, epicatechin16 (4 → 8) catechin], and its basic monomeric unit catechin (CA) with metal ions was studied by the fluorescence quenching spectra. The results showed that the 9-OH quinoid PG was formed at higher pH (10.9) by the oxidization of phenolic hydroxyl. The binding affinities (Ka) and stoichiometry of these metal ions with PG were determined. The Al3+ in PG-Al complex [Al(PG)(H2O)2Cl2]- was coordinated at the 8,9-OH doubly deprotonated catechol site with double chloride ions (Cl-) and double water molecules (H2O). The fluorescence quenching titration with Sn2+, Zn2+, Cu2+, Al3+ and Fe3+ revealed that the stoichiometries of metal-bound PC were 1:1, 2:3, 2:3, 2:3 and 1:1, respectively. The presence of bovine serum albumin (BSA) could enhance the complexing strength of PC with metal ions.

Effect of Cu2+ and Al3+ on the interaction of chlorogenic acid and caffeic acid with serum albumin.

Despite the phenolic acids' health benefits, their interactions with proteins are still unclear. In this study, the interactions of Bovine Serum Albumin (BSA) with chlorogenic acid (CHA), caffeic acid (CA), and their Al3+, Cu2+ complexes were studied by using circular dichroism (CD) spectroscopy, fluorescence spectroscopy, and UV/Vis spectroscopy. It was found that esterification of carboxyl group of CA with quinic acid increased the binding affinities for BSA. After chelating with Cu2+ and Al3+, both CHA and CA exhibited high binding affinities for BSA. CHA could form CHA-Cu2 and CHA-Al2 complex with Cu2+ and Al3+. The result of CD spectroscopy demonstrated that the binding of CHA and Al3+ with BSA contributed to the folding of BSA secondary structure. In addition, with the presence of CHA, binding with Al3+ could also induce changes in BSA conformation. The binding sites of both CHA and CA were closed to Trp213.

The gelation properties of myofibrillar proteins prepared with malondialdehyde and (-)-epigallocatechin-3-gallate.

Impact of malondialdehyde (MDA) and (-)-Epigallocatechin-3-gallate (EGCG) on gelling properties of myofibrillar proteins (MPs) was investigated. Addition of 6 mM MDA enhanced molecular interactions of proteins, thus the strength and elastic modulus (G') of gel were improved. EGCG addition aggravated gel quality deterioration due to further modification of MPs induced by EGCG. Addition of 12 mM MDA jeopardized gel quality according to the increasing of strength and G', but the decreasing of water-holding capacity (WHC), and the collapse of microstructure. Nevertheless, EGCG reacted with MDA forming EGCG-MDA adducts, hence improved gel quality, which was supported by the decreasing of strength, but the increasing of WHC, and the repaired microstructure of gel at 12 mM MDA. Addition of 24 mM MDA severely jeopardized gel quality, which became even worse due to EGCG addition. This work is helpful to understand the impact of MDA and polyphenols on the gel-forming capacity of MPs.