Inflammation is considered to be a crucial factor in the development of chronic diseases, eight of which were listed among the top ten causes of death worldwide in the World Health Organization’s World Health Statistics 2019. Moreover, traditional drugs for inflammation are often linked to undesirable side effects. As gentler alternatives to traditional anti-inflammatory drugs, plant-derived bioactive peptides have been shown to be effective interventions against various chronic diseases, including Alzheimer’s disease, cardiovascular disease and cancer. However, an adequate and systematic review of the structures and anti-inflammatory activities of plant-derived bioactive peptides has been lacking. This paper reviews the latest research on plant-derived anti-inflammatory peptides (PAPs), mainly including the specific regulatory mechanisms of PAPs; the structure–activity relationships of PAPs; and their enzymatic processing based on the structure–activity relationships. Moreover, current research problems for PAPs are discussed, such as the shallow exploration of mechanisms, enzymatic solution determination difficulty, low yield and unknown in vivo absorption and metabolism and proposed future research directions. This work aims to provide a reference for functional activity research, nutritional food development and the clinical applications of PAPs.

Calcium is one of the most important mineral elements in the human body and is closely related to the maintenance of human health. To prevent calcium deficiency, various calcium supplements have been developed, but their application tends to be limited by low calcium content and highly irritating effects on the stomach, among other side effects. Recently, calcium–peptide chelates, which have excellent stability and are easily absorbed, have received attention as an alternative emerging calcium supplement. Calcium-binding peptides (CaBP) are usually obtained via the hydrolysis of animal or plant proteins, and calcium-binding capacity (CaBC) can be further improved through chromatographic purification techniques. In calcium ions, the phosphate group, carboxylic group and nitrogen atom in the peptide are the main binding sites, and the four modes of combination are the unidentate mode, bidentate mode, bridging mode and α mode. The stability and safety of calcium–peptide chelates are discussed in this paper, the intestinal absorption pathways of calcium elements and peptides are described, and the bioavailability of calcium–peptide chelates, both in vitro and in vivo, is also introduced. This review of the research status of calcium–peptide chelates aims to provide a reasonable theoretical basis for their application as calcium supplementation products.

Hyperuricemia (HUA), or elevated uric acid in the blood, has become more prevalent in recent years. Polyphenols, which are known to have good inhibitory activity on xanthine oxidoreductase (XOR), are effective in uric acid reduction. In this review, we address the structure–activity relationship of flavonoids that inhibit XOR activity from two perspectives: the key residues of XOR and the structural properties of flavonoids. Flavonoids’ inhibitory effect is enhanced by their hydroxyl, methoxy, and planar structures, whereas glycosylation dramatically reduces their activity. The flavonoid structure–activity relationship informed subsequent discussions of the changes that occur in polyphenols’ XOR inhibitory activity during their extraction, processing, gastrointestinal digestion, absorption, and interactions. Furthermore, gastrointestinal digestion and heat treatment during processing can boost the inhibition of XOR. Polyphenols with comparable structures may have a synergistic effect, and their synergy with allopurinol thus provides a promising future research direction.

Hyperuricemia, a disorder of purine metabolism associated with cardiovascular disease, gout, and kidney disease, can be alleviated by food-derived peptides. However, the precise mechanisms remain unclear, hindering their development. This study reviews uric acid-lowering peptides from various sources, focusing on two pathways: inhibiting uric acid production and promoting excretion. Low-molecular-weight peptides (<1000 Da) exhibited superior uric acid-lowering effects. We further explored the relationships between amino acid composition and their target interactions. Peptides rich in cyclic amino acids (tryptophan, phenylalanine, and histidine) and containing small amounts of linear amino acids (leucine, cysteine, and glycine) demonstrated significant potential for lowering uric acid. These findings provide theoretical support for developing novel functional foods for the management of hyperuricemia.

The occupational groups exposed to air pollutants, particularly PM2.5, are closely linked to the initiation and advancement of respiratory disorders. The aim of this study is to investigate the potential protective properties of selenium-enriched soybean peptides (Se-SPeps), a novel Se supplement, in mitigating apoptosis triggered by PM2.5 in A549 lung epithelial cells. The results indicate a concentration-dependent reduction in the viability of A549 cells caused by PM2.5, while Se-SPeps at concentrations of 62.5–500 µg/mL showed no significant effect. Additionally, the Se-SPeps reduced the production of ROS, proinflammatory cytokines, and apoptosis in response to PM2.5 exposure. The Se-SPeps suppressed the PM2.5-induced upregulation of Bax/Bcl-2 and caspase-3, while also restoring reductions in p-Akt in A549 cells. The antiapoptotic effects of Se-SPeps have been found to be more effective compared to SPeps, SeMet, and Na₂SeO₃ when evaluated at an equivalent protein or Se concentration. Our study results furnish evidence that supports the role of Se-SPeps in reducing the harmful effects of PM2.5, particularly in relation to its effect on apoptosis, oxidative stress, and inflammation.

This study systematically explored the inhibitory mechanisms against sucrase exerted by sugarcane molasses polyphenol extract (SMPE) and its three principal chlorogenic acid analogs: neochlorogenic acid (NA), chlorogenic acid (CA), and methyl chlorogenate (MC). By integrating in vitro assays, molecular simulations, and spectroscopic analyses, we demonstrated synergistic inhibition among the components. SMPE exhibited the greatest inhibitory potency (IC₅₀ = 3.58 ± 0.16 mg/mL), with an IC₅₀ significantly lower than those of the individual compounds. Synergy analysis indicated marked synergistic effects for both the CA-NA pair and the ternary mixture. Simultaneous multi-ligand docking further suggested complementary co-binding configurations and interactions with residues surrounding the catalytic region, providing a possible structural interpretation of the experimentally observed synergistic effects. Mechanistically, CA and NA exhibited competitive inhibition, whereas MC and SMPE showed mixed-type inhibition; fluorescence, CD, and thermal stability analyses revealed compound-dependent changes in aromatic residue microenvironments, secondary structure, and protein stability, while molecular modeling predicted peripheral binding of CA/NA and catalytic-region interactions of MC, suggesting distinct but complementary routes for perturbing substrate recognition and catalysis. This study provides mechanistic insight into the synergistic inhibition of sucrase by SMPE and supports its potential development as a natural agent for modulating postprandial glycemia.