Active peptides with hypoglycemic effect obtained from hemp (Cannabis sativa L) protein through identification, molecular docking, and virtual screening.

Hemp (Cannabis sativa L) seeds are rich in proteins of high nutritional value, which makes the study of beneficial properties of hemp seed proteins and peptides, such as hypotensive and hypoglycemic effects, increasingly attractive. The present results confirm the good processability and stability of the hemp protein hydrolysate obtained by enzymatic hydrolysis of non-dehulled hemp seed meal (NDHM). Six peptides with potential hypoglycemic activity were obtained by ethanol-graded precipitation, Nano LC-Q-Orbitrap-MS/MS mass spectrometry, and computerized virtual screening. Further, validation experiments for in vitro synthesis showed that TGLGR, SPVI, FY, and FR exhibited good α-glucosidase inhibitory activity, respectively. Animal experiments showed that the hemp protein peptides modulated blood glucose and blood lipids in hyperglycemic rats. These results indicate that hemp protein peptides can reduce blood glucose levels in hyperglycemic rats, suggesting that hemp proteins may be a promising natural source for the prevention and treatment of hyperglycemia.

Production and characteristics of a novel chicken egg yolk antibody (IgY) against periodontitis-associated pathogens.

Periodontitis is a bacterial biofilm-induced oral disease, mostly caused by Aggregatibacter actinomycetemcomitans (A. actinomycetemcomitans) and Porphyromonas gingivalis (P. gingivalis). Oral administration of chicken egg yolk antibody (IgY) is a promising nutritional strategy to control pathogen infections. The objective of this study was to produce an A. actinomycetemcomitans- and P. gingivalis-specific IgY and evaluate its effects on bacterial agglutination and biofilm formation. Thirty laying hens were immunized with a complex of lysate containing typical molecular weights of membrane proteins of A. actinomycetemcomitans and P. gingivalis. IgY was isolated by polyethylene glycol 6000 and ammonium sulfate and purified by dialysis. The results of enzyme-linked immunosorbent assay showed that the obtained IgY were specific to both A. actinomycetemcomitans and P. gingivalis. In addition, immunoelectron microscopy scanning and crystal violet staining showed that the IgY could bind to cell wall of the pathogens and efficiently accelerate agglutination and inhibit biofilm formation. Furthermore, the activity of the IgY remained stable at different temperature, pH, and storage period. This is the first report that a novel two-in-one IgY was produced to modulate the agglutination and biofilm formation of A. actinomycetemcomitans and P. gingivalis, suggesting the potential of IgY to control periodontitis caused by oral pathogens.