Novel Multitarget ACE Inhibitory Peptides from Bovine Colostrum Immunoglobulin G: Cellular Transport, Efficacy in Regulating Endothelial Dysfunction, and Network Pharmacology Studies.

In this study, we used traditional laboratory methods, bioinformatics, and cellular models to screen novel ACE inhibitory (ACEI) peptides with strong ACEI activity, moderate absorption rates, and multiple targets from bovine colostrum immunoglobulin G (IgG). The purified fraction of the compound proteinase hydrolysate of IgG showed good ACEI activity. After nano-UPLC-MS/MS identification and in silico analysis, eight peptides were synthesized and verified. Among them, SFYPDY, TSFYPDY, FSWF, WYQQVPGSGL, and GVHTFP were identified as ACEI peptides, as they exhibited strong ACEI activity (with IC50 values of 104.7, 80.0, 121.2, 39.8, and 86.3 µM, respectively). They displayed good stability in an in vitro simulated gastrointestinal digestion assay. In a Caco-2 monolayer model, SFYPDY, FSWF, and WYQQVPGSGL exhibited better absorption rates and lower IC50 values than the other peptides and were thereby identified as novel ACEI peptides. Subsequently, in a H2O2-induced endothelial dysfunction (ED) model based on HUVECs, SFYPDY, FSWF, and WYQQVPGSGL regulated ED by reducing apoptosis and ROS accumulation while upregulating NOS3 mRNA expression. Network pharmacology analysis and RT-qPCR confirmed that they regulated multiple targets. Overall, our results suggest that SFYPDY, FSWF, and WYQQVPGSGL can serve as novel multitarget ACEI peptides.

The formation mechanism and textural properties of a complex gel based on soybean glycinin-chitosan complex coacervates: Effects of pH, heat treatment temperature and centrifugation.

The soybean glycinin (11S)-chitosan (CS) complex gels with various textural properties were successfully constructed. The process involved the initial formation of 11S-CS coacervates through electrostatic interactions, followed by a heating treatment to obtain the final complex gels. The impacts of pH, heating temperature, and centrifugation on 11S-CS complex gel properties were investigated. The results indicated that the pore arrangement of the gel formed at pH 7.3 was more tightly and uniformly packed than those formed at pH 6.8 and 7.8. Centrifugation facilitated denser and more ordered gel structures at the three pH values, while increasing the heating temperature exhibited the opposite trend at pH 6.8 and 7.8. These structural differences were also reflected in the rheological and textural properties of the gel. The 11S-CS complex gels exhibited an elasticity-based gel property. The textural properties of gels formed at pH 6.8 were stronger compared to those formed at pH 7.3 and 7.8. However, when the 11S-CS coacervates were heated without centrifugation, the resulting gels were weak. This study emphasizes the potential of using protein/polysaccharide associative interactions during gel formation to alter the microstructure of the gel, meeting various production requirements.