In this study, in silico approaches are employed to investigate the binding mechanism of peptides derived from cowpea β-vignin and HMG-CoA reductase. With the obtained information, we designed synthetic peptides to evaluate their in vitro enzyme inhibitory activity. In vitro, the total protein extract and <3 kDa fraction, at 5000 µg, support this hypothesis (95% and 90% inhibition of HMG-CoA reductase, respectively). Ile-Ala-Phe, Gln-Gly-Phe, and Gln-Asp-Phe peptides were predicted to bind to the substrate binding site of HMGCR via HMG-CoAR. In silico, it was established that the mechanism of HMG-CoA reductase inhibition largely entailed mimicking the interactions of the decalin ring of simvastatin and via H-bonding; in vitro studies corroborated the predictions, whereby the HMG-CoA reductase activity was decreased by 69%, 77%, and 78%, respectively. Our results suggest that Ile-Ala-Phe, Gln-Gly-Phe, and Gln-Asp-Phe peptides derived from cowpea β-vignin have the potential to lower cholesterol synthesis through a statin-like regulation mechanism.

Adzuki seed β-vignin, a vicilin-like globulin, has proven to exert various health-promoting biological activities, notably in cardiovascular health. A simple scalable enrichment procedure of this protein for further nutritional and functional studies is crucial. In this study, a simplified chromatography-independent protein fractionation procedure has been optimized and described. The electrophoretic analysis showed a high degree of homogeneity of β-vignin isolate. Furthermore, the molecular features of the purified protein were investigated. The adzuki bean β-vignin was found to have a native size of 146 kDa, and the molecular weight determined was consistent with a trimeric structure. These were identified in two main polypeptide chains (masses of 56–54 kDa) that are glycosylated polypeptides with metal binding capacity, and one minor polypeptide chain with a mass 37 kDa, wherein these features are absent. The in vitro analysis showed a high degree of digestibility of the protein (92%) and potential anti-inflammatory capacity. The results lay the basis not only for further investigation of the health-promoting properties of the adzuki bean β-vignin protein, but also for a possible application as nutraceutical molecule.

The increased mortality rates associated with antibiotic resistance has become a significant public health problem worldwide. Living beings produce a variety of endogenous compounds to defend themselves against exogenous pathogens. The knowledge of these endogenous compounds may contribute to the development of improved bioactive ingredients with antimicrobial properties, useful against conventional antibiotic resistance. Cowpea is an herbaceous legume of great interest due to its high protein content and high productivity rates. The study of genetic homology of vicillin (7S) from cowpea (Vigna unguiculata L.) with vicilins from soybean and other beans, such as adzuki, in addition to the need for further studies about potential biological activities of this vegetable, led us to seek the isolation of the vicilin fraction from cowpea and to evaluate the potential in vitro inhibitory action of pathogenic microorganisms. The cowpea beta viginin protein was isolated, characterized, and hydrolyzed in silico and in vitro by two enzymes, namely, pepsin and chymotrypsin. The antimicrobial activity of the protein hydrolysate fractions of cowpea flour was evaluated against Staphylococcus aureus and Pseudomonas aeruginosa, confirming the potential use of the peptides as innovative antimicrobial agents.