No abstract

There is a renewed interest on the reliance of food-based bioactive compounds as sources of nutritive factors and health-beneficial chemical compounds. Among these food components, several proteins from foods have been shown to promote health and wellness as seen in proteins such as α/γ-conglutins from the seeds of Lupinus species (Lupin), a genus of leguminous plant that are widely used in traditional medicine for treating chronic diseases. Lupin-derived peptides (LDPs) are increasingly being explored and they have been shown to possess multifunctional health improving properties. This paper discusses the intestinal transport, bioavailability and biological activities of LDPs, focusing on molecular mechanisms of action as reported in in vitro, cell culture, animal and human studies. The potentials of several LDPs to demonstrate multitarget mechanism of regulation of glucose and lipid metabolism, chemo- and osteoprotective properties, and antioxidant and anti-inflammatory activities position LDPs as good candidates for nutraceutical development for the prevention and management of medical conditions whose etiology are multifactorial.

Soluble epoxide hydrolase (sEH) contributes to the pathophysiology of neurodegenerative diseases by decreasing the epoxyeicosatrienoic acids/dihydroeicosatrienoic acids ratio and influencing the anti-inflammatory system. Thus, sEH inhibition reduces systemic inflammation, particularly in the brain. This study investigated sEH inhibition by a tetrapeptide, YMSV, and its mechanism of action. Enzyme inhibition kinetics demonstrated that YMSV is a mixed-competitive inhibitor of sEH, with a half-maximal inhibitory concentration (IC50) of 179.5 ± 0.92 µM. Secondary structural analysis of sEH by circular dichroism showed that YMSV decreased the α-helices by 7.7% and increased the β-sheets and random coils by 11.4% and 22%, respectively. Molecular docking simulation indicated that YMSV formed a hydrogen bond with the Asp333 residue of the hydrolase pocket of sEH in addition to the binding of non-active site residues. The findings provide new insights into the mechanism of sEH inhibition by YMSV and its potential as a peptide-based anti-depressant nutraceutical.