ANTIHYPERTENSIVE AND ANTIDIABETIC PEPTIDES DERIVED FROM IN SILICO SIMULATED GASTROINTESTINAL DIGESTION OF QUINOA (Chenopodium quinoa) GLOBULINS AND MOLECULAR DOCKING STUDY

Abstract

This study evaluated the impact of in silico simulated gastrointestinal digestion (GID) of four quinoa globulins on the potential to release ACE and DPP-IV inhibitor peptides (antihypertensive and antidiabetic properties, respectively), as well as performed a molecular docking study to evaluate the interactions produced in the peptide-enzyme complexes. In silico GID performed on quinoa globulins resulted in the formation of amino acids as well as peptides with two to five residues. The peptides PSF, IPG, CSG, SPR, CSPG and PPN stood out for their high bioactivity scores (> 0.6), for not showing toxicity, as well as presenting potential inhibitory properties to both ACE and DPP-IV enzymes evaluated by ToxinPred, PeptideRanker and BioPep tools, respectively. The molecular docking analysis allowed highlighting that all peptides interacted with the enzymes, finding favorable binding energy values, different number and type of interactions, either at the level of the enzyme active sites or not, characteristics that together would define the potential of the established interaction of the complexes formed. The results, at the level of a first screening, support that GID of quinoa globulins can give rise to peptides with both antihypertensive and antidiabetic properties, requiring further in vitro and in vivo studies.