Pancreatic lipase inhibitory effects of peptides derived from sesame proteins: In silico and in vitro analyses.

Pancreatic lipase (PL) is the main digestive enzyme that is responsible for breaking triglycerides into smaller components for absorption. Inhibition of PL can effectively reduce triglyceride absorption, helping to prevent the development of obesity. The objective of this study was to investigate the PL inhibitory activity of peptides derived from sesame (Sesamum indicum L.) in silico and in vitro. In silico proteolysis of sesame proteins with pepsin, trypsin and chymotrypsin was performed with ExPASy PeptideCutter. Six peptides (TF, EW, QWM, NIF, AGY and PIF) were screened out by PeptideRanker, SwissADME and AutoDock. Molecular docking analysis showed that these six peptides could interact directly with Phe77, His151, Ser152, Phe215 and His263 at the key sites of PL. The six peptides were further synthesized to verify their PL-inhibitory effects in vitro , and TF, EW, QWM, NIF and AGY exhibited inhibitory activity on PL with IC 50 values of 751 ± 75, 907 ± 91, 986 ± 170, 1044 ± 179 and 1183 ± 179 μM, respectively. Inhibitory kinetics indicated that TF, QWM and NIF were mixed-type inhibitors of PL, while EW and AGY were uncompetitive inhibitors. Our results suggest that peptides from sesame could potentially inhibit the activity of PL. [Display omitted] • 11S globulin and 2S albumin from sesame seeds was selected for in silico digestion. • Five pancreatic lipase (PL) inhibitory peptides were screened in silico and in vitro. • The IC 50 values of five peptides were smaller than or close to that of orlistat. • Peptides could interact with active sites of PL via H-bonds and hydrophobic forces. • TF, QWM and NIF were mixed-type inhibitors, while EW and AGY were uncompetitive ones. [ABSTRACT FROM AUTHOR]