4.7 Article

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

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出版社

ELSEVIER
DOI: 10.1016/j.ijbiomac.2022.09.259

关键词

Sesame protein; Peptides; Obesity; Pancreatic lipase inhibition; Molecular docking

资金

  1. Opening Project of Key Laboratory of Trace Element and Nutrition, National Health Commission of the Peoples' Republic of China [wlkfz202205]
  2. Scientific Research and Entrepreneurship Plan of College Students [G037-2022]
  3. Research Foundation for Youth Scholars of Beijing Technology and Business University [QNJJ2022-06]
  4. Discipline Construction-Food Science and Engineering [SPKX-202204]

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Peptides derived from sesame could potentially inhibit the activity of pancreatic lipase, reducing triglyceride absorption and preventing obesity.
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 IC50 values of 751 +/- 75, 907 +/- 91, 986 +/- 170, 1044 +/- 179 and 1183 +/- 179 mu M, 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.

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