Purification, identification and molecular docking of dual‐functional peptides derived from corn protein hydrolysates with antioxidant and anti‐adhesive activity against Helicobacter pylori

Abstract

AbstractBackgroundMore than 50% of the world population is infected with Helicobacter pylori (H. pylori), which is classified as group I carcinogen by the WHO.ResultsCorn protein dual‐functional peptides were identified and functionally analyzed in vitro and in silico. Two novel dual‐functional peptides were identified as Cys‐Gln‐Asp‐Val‐Pro‐Leu‐Leu (CQDVPLL, CQ7) and Thr‐Ile‐Phe‐Pro‐Gln‐Cys (TIFPQC, TI6) by Nano‐LC‐MS/MS. The anti‐adhesive activity against Helicobacter pylori of CQ7 and TI6 was 45.17±2.41% and 48.62±1.84% at 4 mg/mL, respectively. In silico prediction showed that CQ7 and TI6 had good physicochemical properties. Molecular docking demonstrated that CQ7 and TI6 could bind to the adhesions BabA and SabA by hydrophobic interactions and hydrogen bonds, preventing Helicobacter pylori infection. Moreover, CQ7 showed strong antioxidant activity due to its unique amino acid composition.ConclusionThe present study demonstrated that the identified peptides CQ7 and TI6 possess antioxidant and anti‐adhesive effects, preventing Helicobacter pylori infection as well as alleviating oxidative injury to the gastric mucosa.This article is protected by copyright. All rights reserved.