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Interactions of C. frondosa-derived inhibitory peptides against angiotensin I-converting enzyme (ACE), α-amylase and lipase.

Authors
  • Zhang, Yi1
  • He, Shudong2
  • Rui, Xin3
  • Simpson, Benjamin K4
  • 1 Department of Food Science and Agricultural Chemistry, McGill University, Ste-Anne-de-Bellevue H9X 3V9, Québec, Canada; IPREM, E2S UPPA, CNRS, Université de Pau et des Pays de l'Adour, 64000 Pau, France. Electronic address: [email protected] , (Canada)
  • 2 School of Food and Biological Engineering, Hefei University of Technology, Hefei 230009, Anhui, China. Electronic address: [email protected] , (China)
  • 3 College of Food Science and Technology, Nanjing Agricultural University, Jiangsu Province, China. Electronic address: [email protected] , (China)
  • 4 Department of Food Science and Agricultural Chemistry, McGill University, Ste-Anne-de-Bellevue H9X 3V9, Québec, Canada. Electronic address: [email protected] , (Canada)
Type
Published Article
Journal
Food chemistry
Publication Date
Jan 15, 2022
Volume
367
Pages
130695–130695
Identifiers
DOI: 10.1016/j.foodchem.2021.130695
PMID: 34365251
Source
Medline
Keywords
Language
English
License
Unknown

Abstract

The study illustrates the molecular mechanisms by which marine-derived peptides exhibited different structures and inhibition functions to concurrently inhibit multiple enzymes involved in chronic diseases. Peptides (2 mg/mL) exhibited inhibition against angiotensin-converting enzyme (ACE, inhibition of 52.2-78.8%), pancreatic α-amylase (16.3-27.2%) and lipase (5.3-17.0%). Further in silico analyses on physiochemistry, bioactivity, safety and interaction energy with target enzymes indicated that one peptide could inhibit multiple enzymes. Peptide FENLLEELK potent in inhibiting both ACE and α-amylase showed different mechanisms: it had ordered extended structure in ACE active pocket with conventional H-bond towards Arg522 which is the ligand for activator Cl-, while the peptide folded into compact "lariat" conformation within α-amylase active site and the K residue in peptide formed intensive H-bonds and electrostatic interactions with catalytic triad Asp197 - Asp300 - Glu233. Another peptide APFPLR showed different poses in inhibiting ACE, α-amylase and lipase, and it formed direct interactions to lipase catalytic residues Phe77 & His263. Copyright © 2021 Elsevier Ltd. All rights reserved.

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