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New insights into the structure-activity relationships of antioxidative peptide PMRGGGGYHY.

Authors
  • Wu, RiBang1
  • Huang, JiaFeng1
  • Huan, Ran1
  • Chen, LeiLei2
  • Yi, CuiPing3
  • Liu, Dan1
  • Wang, Meng1
  • Liu, CongLing1
  • He, HaiLun4
  • 1 School of Life Sciences, Central South University, Changsha 410013, China. , (China)
  • 2 Beijing Advanced Innovation Center for Food Nutrition and Human Health, Beijing Technology and Business University (BTBU), China; Institute of Agro-Food Science and Technology, Shandong Academy of Agricultural Sciences, Key Laboratory of Agro-Products Processing Technology of Shandong Province, Key Laboratory of Novel Food Resources Processing, Ministry of Agriculture, 202 Gongye North Road, Jinan 250100, China. , (China)
  • 3 School of Chemistry and Food Engineering, Changsha University of Science and Technology, Changsha 410114, China. , (China)
  • 4 School of Life Sciences, Central South University, Changsha 410013, China. Electronic address: [email protected] , (China)
Type
Published Article
Journal
Food chemistry
Publication Date
Feb 01, 2021
Volume
337
Pages
127678–127678
Identifiers
DOI: 10.1016/j.foodchem.2020.127678
PMID: 32791429
Source
Medline
Keywords
Language
English
License
Unknown

Abstract

The sequence and structure of antioxidant peptides play fundamental roles in their antioxidant functions. However, the structural mechanism of antioxidant peptides is still unclear. In this study, we used quantum calculations to reveal the antioxidant mechanism of the peptide PMRGGGGYHY. PMRGGGGYHY has multiple antioxidant active sites, and two tyrosine residues were determined to be the major active sites. Based on the structure-activity relationships of PMRGGGGYHY, the antioxidant activity of the modified peptide significantly improved by 4.8-fold to 9.73 ± 0.61 μmol TE/μmol. In addition, the removal of glycine residues from PMRGGGGYHY would increase the energy of the HOMOs and simplify the hydrogen bonding network, causing a significant increase in antioxidant activity. The intracellular ROS scavenging ability gradually decreased with decreasing glycine content. This same peptide has very different effects in vitro versus as a cellular antioxidant. This paper provides new insights into the structural mechanism and rational design/modification of novel antioxidant peptides. Copyright © 2020 Elsevier Ltd. All rights reserved.

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