Specifically designed peptide structures effectively suppressed oxidative reactions in chemical and cellular systems

被引：31

作者：

Bamdad, Fatemeh ^{[1
]}

Ahmed, Sahar ^{[2
,3
]}

Chen, Lingyun ^{[1
]}

机构：

[1] Univ Alberta, Dept Agr Food & Nutr Sci, Edmonton, AB T6G 2P5, Canada

[2] Assiut Univ, Dept Med Chem, Fac Pharm, Assiut 71526, Egypt

[3] Taibah Univ, Dept Pharmacognosy & Med Chem, Fac Pharm, Al Madinah 41477, Al Munawarah, Saudi Arabia

来源：

JOURNAL OF FUNCTIONAL FOODS | 2015年 / 18卷

基金：

加拿大自然科学与工程研究理事会;

关键词：

Peptides; Antioxidant capacity; Cellular models; Amyloid fibril formation; Antioxidant enzymes; ANTIOXIDANT PROPERTIES; PROTEIN; PURIFICATION; AGGREGATION;

D O I：

10.1016/j.jff.2015.06.055

中图分类号：

TS2 [食品工业];

学科分类号：

0832 ;

摘要：

Peptides were designed based on the identified structural motif of the most potent antioxidant peptides derived from barley protein. Six peptides contained the effective pentapeptide QPYPQ with appended Gln and Pro residues and the other peptides possessed higher hydrophobicity. The peptides have the repetitive sequences of Q P and Y to investigate the contribution of vicinal residues to their antioxidant capacity. Antioxidant activity of the synthetic peptides was evaluated in chemical and cellular models. Free radical scavenging assays demonstrated the positive role of QP and PY pairs in stabilizing the peptide radicals. Cellular models revealed that repetitive peptide sequences effectively inactivate lipid hydroperoxides and intracellular reactive oxygen species. Peptides with alternating residues were also found effective in inhibition of amyloid fibril formation. These results verified that in addition to the chemical structure of individual side chains, the combined effects of the vicinal residues are also important in antioxidant activity of the whole peptide. (C) 2015 Elsevier Ltd. All rights reserved.

引用

页码：35 / 46

页数：12

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