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Analysis of α‐helix unfolding in the pine nut peptide Lys‐Cys‐His‐Lys‐Pro induced by pulsed electric field
Author(s) -
Xing Jie,
Zhang Sitian,
Zhang Mingdi,
Lin Songyi
Publication year - 2017
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.8273
Subject(s) - helix (gastropod) , chemistry , peptide , dpph , hydrogen bond , electric field , antioxidant , abts , food science , biochemistry , molecule , organic chemistry , biology , ecology , physics , quantum mechanics , snail
BACKGROUND A variety of analytical techniques were applied to explore the effects of pulsed electric field ( PEF ) on α‐helix structural changes in the novel antioxidant peptide Lys‐Cys‐His‐Lys‐Pro ( KCHKP , 611.76 Da). RESULTS The relative α‐helix content of the KCHKP peptide was significantly altered from 100% to 89.91 ± 0.97% when the electric pulse frequency was 1800 Hz and the field intensity was 10 kV cm −1 . Moreover, the 1,1‐diphenyl‐2‐pycryl‐hydrazyl ( DPPH ) and 2,2‐azinobis diammonium salt ( ABTS ) radical‐scavenging activities of PEF ‐treated KCHKP were increased from 56.31% ± 0.74% to 84.33% ± 1.23% and from 40.56% ± 0.78% to 51.33% ± 0.27%, respectively. CONCLUSION PEF treatment increased peptide linkage stretch vibration and altered hydrogen bonding of KCHKP . The stability of the α‐helix structure was influenced by hydrogen bonds within the peptide linkage of KCHKP induced by PEF and was related to changes in antioxidant activity. © 2017 Society of Chemical Industry