Characterizations of a Food Decapeptide Chelating with Zn(II)

• Walnut proteins and peptides have been reported to have great zinc-carrying activity. In this study, the decapeptide EPNGLLLPQY (WP-10) derived from walnut protein has been prepared to figure out zinc binding mechanisms and structure-activity relationships. The space-conformation of this peptide has converted after being chelated with Zn(II). As to secondary structure, the beta-sheet structure of the peptide turned into alpha-helix and beta-turn structure. According to the atomic absorption spectra analysis, one peptide could bind with one Zn(II) via four different binding sites. The signals of different groups in infrared spectroscopy have shifted before and after chelation, and the major functional groups of this peptide involved in chelation are -NH2 and -C=O. GLU1, PRO2, ASP3, GLU4, and LEU6, and the molecular docking proved their participation in the chelating with Zn(II). (c) 2020 International Association of Dietetic Nutrition and Safety. Publishing services by Atlantis Press International B.V. This is an open access article distributed under the CC BY-NC 4.0 license (http://creativecommons.org/licenses/by-nc/4.0/).

Ämnesord

NATURVETENSKAP  -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)

NATURAL SCIENCES  -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)

Nyckelord

Peptide

zinc

binding sites

molecular docking

structure

Publikations- och innehållstyp

ref (ämneskategori)

art (ämneskategori)