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Corn gluten meal peptides inhibit prolyl oligopeptidase and modulate α-synuclein aggregation in KCl-treated SH-SY5Y cells
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Document Title
Corn gluten meal peptides inhibit prolyl oligopeptidase and modulate α-synuclein aggregation in KCl-treated SH-SY5Y cells
Author
Chanajon P., Tian F., Noisa P., Roytrakul S., Yongsawatdigul J.
Affiliations
School of Food Technology, Institute of Agricultural Technology, Suranaree University of Technology, Ratchasima, Nakhon, 30000, Thailand; School of Biotechnology, Institute of Agricultural Technology, Suranaree University of Technology, Ratchasima, Nakhon, 30000, Thailand; National Center for Genetic Engineering and Biotechnology, Pathumthani, 12120, Thailand
Type
Article
Source Title
Journal of Functional Foods
ISSN
17564646
Year
2023
Volume
104
Page
-
Open Access
All Open Access, Gold
Publisher
Elsevier Ltd
DOI
10.1016/j.jff.2023.105501
Format
Abstract
Prolyl oligopeptidase (POP) is known to be related to neurocognitive disorder as it degrades neuroactive peptides. POP inhibitory peptides from corn gluten meal hydrolysate (CGM-H) were identified and characterized. After a series of chromatographic separations, ALLTLSPLGPA was identified as the most effective POP inhibitor, with an IC50 value of 0.79 ± 0.004 mM. Its in silico gastrointestinal (GI)-digested peptide, SPLGPA, exhibited 3-fold lower POP inhibitory activity, while higher inhibition was observed in SH-SY5Y cells when compared to its parent peptide. In addition, 25 µM ALLTLSPLGPA notably reduced α-synuclein aggregation in KCl-treated SH-SY5Y cells. ALLTLSPLGPA and SPLGPA were characterized as mixed-type and uncompetitive inhibitors, respectively. They bound to POP via hydrogen bonds at the β-propeller domain. These results demonstrated that peptides derived from CGM could have potential for developing nutraceutical products targeting brain health. © 2023 The Author(s)
Funding Sponsor
National Research Council of Thailand
Publication Source
WOS