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Abstract Title:

Isolation, Identification, and Immunomodulatory Mechanism of Peptides from(Maca) Protein Hydrolysate.

Abstract Source:

J Agric Food Chem. 2022 Mar 31. Epub 2022 Mar 31. PMID: 35357828

Abstract Author(s):

Ping He, Leiman Pan, Hui Wu, Lina Zhang, Yi Zhang, Yizhe Zhang, Jinxi Yang, Zhengli Lin, Mengmeng Zhang

Article Affiliation:

Ping He

Abstract:

Maca is a protein-enriched edible plant with immunomodulatory activity. However, the role of proteins in the immunomodulatory activity of maca is unclear. In this study, peptide products of maca proteins obtained through in vitro gastrointestinal digestion were isolated and purified, and the immunomodulatory activities of these peptides were assessed in macrophages (RAW 264.7 cells). The results show that the maca protein hydrolysate enhanced the phagocytic capacity and NO, TNF-α, and IL-6 secretion of RAW 264.7 cells. Forty-five peptides from known proteins of maca or the cruciferous family were identified by ultraperformance liquid chromatography-tandem mass spectrometry in the hydrolysate, and the peptide RNPFLP exhibited the strongest immunomodulatory activity. Antibody blocking, siRNA, pathway inhibitors, and western blot assays showed that RNPFLP-activated RAW 264.7 cells through the NF-κB and MAPK signaling pathways mediated by TLR2 and TLR4 receptors. An analysis of the structure-activity relationship showed that the N-Hactive site in arginine plays an important role in the immunomodulatory activity of RNPFLP. This study provides a new understanding of the immunomodulatory activity of maca.

Study Type : In Vitro Study
Additional Links
Pharmacological Actions : Immunomodulatory : CK(4048) : AC(2154)

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