Novel antioxidant peptides from MFGM protein Hydrolysates: Separation, identification and effects on Dexamethasone-induced mitochondrial dysfunction. (1st March 2023)
- Record Type:
- Journal Article
- Title:
- Novel antioxidant peptides from MFGM protein Hydrolysates: Separation, identification and effects on Dexamethasone-induced mitochondrial dysfunction. (1st March 2023)
- Main Title:
- Novel antioxidant peptides from MFGM protein Hydrolysates: Separation, identification and effects on Dexamethasone-induced mitochondrial dysfunction
- Authors:
- Li, He
Guan, Kaifang
Liu, Min
Liu, Dandan
Wang, Wenqiong
Zhu, Aihua - Abstract:
- Graphical abstract: Highlights: The MFGM antioxidant peptides were prepared, separated and purified by in vitro digestion and DEAE-52. The novel cellular antioxidant activity peptides TGIIT and YAR were identified from MFGM hydrolysates. TGIIT and YAR exhibited excellent mitochondrial function and cytoprotective effect. TGIIT and YAR alleviate mitochondrial dysfunction via Sirt-1/PGC-1α signaling pathway. Abstract: Milk fat globule membrane (MFGM) protein is a complex milk protein system with antioxidant property, which can alleviate skeletal muscle dysfunction caused by oxidative stress. In this study, peptide products of MFGM protein obtained through in vitro digestion were isolated and purified, and the composition and antioxidant activities of MFGM peptides (MFGMP) were identified and assessed using LC-MS/MS combined with molecular docking and in vitro approach. Three novel antioxidant peptides TGIIT, YAR and YYK were identified from MFGMPF1, among which TGIIT and YAR exhibited excellent antioxidant effects and protected dexamethasone (Dex)-induced L6 cells by enhancing mitochondrial function and biogenesis involving modulating Sirt-1/PGC-1α signaling pathway. Furthermore, YAR and TGIIT also significantly decreased expression of pro-apoptotic factors such as cyt-c, cleaved caspase-3 and caspase-9. Therefore, YAR and TGIIT, two novel antioxidant peptides, are expected to be utilized in functional food or medicine, providing an emerging role of MFGMP in maintainingGraphical abstract: Highlights: The MFGM antioxidant peptides were prepared, separated and purified by in vitro digestion and DEAE-52. The novel cellular antioxidant activity peptides TGIIT and YAR were identified from MFGM hydrolysates. TGIIT and YAR exhibited excellent mitochondrial function and cytoprotective effect. TGIIT and YAR alleviate mitochondrial dysfunction via Sirt-1/PGC-1α signaling pathway. Abstract: Milk fat globule membrane (MFGM) protein is a complex milk protein system with antioxidant property, which can alleviate skeletal muscle dysfunction caused by oxidative stress. In this study, peptide products of MFGM protein obtained through in vitro digestion were isolated and purified, and the composition and antioxidant activities of MFGM peptides (MFGMP) were identified and assessed using LC-MS/MS combined with molecular docking and in vitro approach. Three novel antioxidant peptides TGIIT, YAR and YYK were identified from MFGMPF1, among which TGIIT and YAR exhibited excellent antioxidant effects and protected dexamethasone (Dex)-induced L6 cells by enhancing mitochondrial function and biogenesis involving modulating Sirt-1/PGC-1α signaling pathway. Furthermore, YAR and TGIIT also significantly decreased expression of pro-apoptotic factors such as cyt-c, cleaved caspase-3 and caspase-9. Therefore, YAR and TGIIT, two novel antioxidant peptides, are expected to be utilized in functional food or medicine, providing an emerging role of MFGMP in maintaining anti-oxidant/oxidant status. … (more)
- Is Part Of:
- Food chemistry. Volume 403(2023)
- Journal:
- Food chemistry
- Issue:
- Volume 403(2023)
- Issue Display:
- Volume 403, Issue 2023 (2023)
- Year:
- 2023
- Volume:
- 403
- Issue:
- 2023
- Issue Sort Value:
- 2023-0403-2023-0000
- Page Start:
- Page End:
- Publication Date:
- 2023-03-01
- Subjects:
- MFGM peptide -- Antioxidant activity -- Mitochondrial function -- Molecular docking -- Sirt-1/PGC-1α signaling pathway
Food -- Analysis -- Periodicals
Food -- Composition -- Periodicals
664 - Journal URLs:
- http://www.sciencedirect.com/science/journal/03088146 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.foodchem.2022.134473 ↗
- Languages:
- English
- ISSNs:
- 0308-8146
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3977.284000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 24240.xml