Novel anti-atrophic peptide isolated from olive flounder surimi as a nutraceutical additive against TNF-α induced muscle atrophy

[Display omitted] •A novel peptide (OFSP) was isolated from olive flounder surimi.•OFSP binds to TNF-α, inhibiting its binding to TNFR1 receptor.•OFSP binds to TNF-α active site and inhibits formation of TNF-α-TNFR1 complex.•OFSP inhibits E2 ubiquitin ligases and NF-κB activation in TNF-α induced my...

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Bibliographic Details
Published in:Journal of functional foods 2023-11, Vol.110, p.105836, Article 105836
Main Authors: Liyanage, N.M., Nagahawatta, D.P., Jayawardena, Thilina.U., Jayawardhana, H.H.A.C.K., Jang, Mi-Soon, Son, Kwang-Tae, Oh, Jae-Young, Jeon, You-Jin
Format: Article
Language:English
Subjects:
Atrophy
Functional food
Myotube
Surimi-peptide
TNF-α
TNFR1 receptor
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Summary:[Display omitted] •A novel peptide (OFSP) was isolated from olive flounder surimi.•OFSP binds to TNF-α, inhibiting its binding to TNFR1 receptor.•OFSP binds to TNF-α active site and inhibits formation of TNF-α-TNFR1 complex.•OFSP inhibits E2 ubiquitin ligases and NF-κB activation in TNF-α induced myotube.•OFSP protects muscle cells from TNF-α induced muscle atrophy. Skeletal muscle atrophy has significant negative functional effects, especially on patients with inflammatory diseases. Tumor necrosis factor alpha (TNF-α) plays a crucial role in muscle pathology associated with muscle wasting and impairment of differentiation. The present study evaluated the anti-atrophic activity and related mechanism of a novel peptide (Tryptophan-Tyrosine-Lysine) derived from Olive Flounder surimi (OFSP), against TNF-α induced muscle atrophy in C2C12 myotubes. Molecular docking results showed that OFSP binds to TNF-α, inhibiting its binding to TNFR1 receptor. OFSP treatment increased the cell viability and decreased intracellular reactive oxygen species production caused by TNF-α. OFSP markedly downregulated the NF- κB pathway proteins phosphorylation, thereby inhibiting pathway activation. Furthermore, OFSP suppressed IL-6 production and expression of E2 ubiquitin ligases, atrogin-1/MAFbx and MuRF1, while increasing myogenic marker expressions. Current findings indicate that OFSP exhibits excellent anti-atrophic activity against inflammation-induced muscle atrophy, and these characteristics may be valuable in anti-atrophic functional food development.
ISSN:1756-4646
2214-9414
DOI:10.1016/j.jff.2023.105836