High hydrostatic pressure reduces inflammation induced by litchi thaumatin-like protein via altering active domain

• Published in: Food chemistry 2024-12, Vol.461, p.140858, Article 140858
• Main Authors: Li, Yun, Li, Chuyuan, Pan, Fei, Wang, Kai, Weng, Shaoquan, Zhao, Min, Li, Qian, Wang, Dongwei, Zhao, Lei, Liu, Xuwei, Hu, Zhuoyan
• Format: Article
• Language: English
• Subjects: Animals; Computational modelling; Fruit - chemistry; Fruit - immunology; High hydrostatic pressure; Humans; Hydrostatic Pressure; Inflammation; Inflammation - immunology; Litchi - chemistry; Litchi thaumatin-like proteins; Mice; Molecular Dynamics Simulation; Plant Proteins - chemistry; Plant Proteins - immunology; Protein Domains; RAW 264.7 Cells; Structural characterization
• ISSN: 0308-8146; 1873-7072; 1873-7072
• DOI: 10.1016/j.foodchem.2024.140858

Thaumatin-like proteins (TLP), existing in various fruits, have allergenic and pro-inflammatory activities. The current research attempts to reduce the pro-inflammatory activity of litchi TLP (LcTLP) through high hydrostatic pressure (HHP). This study demonstrated that HHP (250–500 MPa, 5–10 min) was a potential technique to reduce the pro-inflammatory activity of LcTLP, which was attributed to the irreversible destruction of the active domain, ie., V-cleft. SDS-PAGE showed no change in the protein profile. Continuous HHP treatment promoted LcTLP unfolding and then reassembling (400 MPa was the transition pressure), and the content of β-sheets decreased from 35.4% to 31.1%. HHP treatment could mitigate inflammatory responses of LcTLP, as confirmed by ELISA and western blot. Molecular dynamics simulations showed significant changes in the residue network under HHP, thereby affecting the V-cleft. These findings provide a theoretical explanation and structural insights into the HHP-induced reduction of pro-inflammatory activity of LcTLP. [Display omitted] •HHP could mitigate inflammatory responses of LcTLP.•HHP led to a decrease in β-sheet with increasing pressure and treatment time.•Tertiary structure exhibited unfolding and then reassembling.•HHP altered the residue network, and 400 MPa was a transitional pressure point.•HHP affected V-cleft between domains I and II, i.e., the inflammatory active domain.