1. High hydrostatic pressure reduces inflammation induced by litchi thaumatin-like protein via altering active domain.
- Author
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Li Y, Li C, Pan F, Wang K, Weng S, Zhao M, Li Q, Wang D, Zhao L, Liu X, and Hu Z
- Subjects
- Animals, Mice, Molecular Dynamics Simulation, Fruit chemistry, Fruit immunology, RAW 264.7 Cells, Protein Domains, Humans, Hydrostatic Pressure, Plant Proteins chemistry, Plant Proteins immunology, Litchi chemistry, Inflammation immunology
- Abstract
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., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper. The following are the supplementary data related to this article. Supplementary data to this article can be found online at https://doi.org/10.1016/j.foodchem.2024.140858., (Copyright © 2024 Elsevier Ltd. All rights reserved.)
- Published
- 2024
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