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Open Access Research Article Just Accepted
Polyphenol-rich extract from Sanghuangporous vaninii against acetaminophen-induced liver injury by blocking ferroptosis via NRF2/GPX4 pathway
Food Science and Human Wellness
Available online: 17 July 2024
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Acetaminophen (APAP) used as an antipyretic and analgesic agent can cause acute liver injury (AILI) under overdose. Sanghuangporous vaninii (S. vaninii) is a edible fungus with abundant metabolites exhibits excellent hepatoprotective activities, but the effect for AILI is not yet fully understood. In this study, the polyphenol-rich extract from S. vaninii (PSV) was prepared, with a total phenolic content of 75.72% and 34 compounds. The data of hepatoprotection indicated that PSV obviously alleviated the hepatocellular injury induced by APAP in vivo and in vitro. The protective mechanism of PSV against APAP-induced AILI might be attributed to the activating NRF2/GPX4 pathway. Based on network pharmacology analysis, the active components of PSV such as caffeic acid, osmundacetone and hispolone played a key role in hepatoprotection of PSV. Consequently, this study highlights the protection of PSV on AILI, which provides new insight into bioactivities of S. vaninii.

Open Access Issue
Exploring the taste presentation and receptor perception mechanism of salty peptides from Stropharia rugosoannulata based on molecular dynamics and thermodynamics simulation
Food Science and Human Wellness 2024, 13(4): 2277-2288
Published: 20 May 2024
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The taste presentation and receptor perception mechanism of the salty peptide of Stropharia rugosoannulata were predicted and verified using peptide omics and molecular interaction techniques. The combination of aspartic acid (D) and glutamic acid (E), or peptide fragments composed of arginine (R), constitute the characteristic taste structural basis of salty peptides of S. rugosoannulata. The taste intensity of the salty peptide positively correlates with its concentration within a specific concentration range (0.25–1.0 mg/mL). The receptor more easily recognizes the first amino acid residue at the N-terminal of salty peptides and the aspartic acid residue in the peptides. GLU513, ASP707, and VAL508 are the critical amino acid residues for the receptor to recognize salty peptides. TRPV1 is specifically the receptor for recognizing salty peptides. Hydrogen bonds and electrostatic interactions are the main driving forces for the interactions between salty peptides and TRPV1 receptors. KSWDDFFTR has the most potent binding capacity with the receptor and has tremendous potential for application in sodium salt substitution. This study confirmed the taste receptor that specifically recognizes salty peptides, analyzed the receptor-peptide binding interaction, and provided a new idea for understanding the taste receptor perception of salty peptides.

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