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This research investigates how the structure of proanthocyanidins affects their interaction with LcTLP and their anti-inflammatory effects.

May 15, 2026Journal of Agricultural and Food Chemistry0 citations

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Vital Roles of A-Type Linkage and Polymerization Degree in Governing Proanthocyanidin Interaction and Anti-inflammatory Action on Litchi Thaumatin-Like Protein

YLYJ LiSouth China Agricultural University CUChibuike C. UdenigweUniversity of Ottawa CBCarine Le BourvellecUniversité d'Avignon et des Pays de Vaucluse

Key Points

This research investigates how the structure of proanthocyanidins affects their interaction with LcTLP and their anti-inflammatory effects.
Thermodynamic analysis of proanthocyanidin and LcTLP interactions
Assessment of inflammatory marker secretion (NO, TNF-α, IL-6) in RAW264.7 cells after co-treatment with proanthocyanidins
Identification of binding sites on LcTLP for oligomeric proanthocyanidins
Proanthocyanidins effectively suppressed NO, TNF-α, and IL-6 secretion in RAW264.7 cells.
Key residues GLU84 and TYR85 on LcTLP were identified as binding sites for proanthocyanidins.
Hydrogen bonding was confirmed as a dominant interaction mechanism, suggesting a significant role in anti-inflammatory action.

Abstract

a = 283.7 L/mol) with LcTLP. Thermodynamic parameters indicated hydrogen bonding as dominant, reflecting an enthalpy-driven process. In RAW264.7 cells, PAPC more effectively suppressed LcTLP-induced NO, TNF-α, and IL-6 secretion by coating LcTLP surface. However, oligomeric proanthocyanidins occupied LcTLP active site by binding to the key residues, including GLU84 and TYR85.

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Vital Roles of A-Type Linkage and Polymerization Degree in Governing Proanthocyanidin Interaction and Anti-inflammatory Action on Litchi Thaumatin-Like Protein

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Abstract

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