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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

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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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