TLR 2/1 interaction of pectin depends on its chemical structure and conformation

Éva Jermendi, Cynthia Fernández-Lainez, Martin Beukema, Gabriel López-Velázquez, Marco A. van den Berg, Paul de Vos, Henk A. Schols*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

6 Citations (Scopus)

Abstract

Citrus pectins have demonstrated health benefits through direct interaction with Toll-like receptor 2. Methyl-ester distribution patterns over the homogalacturonan were found to contribute to such immunomodulatory activity, therefore molecular interactions with TLR2 were studied. Molecular-docking analysis was performed using four GalA-heptamers, GalA7Me0, GalA7Me1,6, GalA7Me1,7 and GalA7Me2,5. The molecular relations were measured in various possible conformations. Furthermore, commercial citrus pectins were characterized by enzymatic fingerprinting using polygalacturonase and pectin-lyase to determine their methyl-ester distribution patterns. The response of 12 structurally different pectic polymers on TLR2 binding and the molecular docking with four pectic oligomers clearly demonstrated interactions with human-TLR2 in a structure-dependent way, where blocks of (non)methyl-esterified GalA were shown to inhibit TLR2/1 dimerization. Our results may be used to understand the immunomodulatory effects of certain pectins via TLR2. Knowledge of how pectins with certain methyl-ester distribution patterns bind to TLRs may lead to tailored pectins to prevent inflammation.

Original languageEnglish
Article number120444
JournalCarbohydrate Polymers
Volume303
DOIs
Publication statusPublished - 1 Mar 2023

Keywords

  • Citrus pectin
  • HILIC-MS
  • HPAEC
  • Immunomodulation
  • Methyl-ester distribution
  • Toll-like receptors

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