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TLR 2/1 interaction of pectin depends on its chemical structure and conformation
- Source :
- ISSN: 0144-8617
- Publication Year :
- 2023
-
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.
Details
- Database :
- OAIster
- Journal :
- ISSN: 0144-8617
- Notes :
- application/pdf, Carbohydrate Polymers 303 (2023), ISSN: 0144-8617, ISSN: 0144-8617, English
- Publication Type :
- Electronic Resource
- Accession number :
- edsoai.on1356879134
- Document Type :
- Electronic Resource