Novel role of homogalacturonan region of pectin in disrupting the interaction between fibronectin and integrin β1

Pectin interacts with fibronectin (FN), a modular protein in the extracellular matrix. This interaction is significant as FN plays a pivotal role by binding to the receptor integrin α5β1. However, the molecular mechanism underlying the pectin-FN interaction and its impact on integrin binding remains unknown. In this study, water-soluble pectins (WSPs) were extracted from three different pectin sources and subsequently characterized. These included Citrus WSP, which primarily comprises the homogalacturonan region, and Kaki and Yuzu WSPs, both of which are rich in rhamnogalacturonan regions. We investigated the molecular interactions between these WSPs and two FN fragments, Anastellin and RetroNectin, using surface plasmon resonance analysis. Citrus WSP exhibited a notable binding affinity to FN, with a dissociation constant (KD) of approximately 10