Different molecular sizes and chain conformations of water-soluble yeast β-glucan fractions and their interactions with receptor Dectin-1.

Although β-glucan could bind to Dectin-1 to exert bioactivity, the influence of molecular size and chain conformation of β-glucan on its interaction with Dectin-1 is still unclear. This work investigated the molecular sizes and chain conformations of five water-soluble yeast β-glucan (WYG1-5) fractions as well as their interactions with Dectin-1 by fluorescence spectroscopy and microscale thermophoresis. Results revealed a spherical conformation for higher molecular weight WYG and a stiff chain conformation for smaller molecular weight WYG. The WYG and Dectin-1 interactions were in the order of WYG-2 > WYG-1 > WYG-3 > WYG-4 > WYG-5. The spherical WYG-2 exhibited the largest binding constant of 7.91 × 10 M and the lowest dissociation constant of 22.1 nM to Dectin-1. Additionally, the underlying interaction mechanism showed that it may be easier for spherical WYG with longer side chains to interact with receptor Dectin-1.