Unravelling structure-function interactions between fluorinated heparan sulfate mimetics and signaling proteins.

ABSTRACT: Fluorinated carbohydrates are emerging scaffolds in glycobiology, enabling the elucidation of the roles of the individual hydroxyl groups of a carbohydrate in protein binding and drug discovery. Herein, we report a divergent strategy to synthesize seven heparan sulfate (HS) mimetics featuring a fluorine atom at the C3 position of the glucuronic acid residue, with the objective of modulating structure-function relationships. The sensitivity of fluorine signals to sulfation patterns was confirmed via ¹⁹F-NMR spectroscopy, while ³ J _HH coupling and NOE data demonstrated that the glucuronic acid residue retained its ⁴C₁ conformation. Glycan microarray analysis and SPR binding studies revealed that a single hydroxyl-to-fluorin

SUBMITTER: Mahida V 

PROVIDER: S-EPMC12311619 | biostudies-literature | 2025 Jul

REPOSITORIES: biostudies-literature