A revised structure for fucoidan may explain some of its biological activities

Fucoidan from Fucus vesiculosus inhibits human sperm-zona pellucida binding and blocks the zona pellucida-induced acrosome reaction in human sperm. Fucoidan also potently inhibits selectin-mediated adhesion of leukocytes to vascular endothelium. To understand the molecular basis for fucoidan's inhibition of specific cell adhesion events, we have investigated the structure of this fucan using definitive methods of carbohydrate structural analysis. We report the revised average structure for fucoidan. [formula: see text] This average structure differs from the previous model for fucoidan in two respects. First, the core region of the fucan is composed primarily of a polymer of alpha 1-3-linked fucose with sulfate groups substituted at the 4 position on some of the fucose residues. Secondly, fucose is also attached to this polymer to form branch points, one for every 2-3 fucose residues within the chain. This revised average structure is consistent with previous studies suggesting a branched random coil as the best model for this polysaccharide. The proposed model is also a closer structural analogue of the sulfated carbohydrate ligands that bind to selectins. This information should be useful for determining whether a relationship exists between selectin-mediated adhesion of leukocytes and human sperm-egg binding.