Structure-function relationship of anticoagulant and antithrombotic well-defined sulfated polysaccharides from marine invertebrates.

Marine sulfated polysaccharides (MSPs), such as sulfated fucans (SFs), sulfated galactans (SGs), and glycosaminoglycans (GAGs) isolated from invertebrate animals, are highly anionic polysaccharides capable of interacting with certain cationic proteins, such as (co)-factors of the coagulation cascade during clotting-inhibition process. Primarily, these molecular complexes between MSPs and coagulation-related proteins seem to be driven mostly by electrostatic interactions. However, through a systematic comparison using several novel well-defined sulfated polysaccharides composed of repetitive oligosaccharides with clear sulfation patterns, it was proved that those molecular interactions are essentially regulated by the stereochemistry of the glycans (which depends on a conjunction of anomeric configurations, sugar types, conformational preferences, glycosylation, and sulfation sites), rather than just a mere consequence of the electronegative density charges (mainly from number of sulfate groups). Here, we present an overview about the structure-function relationship of the invertebrate MSPs with regular structures as potential anticoagulant and antithrombotic agents, as pathologies related to the cardiovascular system are one of the major causes of mortality in the world. Copyright Â