Plant origin and synthetic derivatives of sulfated polysaccharides. Many biological activities of heparin/HS are attributed to their precise interaction and regulation with numerous heparin-binding cytokines, antithrombin (AT), and extracellular matrix (ECM) biomolecules. Specific domains with distinct saccharide gp130/CD130 Proteins Biological Activity sequences in heparin/HS mediate these interactions are mediated and demand different extremely sulfated saccharide sequences with distinct combinations of sulfated groups. Multivalent and cluster effects from the certain sulfated sequences in heparinoids are also significant factors that manage their interactions and biological activities. This evaluation gives an overview of heparinoid-based biomaterials that provide novel suggests of engineering of different heparin-binding cytokine-delivery systems for biomedical applications and it focuses on our original studies on non-anticoagulant heparin-carrying polystyrene (NAC-HCPS) and polyelectrolyte complex-nano/microparticles (N/MPs), in addition to heparin-coating devices. Keywords and phrases: glycosaminoglycan; heparinoid; heparinoid-based biomaterials; heparin-binding cytokines; heparinoid-carrying polystyrene; polyelectrolyte complexes1. Introduction Heparinoids are generically known as heparin, heparan sulfate (HS), and heparin-like molecules, and they may be involved in different biological processes involving heparin-binding proteins, such as numerous cytokines. Heparinoids are a sub-group of glycosaminoglycans (GAGs) discovered in animal tissues. GAGs consist of other polysaccharides, including hyaluronic acid (HA), chondroitin sulfate (CS), dermatan sulfate, and keratan sulfate, as well as heparinoids, all of which bear adverse charges that vary in density and position [1]. CS is formed by the repetitive unit of CD66c/CEACAM6 Proteins Recombinant Proteins glucuronic acid linked 13 to a -N-acetylgalactosamine. The galactosamine residues could possibly be O-sulfated in the C-4 and/or C-6 position, however they contain no N-sulfated group [1]. These GAGs exhibit little anti-thrombotic activity, which is typically a distinct function of heparin. Alternatively, hexuronate residues in heparin/HS are present as either as -d-glucuronate (GlcA) or the C-5 epimer, -l-iduronate (IdoA). Heparin/HS essentially consist of a disaccharide repeat of (14 linked) -d-glucosamine (GlcN) and hexuronate, in which the GlcN might be either N-acetylated (GlcNAc) or N-sulfated (GlcNS), and the hexuronate residues are present as either GlcA or the C-5 epimer, IdoA. Ester O-sulfations areMolecules 2019, 24, 4630; doi:ten.3390/molecules24244630 www.mdpi.com/journal/moleculesMolecules 2019, 24,2 ofprincipally at the C-2 position of hexuronate (GlcA or IdoA) as well as the C-6 position in the GlcNS [4,5]. GAGs, except HA, are normally present in the kind of proteoglycans (PGs), in which many GAGs are covalently attached to a core protein [1,6,7]. Heparin is commercially made from animal tissues (pig or bovine intestinal mucosa, bovine lung, and so forth.) and it’s clinically applied as an antithrombotic drug. Heparin is confined to mast cells, where it can be stored in cytoplasmic granules in intact tissue [8,9]. In contrast, HS is ubiquitously distributed on cell surfaces and in the extracellular matrix (ECM) [10,11]. Heparin/HS are implicated in cell adhesion, recognition, migration, as well as the regulation of various enzymatic activities, also as their well-known anticoagulant action [115]. Most of the biological functions of heparin/HS rely upon the binding of numerous functional proteins, med.
