Peptides short amino acid chains or epitopes or blocking antagonists. The shortest peptides are dipeptides, consisting of 2 amino acids joined by a single peptide bond, followed by tripeptides, tetra peptides, ... till polypeptides that are long, continuous, and unbranched synthetic peptide chains. These biological oligomers and polymers can be Solid-phase peptide synthesis (SPPS), or in continue produced for custom peptide synthesis projects. The High-efficiency solid phase peptide synthesis (HE-SPPS) is give very low production costs.
Thrombin is the final protease in the blood coagulation cascade and serves both pro- and anticoagulant functions through the cleavage of several targets. The ability of thrombin to specifically recognize a wide range of substrates derives from interactions which occur outside of the active site of thrombin. Thrombin possesses two anion binding exosites which mediate many of its interactions with cofactors and substrates, and although many structures of thrombin have been solved, few such interactions have been described in molecular detail. Glycosaminoglycan binding to exosite II of thrombin plays a major role in switching off the procoagulant functions of thrombin by mediating its irreversible inhibition by circulating serpins and by its binding to the endothelial cell surface receptor thrombomodulin.