Abstract
In this thesis,we are going to investigate the interaction of the heparinderived disaccharide with the cardiotoxin V (CTX A5). Cardiotoxinswill envenom the target cells and might cause severe necrosis and inflammation,and glycosaminoglycan serve as potential target within the process. The distinct loop regions of CTX A5 differs by two inserts and mutations on the loop I and II make it exhibit much higher affinity to glycosaminoglycans and lipids than other cardiotoxin homologues. From our result of auto-docking and the preliminary x-ray structure suggest the binding of heparin derived disaccharide to CTX A5 is through loop II region and induces protein local conformation change. Compared with the former complex structure CTX A3, CTX A5 complex shows a novel binding site which is consist with the long-chain heparin SPR data. And the binding specificities is proven to depend on the sulfation motif of the disaccharide, thus suggest recognition of CTX A5 to glycosaminoglycans.