Snake venom Kunitz/BPTi family: Structure, classification and pharmacological potential
Morjen, M.; Abdelkafi-Koubaa, Z.; Luis, J.; Othman, H.; Srairi-Abid, N.; El Ayeb, M.; Marrakchi, N.
Archives de l'Institut Pasteur de Tunis 91(1-4): 3-13
2014
ISSN/ISBN: 0020-2509 PMID: 26402966 Document Number: 673757
Snake venoms are rich sources of serine proteinase inhibitors that are members of the KunitzBPTI (bovine pancreatic trypsin inhibitor) family. Generally, these inhibitors are formed by 60 amino acids approximately. Their folding is characterised by a canonical loop that binds in a complementary manner to the active site of serine protease. Some variants from snake venoms show only weak inhibitory activity against proteases while others are neurotoxic. Moreover, proteases inhibitors are involved in various physiological prdcesses, such as blood coagulation, fibrinolysis, and inflammation. Also, these molecules showed an anti-tumoralpotent and anti-metastatic effect. Interestingly, KunitzBPTI peptides can have exquisite binding specificities and possess high potency for their targets making them excellent therapeutic candidates.