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La famille Kunitz/BPTI des venins de serpents: Structure, classification et potentiel pharmacologique

Abstract : Snake venoms are rich sources of serine proteinase inhibitors that are members of the Kunitz/BPTI (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 processes, such as blood coagulation, fibrinolysis, and inflammation. Also, these molecules showed an anti-tumoral potent and anti-metastatic effect. Interestingly, Kunitz/BPTI peptides can have exquisite binding specificities and possess high potency for their targets making them excellent therapeutic candidates.
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https://hal-amu.archives-ouvertes.fr/hal-01481713
Contributor : José Luis <>
Submitted on : Thursday, March 2, 2017 - 6:48:48 PM
Last modification on : Wednesday, October 28, 2020 - 9:52:04 AM
Long-term archiving on: : Wednesday, May 31, 2017 - 4:38:06 PM

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  • HAL Id : hal-01481713, version 1
  • PUBMED : 26402966

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Maram Morjen, Zaineb Abdelkafi-Koubaa, José Luis, Houcemeddine Othman, Najet Srairi-Abid, et al.. La famille Kunitz/BPTI des venins de serpents: Structure, classification et potentiel pharmacologique. Archives de l'Institut Pasteur de Tunis, 2014, 91 (1-4), pp.3-13. ⟨hal-01481713⟩

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