The scorpion Tityus serrulatus is considered the most dangerous species of Brazil due to the high number of accidents presenting severe manifestations of envenoming. The scorpion venom is a complex mixture of molecules, most of which are peptides that have different biological activities, among them, neurotoxic effects with actions on ion channels. Toxins from T. serrulatus venom have been extensively studied with respect to their structural and functional characteristics to better understanding the context of envenoming and to obtain new molecules with therapeutic potential. Considering the relevance of the actions of this venom, this work aims the purification of new components present in fraction I obtained from chromatography of the venom in the cation exchange column. The fraction I was not been well characterized, justifying its choice for these studies. Preliminary tests show that it has components of various molecular masses and probably quite distinct activities, such enzymatic activity. The isolation of these components will be performed by fast protein liquid chromatography (FPLC) on reverse phase or other chromatographic procedures if necessary. For structural characterization of new molecules will be employed methods such as mass spectrometry, amino-terminal sequencing, polyacrylamide gel electrophoresis and in silico analysis. We aim to characterize the components isolated from fraction I using assays to identify enzymes (protease, phospholipase, L-amino acid oxidase, hyaluronidase) or enzyme inhibitors (bradykinin potentiating peptides, protease inhibitors) with biotechnological interest. The choice of tests for functional assessment will be made based on sequence homology with proteins deposited in databases.
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