Abstract
Bioaffinity capturing of molecules allows the discovery of bioactive compounds and decreases the need for various stages in the natural compound isolation process. Despite the high selectivity of this technique, the screening and identification methodology depends on the presence of a protein to capture potential ligands. However, some proteins, such as snake secretory phospholipase A2 (sPLA2), have never been investigated using this approach. The purpose of this study was to evaluate the use of a new method for screening natural compounds using a bioaffinity-guided ultrafiltration method on Crotalus durissus terrificus sPLA2 followed by HPLC-MS to identify the compounds, and this method could be used to discover new anti-inflammatory compounds from the various organisms originating from biodiversity. Different extracts were selected to evaluate their ability to inhibit sPLA2 activity. The extracts were incubated with sPLA2 and the resulting mixture was ultrafiltrated to elute unbound components. The resulting compounds were identified by HPLC-MS. We identified hispidulin as one of the components present in the Moquiniastrum floribundum leaf and evaluated the ability of this isolated compound to neutralize the inflammatory activity of sPLA2 from Crotalus durissus terrificus.
Highlights
Secretory A2 phospholipases from snake venom in species such as Crotalus durissus terrificus (Cdt) have structural and functional similarity to most human secretory phospholipase A2 (sPLA2), and both have common enzymatic functions and properties [1]
The results strongly suggest that these extracts should have a potential anti-inflammatory compound interacting with sPLA2
Hispidulin showed promising activity against acute inflammation induced by sPLA2 and its identification was possible using a new method bioguided by molecular and functional bioaffinity against sPLA2 from Crotalus durissus terrificus to identify some potential secondary plant metabolites in various extracts
Summary
Secretory A2 phospholipases (sPLA2) from snake venom in species such as Crotalus durissus terrificus (Cdt) have structural and functional similarity to most human sPLA2, and both have common enzymatic functions and properties [1] These sPLA2 enzymes have been used as research tools both in silico and experimentally in the search for new anti-inflammatory compounds. SPLA2 is a pro-inflammatory protein involved in the mobilization of arachidonic acid (AA) through the indirect activation of cytosolic phospholipase A2 (cPLA2) and phospholipase C (PLC) These enzymes lead to cyclooxygenase 2 (COX-2) activation, which is responsible for AA metabolism, releasing. In addition to AA, another important product for sPLA2-induced pharmacological activities is lysophospholipids, which are involved in the inflammatory process [2,3] Both mediators induce an increase in the cytosolic expression of COX-2 and the consequent increase in prostaglandin synthesis [4,5]. SPLA2 is able to induce inflammation through its ability to generate AA, initiating a series of cellular events and inducing an increase in reactive oxygen species (ROS)
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