Introduction: Bacterial resistance is a worldwide public health problem, requiring new therapeutic options. An alternative approach to this problem is the use of animal toxins isolated from snake venom, such as phospholipases A (PLA), which have important antimicrobial activities. is one of the snake species in the northeast of Brazil that attracts great medical-scientific interest. Here, we aimed to purify and characterize a PLA from , searching for heterologous activities against bacterial biofilms.
Methods: Venom extraction and quantification were followed by reverse-phase high-performance liquid chromatography (RP-HPLC) in C18 column, matrix-assisted ionization time-of-flight (MALDI-ToF) mass spectrometry, and sequencing by Edman degradation. All experiments were monitored by specific activity using a 4-nitro-3-(octanoyloxy) benzoic acid (4NOBA) substrate. In addition, hemolytic tests and antibacterial tests including action against , and were carried out. Moreover, tests of antibiofilm action against were also performed.
Results: PLA, after one purification step, presented 31 -terminal amino acid residues and a molecular weight of 13.6564 Da, with enzymatic activity confirmed in 0.06 µM concentration. Antibacterial activity against (IC = 30.2 µM) and antibiofilm activity against (IC = 1.1 µM) were observed.
Conclusions: This is the first time that PLA purified from venom has appeared as an alternative candidate in studies of new antibacterial medicines.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7551604 | PMC |
| http://dx.doi.org/10.3390/toxins12090606 | DOI Listing |
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