“…Indeed, studies of the molecular mechanisms for the inhibition of PLA 2 -like toxins with different molecules have confirmed the proposal of myotoxic sites. It has been observed that these molecules inhibit PLA 2 -like proteins in different ways, including: (i) binding to Helix-I/MDiS region, physically blocking access to the hydrophobic channel (e.g., rosmarinic 48 , 50 , chicoric 30 , and aristolochic acids 4 ); (ii) binding to the MDoS (e.g., caffeic acid 4 and suramin 20 ); (iii) binding in the hydrophobic channel (e.g., caftaric acid 42 , p-bromophenacyl bromide (BPB) 9 ; Varespladib 51 and zinc ions 26 ); (iv) binding to the MDiS (e.g., aristolochic 4 , chicoric acid 30 , zinc ions 26 , suramin 19 , 20 and Varespladib 51 ); or (v) induction of the toxin’s oligomerization (e.g., suramin 19 ). Although the binding regions of the inhibitors are well described, the structural importance of an allosteric activator is only related to the dimer reorientation 14 , 26 .…”