IntroductionThe growth-inhibiting effect of the peptide Uy234, present in the venom of the scorpion Urodacus yaschenkoi, has been investigated in two bacterial pathogens: Staphylococcus aureus ATCC 25923 and Acinetobacter baumannii AE12, the latter being a multidrug-resistant clinical isolate. With the aim of determining the possible role of specific residues in the bioactivity of this peptide, we studied a proline residue at position 9 and the C-terminal amidation of this peptide.MethodsTwo ina
Structural determinants of the scorpion venom peptide Uy234 govern bactericidal activity and membrane-disruptive properties
Verónica Quintero-Hernández
