作者: Cibele Nicolaski Pedron , Iris Araújo , Pedro Ismael da Silva Junior , Fernanda Dias da Silva , Marcelo Der Torossian Torres
DOI: 10.1016/J.BIOORG.2019.103038
关键词: Biochemistry 、 Proline 、 Glycine 、 Antimicrobial 、 Proteases 、 Chemistry 、 Venom 、 Peptide 、 Bacteria 、 Structure–activity relationship
摘要: Abstract VmCT1 is a cationic antimicrobial peptide (AMP) from the venom of scorpion Vaejovis mexicanus. and analogs were designed with single substitutions for verifying influence changes in physicochemical features described as important AMPs hemolytic activities, well their effect on resistance against proteases action. The increase net positive charge by introduction an arginine residue positions hydrophilic face helical structure affected directly activity. Arg-substituted presented activity Gram-negative bacteria ESKAPE list pathogens that not observed VmCT1. Additionally, peptides higher increased values ranging 0.39 to 12.5 μmol L−1 Gram-positive fungi. phenylalanine substitution glycine (position 1), valine proline 8) led lower (at concentrations 50 100 μmol L−1, respectively). These results revealed it possible modulate biological activities derivatives designing substituted-analogs prospective therapeutics