Both aromatic and cationic residues contribute to the membrane-lytic and bactericidal activity of eosinophil cationic protein

摘要: Eosinophil cationic protein (ECP) and eosinophil derived neurotoxin (EDN) are proteins of the ribonuclease A (RNase A) superfamily that have developed biological properties related to function eosinophils. ECP is a potent cytotoxic molecule, although mechanism still unknown this activity has been associated with its highly character. Using liposome vesicles as model, we demonstrated tends disrupt preferentially acidic membranes. On basis structure analysis, variants modified at basic hydrophobic residues constructed. Changes in leakage by these indicated role both aromatic specific amino acids cellular membrane disruption. This case two tryptophans positions 10 35, but not phenylalanine 76, arginines 101 104. The bactericidal native point-mutated variants, tested against Escherichia coli Staphyloc...