Design, structural and functional characterization of a Temporin-1b analog active against Gram-negative bacteria

► A new Temporin B analog, TB_KKG6A, was designed. ► TB_KKG6A is active against Gram-positive and Gram-negative bacteria. ► The peptide strongly interacts with the LPS of E. coli. ► The peptide folds into a kinked helix upon interaction with LPS. ► The peptide shows very low hemolytic activity.