@article {Duval_etal2009,
	title = {{KKKKPLFGLFFGLF: A cationic peptide designed to exert antibacterial activity}},
	journal = {Peptides},
	volume = {30},
	number = {9},
	year = {2009},
	pages = {1608{\textendash}1612},
	abstract = {With 14 residues organized as two domains linked by a single proline, the de novo peptide called K4 was designed, using Antimicrobial Peptide Database, to exert antibacterial activity. The N-terminal domain is composed of four lysines enhancing membrane interactions, and the C-terminal domain is putatively folded into a hydrophobic $\alpha$-helix. Following the synthesis, the purification and the structural checking, antibacterial assays revealed a strong activity against gram-positive and gram-negative bacteria including human pathogenic bacteria such as Staphylococcus aureus and some marine bacteria of the genus Vibrio. Scanning electron microscopy of Escherichia coli confirmed that K4 lyses bacterial cells. The cytotoxicity was tested against rabbit erythrocytes and chinese hamster ovary cells (CHO-K1). These tests revealed that K4 is non-toxic to mammalian cells for bacteriolytic concentrations. The peptide K4 could be a valuable candidate for future therapeutic applications.},
	issn = {0196-9781},
	author = {Duval, E and C{\'e}line Zatylny-Gaudin and Laurencin, M and Baudy-Floc{\textquoteright}h, M and Jo{\"e}l Henry}
}
