184776-51-0

LAH4 is an antimicrobial peptide that strongly interacts with phospholipid membranes, exhibiting in vitro transfection efficiency.

LAH4 exhibits potent antimicrobial, nucleic acid transfection and cell penetration activities[1]. LAH4 mediates the transport of functional β-galactosidase, a large tetrameric protein of about 0.5 MDa, into the cell interior[2]. At acidic pH, LAH4 has exhibited a high tendency to interact strongly with and be adsorbed on anionic membrane[3].

LAH4, an alpha-helix of the designed amphipathic peptide antibiotic, exhibits potent antimicrobial, nucleic acid transfection and cell penetration activities. LAH4 possesses high plasmid DNA delivery capacities. LAH4 has a strong affinity for anionic lipids found in the outer membrane of bacterial membranes[1][2][3].

[1]. Perrone B, et al. Lipid interactions of LAH4, a peptide with antimicrobial and nucleic acid transfection activities. Eur Biophys J. 2014 Nov;43(10-11):499-507. [2]. Moulay G, et al. Histidine-rich designer peptides of the LAH4 family promote cell delivery of a multitude of cargo. J Pept Sci. 2017 Apr;23(4):320-328. [3]. Islami M, et al. Study of orientation and penetration of LAH4 into lipid bilayer membranes: pH and composition dependence. Chem Biol Drug Des. 2014 Aug;84(2):242-52.