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Aggregation and membrane permeabilizing properties of designed histidine‐containing cationic linear peptide antibiotics
Author(s) -
Marquette Arnaud,
Mason A. James,
Bechinger Burkhard
Publication year - 2008
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.966
Subject(s) - popc , chemistry , amphiphile , peptide , vesicle , bilayer , membrane , calcein , cationic polymerization , biophysics , viologen , monomer , supramolecular chemistry , liposome , combinatorial chemistry , lipid bilayer , micelle , sonication , aqueous solution , stereochemistry , organic chemistry , biochemistry , chromatography , copolymer , molecule , polymer , biology
Members of the LAH4 family of cationic linear peptide antibiotics have been designed to form amphipathic helical structures in membrane environments and switch from alignments parallel to the bilayer surface to transmembrane orientations in a pH‐dependent manner. Here the aggregation in aqueous buffer of two members of the family has been investigated by DLS. The peptides form monomers or small oligomers at pH = 5 but associate into nano‐sized aggregates at physiological pH. The diameter of these latter complexes can be considerably reduced by sonication. Furthermore, the membrane interactions of the various supramolecular aggregates with POPC or mixed POPC/POPS vesicles have been investigated in calcein‐release assays. In all the cases tested, the large preformed oligomeric peptide aggregates of 20–40 nm in size were more active than the structures with the smallest hydrodynamic radii in releasing the fluorescent dye from LUV. In contrast, the relative activity after sonication depends on the specific environment tested. The data suggest that these amphiphiles form micellar structures and support the notion that they can act in a manner comparable to detergents. Copyright © 2007 European Peptide Society and John Wiley & Sons, Ltd.