Interaction between a Cationic Surfactant-like Peptide and Lipid Vesicles and Its Relationship to Antimicrobial Activity | Zendy

Ashkan Dehsorkhi | Zendy; Valeria Castelletto | Zendy; Ian W. Hamley | Zendy; Jani Seitsonen | Zendy; Janne Ruokolainen | Zendy

Open Access

Interaction between a Cationic Surfactant-like Peptide and Lipid Vesicles and Its Relationship to Antimicrobial Activity

Author(s) -

Ashkan Dehsorkhi,

Valeria Castelletto,

Ian W. Hamley,

Jani Seitsonen,

Janne Ruokolainen

Publication year - 2013

Publication title -

langmuir

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.042

H-Index - 333

eISSN - 1520-5827

pISSN - 0743-7463

DOI - 10.1021/la403447u

Subject(s) - vesicle , peptide , chemistry , pulmonary surfactant , lipid bilayer , antimicrobial peptides , cationic polymerization , bilayer , membrane , lysis , antimicrobial , biophysics , crystallography , biochemistry , organic chemistry , biology

We investigate the properties of an antimicrobial surfactant-like peptide (Ala)6(Arg), A6R, containing a cationic headgroup. The interaction of this peptide with zwitterionic (DPPC) lipid vesicles is investigated using a range of microscopic, X-ray scattering, spectroscopic, and calorimetric methods. The β-sheet structure adopted by A6R is disrupted in the presence of DPPC. A strong effect on the small-angle X-ray scattering profile is observed: the Bragg peaks from the DPPC bilayers in the vesicle walls are eliminated in the presence of A6R and only bilayer form factor peaks are observed. All of these observations point to the interaction of A6R with DPPC bilayers. These studies provide insight into interactions between a model cationic peptide and vesicles, relevant to understanding the action of antimicrobial peptides on lipid membranes. Notably, peptide A6R exhibits antimicrobial activity without membrane lysis.

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