Peptide-Loaded Cubosomes Functioning as an Antimicrobial Unit against Escherichia coli
Journal article, 2019

Dispersions of cubic liquid crystalline phases, also known as cubosomes, have shown great promise as delivery vehicles for a wide range of medicines. Due to their ordered structure, comprising alternating hydrophilic and hydrophobic domains, cubosomes possess unique delivery properties and compatibility with both water-soluble and -insoluble drugs. However, the drug delivery mechanism and cubosome interaction with human cells and bacteria are still poorly understood. Herein, we reveal how cubosomes loaded with the human cathelicidin antimicrobial peptide LL-37, a system with high bacteria-killing effect, interact with the bacterial membrane and provide new insights into the eradication mechanism. Combining the advanced experimental techniques neutron reflectivity and quartz crystal microbalance with dissipation monitoring, a mechanistic drug delivery model for LL-37-loaded cubosomes on bacterial mimicking bilayers was constructed. Moreover, the cubosome interaction with Escherichia coli was directly visualized using super-resolution laser scanning microscopy and cryogenic electron tomography. We could conclude that cubosomes loaded with LL-37 adsorbed and distorted bacterial membranes, providing evidence that the peptide-loaded cubosomes function as an antimicrobial unit.




antimicrobial peptide



Lukas Boge

Chalmers, Chemistry and Chemical Engineering, Applied Chemistry

RISE Research Institutes of Sweden

Kathryn L. Browning

University of Copenhagen

Randi Nordström

Uppsala University

Mario Campana

STFC Rutherford Appleton Laboratory

Liv S.E. Damgaard

University of Copenhagen

Josefin Seth Caous

RISE Research Institutes of Sweden

Maja S. Hellsing

RISE Research Institutes of Sweden

Lovisa Ringstad

RISE Research Institutes of Sweden

Martin Andersson

Chalmers, Chemistry and Chemical Engineering, Applied Chemistry

ACS Applied Materials & Interfaces

1944-8244 (ISSN) 1944-8252 (eISSN)

Vol. 11 24 21314-21322

Subject Categories

Pharmaceutical Sciences

Physical Chemistry

Structural Biology



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