Antimicrobial Peptide-Driven Colloidal Transformations in Liquid-Crystalline Nanocarriers
Research output: Contribution to journal › Journal article › Research › peer-review
Designing efficient colloidal systems for the delivery of membrane active antimicrobial peptides requires in-depth understanding of their structural and morphological characteristics. Using dispersions of inverted type bicontinuous cubic phase (cubosomes), we examine the effect of integrating the amphiphilic peptide LL-37 at different concentrations on the self-assembled structure and evaluate its bactericidal ability against Escherichia coli. Small-angle X-ray scattering, dynamic light scattering, and cryogenic transmission electron microscopy show that LL-37 integrates into the bicontinuous cubic structure, inducing colloidal transformations to sponge and lamellar phases and micelles in a concentration-dependent manner. These investigations, together with in vitro evaluation studies using a clinically relevant bacterial strain, established the composition-nanostructure-activity relationship that can guide the design of new nanocarriers for antimicrobial peptides and may provide essential knowledge on the mechanisms underlying the bacterial membrane disruption with peptide-loaded nanostructures.
Original language | English |
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Journal | Journal of Physical Chemistry Letters |
Volume | 7 |
Issue number | 17 |
Pages (from-to) | 3482-3486 |
Number of pages | 5 |
ISSN | 1948-7185 |
DOIs | |
Publication status | Published - 24 Aug 2016 |
ID: 165000607