TY - JOUR
T1 - Antimicrobial Peptide-Driven Colloidal Transformations in Liquid-Crystalline Nanocarriers
AU - Gontsarik, Mark
AU - Buhmann, Matthias T
AU - Yaghmur, Anan
AU - Ren, Qun
AU - Maniura-Weber, Katharina
AU - Salentinig, Stefan
PY - 2016/9/1
Y1 - 2016/9/1
N2 - 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.
AB - 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.
U2 - 10.1021/acs.jpclett.6b01622
DO - 10.1021/acs.jpclett.6b01622
M3 - Journal article
C2 - 27541048
SN - 1948-7185
VL - 7
SP - 3482
EP - 3486
JO - Journal of Physical Chemistry Letters
JF - Journal of Physical Chemistry Letters
IS - 17
ER -