Antimicrobial Peptide-Driven Colloidal Transformations in Liquid-Crystalline Nanocarriers

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 -