Magainin 2 and PGLa in bacterial membrane mimics IV: Membrane curvature and partitioning

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F22%3A00127107" target="_blank" >RIV/00216224:14740/22:00127107 - isvavai.cz</a>

Result on the web

<a href="https://www.sciencedirect.com/science/article/pii/S0006349522008566#" target="_blank" >https://www.sciencedirect.com/science/article/pii/S0006349522008566#</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.bpj.2022.10.018" target="_blank" >10.1016/j.bpj.2022.10.018</a>

Result language

angličtina

Original language name

Magainin 2 and PGLa in bacterial membrane mimics IV: Membrane curvature and partitioning

Original language description

We previously reported that the synergistically enhanced antimicrobial activity of magainin 2 (MG2a) and PGLa is related to membrane adhesion and fusion. Here, we demonstrate that equimolar mixtures of MG2a and L18W-PGLa induce positive monolayer curvature stress and sense, at the same time, positive mean and Gaussian bilayer curvatures already at low amounts of bound peptide. The combination of both abilities—membrane curvature sensing and inducing—is most likely the base for the synergistically enhanced peptide activity. In addition, our coarse-grained simulations suggest that fusion stalks are promoted by decreasing the free-energy barrier for their formation rather than by stabilizing their shape. We also interrogated peptide partitioning as a function of lipid and peptide concentration using tryptophan fluorescence spectroscopy and peptide-induced leakage of dyes from lipid vesicles. In agreement with a previous report, we find increased membrane partitioning of L18W-PGLa in the presence of MG2a. However, this effect does not prevail to lipid concentrations higher than 1 mM, above which all peptides associate with the lipid bilayers. This implies that synergistic effects of MG2a and L18W-PGLa in previously reported experiments with lipid concentrations &gt;1 mM are due to peptide-induced membrane remodeling and not their specific membrane partitioning. Significance

Czech name

—

Czech description

—

Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

—

OECD FORD branch

10610 - Biophysics

Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year

2022

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

BIOPHYSICAL JOURNAL

ISSN

0006-3495

e-ISSN

1542-0086

Volume of the periodical

121

Issue of the periodical within the volume

23

Country of publishing house

GB - UNITED KINGDOM

Number of pages

13

Pages from-to

4689-4701

UT code for WoS article

000901491100004

EID of the result in the Scopus database

2-s2.0-85141523285