Magainin 2 and PGLa in Bacterial Membrane Mimics III: Membrane Fusion and Disruption.

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F22%3A00125525" target="_blank" >RIV/00216224:14740/22:00125525 - isvavai.cz</a>

Result on the web

<a href="https://www.sciencedirect.com/science/article/pii/S000634952103959X?via%3Dihub" target="_blank" >https://www.sciencedirect.com/science/article/pii/S000634952103959X?via%3Dihub</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.bpj.2021.12.035" target="_blank" >10.1016/j.bpj.2021.12.035</a>

Result language

angličtina

Original language name

Magainin 2 and PGLa in Bacterial Membrane Mimics III: Membrane Fusion and Disruption.

Original language description

We previously speculated that the synergistically enhanced antimicrobial activity of Magainin 2 and PGLa is related to membrane adhesion, fusion, and further membrane remodeling. Here we combined computer simulations with time-resolved in vitro fluorescence microscopy, cryoelectron microscopy, and small-angle X-ray scattering to interrogate such morphological and topological changes of vesicles at nanoscopic and microscopic length scales in real time. Coarse grained simulations revealed formation of an elongated and bent fusion zone between vesicles in the presence of equimolar peptide mixtures. Vesicle adhesion and fusion were observed to occur within a few seconds by cryoelectron microscopy and corroborated by small-angle X-ray scattering measurements. The latter experiments indicated continued and time-extended structural remodeling for individual peptides or chemically linked peptide heterodimers but with different kinetics. Fluorescence microscopy further captured peptide-dependent adhesion, fusion, and occasional bursting of giant unilamellar vesicles a few seconds after peptide addition. The synergistic interactions between the peptides shorten the time response of vesicles and enhance membrane fusogenic and disruption properties of the equimolar mixture compared with the individual peptides.

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

—

Volume of the periodical

121

Issue of the periodical within the volume

5

Country of publishing house

GB - UNITED KINGDOM

Number of pages

10

Pages from-to

852-861

UT code for WoS article

000765012800016

EID of the result in the Scopus database

2-s2.0-85125440007