J 2022

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

KABELKA, Ivo, Vasil GEORGIEV, Lisa MARX, Peter PAJTINKA, Karl LOHNER et. al.

Basic information

Original name

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

Authors

KABELKA, Ivo (203 Czech Republic, belonging to the institution), Vasil GEORGIEV, Lisa MARX, Peter PAJTINKA (703 Slovakia, belonging to the institution), Karl LOHNER, Georg PABST, Rumiana DIMOVA and Robert VÁCHA (203 Czech Republic, guarantor, belonging to the institution)

Edition

Biophysical Journal, New York, USA, Cell Press, 2022, 0006-3495

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10610 Biophysics

Country of publisher

United Kingdom of Great Britain and Northern Ireland

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

Impact factor

Impact factor: 3.400

RIV identification code

RIV/00216224:14740/22:00125525

Organization unit

Central European Institute of Technology

UT WoS

000765012800016

Keywords in English

Cell Membrane; Cryoelectron Microscopy; Lipid Bilayers; Magainins; Membrane Fusion

Tags

Tags

International impact, Reviewed
Změněno: 18/10/2024 11:23, Ing. Jana Kuchtová

Abstract

V originále

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.

Links

GA20-20152S, research and development project
Name: Proteinová přitažlivost a selektivita pro buněčné membrány
Investor: Czech Science Foundation
LL2007, research and development project
Name: Peptidoví zabijáci bakterií (Acronym: PeptideKillers)
Investor: Ministry of Education, Youth and Sports of the CR
LM2015085, research and development project
Name: CERIT Scientific Cloud (Acronym: CERIT-SC)
Investor: Ministry of Education, Youth and Sports of the CR, CERIT Scientific Cloud
90127, large research infrastructures
Name: CIISB II