Detailed Information on Publication Record
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
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 |
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LL2007, research and development project |
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LM2015085, research and development project |
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90127, large research infrastructures |
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