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.Základní údaje
Originální název
Magainin 2 and PGLa in Bacterial Membrane Mimics III: Membrane Fusion and Disruption.
Autoři
KABELKA, Ivo (203 Česká republika, domácí), Vasil GEORGIEV, Lisa MARX, Peter PAJTINKA (703 Slovensko, domácí), Karl LOHNER, Georg PABST, Rumiana DIMOVA a Robert VÁCHA (203 Česká republika, garant, domácí)
Vydání
Biophysical Journal, New York, USA, Cell Press, 2022, 0006-3495
Další údaje
Jazyk
angličtina
Typ výsledku
Článek v odborném periodiku
Obor
10610 Biophysics
Stát vydavatele
Velká Británie a Severní Irsko
Utajení
není předmětem státního či obchodního tajemství
Odkazy
Impakt faktor
Impact factor: 3.400
Kód RIV
RIV/00216224:14740/22:00125525
Organizační jednotka
Středoevropský technologický institut
UT WoS
000765012800016
Klíčová slova anglicky
Cell Membrane; Cryoelectron Microscopy; Lipid Bilayers; Magainins; Membrane Fusion
Příznaky
Mezinárodní význam, Recenzováno
Změněno: 18. 10. 2024 11:23, Ing. Jana Kuchtová
Anotace
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.
Návaznosti
GA20-20152S, projekt VaV |
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LL2007, projekt VaV |
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LM2015085, projekt VaV |
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90127, velká výzkumná infrastruktura |
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