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

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Publikace nespadá pod Ekonomicko-správní fakultu, ale pod Středoevropský technologický institut. Oficiální stránka publikace je na webu muni.cz.
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KABELKA Ivo GEORGIEV Vasil MARX Lisa PAJTINKA Peter LOHNER Karl PABST Georg DIMOVA Rumiana VÁCHA Robert

Rok publikování 2022
Druh Článek v odborném periodiku
Časopis / Zdroj Biophysical Journal
Fakulta / Pracoviště MU

Středoevropský technologický institut

Citace
www https://www.sciencedirect.com/science/article/pii/S000634952103959X?via%3Dihub
Doi http://dx.doi.org/10.1016/j.bpj.2021.12.035
Klíčová slova Cell Membrane; Cryoelectron Microscopy; Lipid Bilayers; Magainins; Membrane Fusion
Popis 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.
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