English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Magainin 2 and PGLa in bacterial membrane mimics III : membrane fusion and disruption

Kabelka, I., Georgiev, V., Marx, L., Pajtinka, P., Lohner, K., Pabst, G., et al. (2022). Magainin 2 and PGLa in bacterial membrane mimics III: membrane fusion and disruption. Biophysical Journal, 121(5), 852-861. doi:10.1016/j.bpj.2021.12.035.

Item is

Basic

show hide
Genre: Journal Article

Files

show Files
hide Files
:
Article.pdf (Publisher version), 3MB
Name:
Article.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-

Locators

show

Creators

show
hide
 Creators:
Kabelka, Ivo, Author
Georgiev, Vasil1, Author              
Marx, Lisa, Author
Pajtinka, Peter, Author
Lohner, Karl, Author
Pabst, Georg, Author
Dimova, Rumiana1, Author              
Vácha, Robert, Author
Affiliations:
1Rumiana Dimova, Theorie & Bio-Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_1863328              

Content

show
hide
Free keywords: -
 Abstract: We previously speculated that the synergistically enhanced antimicrobial activity of Magainin 2 and PGLa is related to membrane adhesion, fusion, and further membrane remodelling. Here, we combined computer simulations with time-resolved in vitro fluorescence microscopy, cryogenic electron microscopy (cryo-EM), and small-angle X-ray scattering (SAXS) to interrogate such morphological and topological changes of vesicles at nanoscopic and microscopic length scales in real time. Coarse-grained simulations revealed the formation of an elongated and bent fusion zone between vesicles in the presence of equimolar peptide mixtures. Vesicle adhesion and fusion was observed to occur within few seconds by cryo-EM and corroborated by SAXS measurements. The latter experiments further indicated continued and time-extended structural remodelling also 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 already few seconds after peptide addition. The synergistic interactions between the peptides shorten the time response of vesicles and enhance membrane fusogenic and disrupting properties of the equimolar mixture compared to the individual peptides.

Details

show
hide
Language(s): eng - English
 Dates: 2022-02-052022
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: DOI: 10.1016/j.bpj.2021.12.035
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Biophysical Journal
  Other : Biophys. J.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Cambridge, Mass. : Cell Press
Pages: - Volume / Issue: 121 (5) Sequence Number: - Start / End Page: 852 - 861 Identifier: ISSN: 0006-3495