The use of giant unilamellar vesicles to study functional properties of pore-forming toxins.

Binding Droplet transfer Electroformation Giant unilamellar vesicles In vitro transcription and translation Permeabilisation Pore formation Pore-forming toxins

Journal

Methods in enzymology
ISSN: 1557-7988
Titre abrégé: Methods Enzymol
Pays: United States
ID NLM: 0212271

Informations de publication

Date de publication:
2021
Historique:
entrez: 13 3 2021
pubmed: 14 3 2021
medline: 24 6 2021
Statut: ppublish

Résumé

Pore-forming toxins (PFTs) act upon lipid membranes and appropriate model systems are of great importance in researching these proteins. Giant unilamellar vesicles (GUVs) are an excellent model membrane system to study interactions between lipids and proteins. Their main advantage is the size comparable to cells, which means that GUVs can be observed directly under the light microscope. Many PFTs properties can be studied by using GUVs, such as binding specificity, membrane reorganization upon protein binding and oligomerization, pore properties and mechanism of pore formation. GUVs also represent a good model for biotechnological approaches, e.g., in applications in synthetic biology and medicine. Each research area has its own demands for GUVs properties, so several different approaches for GUVs preparations have been developed and will be discussed in this chapter.

Identifiants

pubmed: 33712188
pii: S0076-6879(21)00038-0
doi: 10.1016/bs.mie.2021.01.016
pii:
doi:

Substances chimiques

Lipids 0
Unilamellar Liposomes 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

219-251

Informations de copyright

Copyright © 2021 Elsevier Inc. All rights reserved.

Auteurs

Saša Aden (S)

Department for Molecular Biology and Nanobiotechnology, National Institute of Chemistry, Ljubljana, Slovenia.

Tina Snoj (T)

Department for Molecular Biology and Nanobiotechnology, National Institute of Chemistry, Ljubljana, Slovenia.

Gregor Anderluh (G)

Department for Molecular Biology and Nanobiotechnology, National Institute of Chemistry, Ljubljana, Slovenia. Electronic address: gregor.anderluh@ki.si.

Articles similaires

Conservation of the cooling agent binding pocket within the TRPM subfamily.

Kate Huffer, Matthew C S Denley, Elisabeth V Oskoui et al.
1.00
TRPM Cation Channels Animals Binding Sites Mice Pyrimidinones
Fucosyltransferases Drug Repositioning Molecular Docking Simulation Molecular Dynamics Simulation Humans
Receptor, Cannabinoid, CB1 Ligands Molecular Dynamics Simulation Protein Binding Thermodynamics

Structural basis for molecular assembly of fucoxanthin chlorophyll

Koji Kato, Yoshiki Nakajima, Jian Xing et al.
1.00
Diatoms Photosystem I Protein Complex Chlorophyll Binding Proteins Cryoelectron Microscopy Light-Harvesting Protein Complexes

Classifications MeSH