Amphipathic Peptides Impede Lipid Domain Fusion in Phase-Separated Membranes

Cell membranes are heterogeneous in lipid composition which leads to the phase separation with the formation of nanoscopic liquid-ordered domains, also called rafts. There are multiple cell processes whereby the clustering of these domains into a larger one might be involved, which is responsible fo...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Konstantin V. Pinigin, Timur R. Galimzyanov, Sergey A. Akimov
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	lipid membrane theory of elasticity liquid-ordered domain domain interaction amphipathic peptide Chemical technology TP1-1185 Chemical engineering TP155-156
Acceso en línea:	https://doaj.org/article/217fc287ebd2468997f0addbb8e70197
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:217fc287ebd2468997f0addbb8e70197
record_format	dspace
spelling	oai:doaj.org-article:217fc287ebd2468997f0addbb8e701972021-11-25T18:19:25ZAmphipathic Peptides Impede Lipid Domain Fusion in Phase-Separated Membranes10.3390/membranes111107972077-0375https://doaj.org/article/217fc287ebd2468997f0addbb8e701972021-10-01T00:00:00Zhttps://www.mdpi.com/2077-0375/11/11/797https://doaj.org/toc/2077-0375Cell membranes are heterogeneous in lipid composition which leads to the phase separation with the formation of nanoscopic liquid-ordered domains, also called rafts. There are multiple cell processes whereby the clustering of these domains into a larger one might be involved, which is responsible for such important processes as signal transduction, polarized sorting, or immune response. Currently, antimicrobial amphipathic peptides are considered promising antimicrobial, antiviral, and anticancer therapeutic agents. Here, within the framework of the classical theory of elasticity adapted for lipid membranes, we investigate how the presence of the peptides in a phase-separated membrane influences the fusion of the domains. We show that the peptides tend to occupy the boundaries of liquid-ordered domains and significantly increase the energy barrier of the domain-domain fusion, which might lead to misregulation of raft clustering and adverse consequences for normal cell processes.Konstantin V. PiniginTimur R. GalimzyanovSergey A. AkimovMDPI AGarticlelipid membranetheory of elasticityliquid-ordered domaindomain interactionamphipathic peptideChemical technologyTP1-1185Chemical engineeringTP155-156ENMembranes, Vol 11, Iss 797, p 797 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	lipid membrane theory of elasticity liquid-ordered domain domain interaction amphipathic peptide Chemical technology TP1-1185 Chemical engineering TP155-156
spellingShingle	lipid membrane theory of elasticity liquid-ordered domain domain interaction amphipathic peptide Chemical technology TP1-1185 Chemical engineering TP155-156 Konstantin V. Pinigin Timur R. Galimzyanov Sergey A. Akimov Amphipathic Peptides Impede Lipid Domain Fusion in Phase-Separated Membranes
description	Cell membranes are heterogeneous in lipid composition which leads to the phase separation with the formation of nanoscopic liquid-ordered domains, also called rafts. There are multiple cell processes whereby the clustering of these domains into a larger one might be involved, which is responsible for such important processes as signal transduction, polarized sorting, or immune response. Currently, antimicrobial amphipathic peptides are considered promising antimicrobial, antiviral, and anticancer therapeutic agents. Here, within the framework of the classical theory of elasticity adapted for lipid membranes, we investigate how the presence of the peptides in a phase-separated membrane influences the fusion of the domains. We show that the peptides tend to occupy the boundaries of liquid-ordered domains and significantly increase the energy barrier of the domain-domain fusion, which might lead to misregulation of raft clustering and adverse consequences for normal cell processes.
format	article
author	Konstantin V. Pinigin Timur R. Galimzyanov Sergey A. Akimov
author_facet	Konstantin V. Pinigin Timur R. Galimzyanov Sergey A. Akimov
author_sort	Konstantin V. Pinigin
title	Amphipathic Peptides Impede Lipid Domain Fusion in Phase-Separated Membranes
title_short	Amphipathic Peptides Impede Lipid Domain Fusion in Phase-Separated Membranes
title_full	Amphipathic Peptides Impede Lipid Domain Fusion in Phase-Separated Membranes
title_fullStr	Amphipathic Peptides Impede Lipid Domain Fusion in Phase-Separated Membranes
title_full_unstemmed	Amphipathic Peptides Impede Lipid Domain Fusion in Phase-Separated Membranes
title_sort	amphipathic peptides impede lipid domain fusion in phase-separated membranes
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/217fc287ebd2468997f0addbb8e70197
work_keys_str_mv	AT konstantinvpinigin amphipathicpeptidesimpedelipiddomainfusioninphaseseparatedmembranes AT timurrgalimzyanov amphipathicpeptidesimpedelipiddomainfusioninphaseseparatedmembranes AT sergeyaakimov amphipathicpeptidesimpedelipiddomainfusioninphaseseparatedmembranes
_version_	1718411306231398400

Amphipathic Peptides Impede Lipid Domain Fusion in Phase-Separated Membranes

Ejemplares similares