Charge of a transmembrane peptide alters its interaction with lipid membranes.

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388955%3A_____%2F24%3A00582992" target="_blank" >RIV/61388955:_____/24:00582992 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/61388963:_____/24:00582943

Výsledek na webu

<a href="https://hdl.handle.net/11104/0351018" target="_blank" >https://hdl.handle.net/11104/0351018</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.colsurfb.2024.113765" target="_blank" >10.1016/j.colsurfb.2024.113765</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Charge of a transmembrane peptide alters its interaction with lipid membranes.

Popis výsledku v původním jazyce

Transmembrane (TM) proteins interact closely with the surrounding membrane lipids. Lipids in the vicinity of TM proteins were reported to have hindered mobility, which has been associated with lipids being caught up in the rough surface of the TM domains. These reports, however, neglect one important factor that largely influences the membrane behavior electrostatics of the TM peptides that are usually positively charged at their cytosolic end. Here, we study on the example of a neutral and a positively charged WALP peptide, how the charge of a TM peptide influences the membrane. We investigate both its dynamics and mechanics by: (i) time dependent fluorescent shift in combination with classical and FRET generalized polarization to evaluate the mobility of lipids at short and long-range distance from the peptide, (ii) atomic force microscopy to observe the mechanical stability of the peptide-containing membranes, and (iii) molecular dynamics simulations to analyze the peptide-lipid interactions. We show that both TM peptides lower lipid mobility in their closest surroundings. The peptides cause lateral heterogeneity in lipid mobility, which in turn prevents free lipid rearrangement and lowers the membrane ability to seal ruptures after mechanical indentations. Introduction of a positive charge to the peptide largely enhances these effects, affecting the whole membrane. We thus highlight that unspecific peptide-lipid interactions, especially the electrostatics, should not be overlooked as they have a great impact on the mechanics and dynamics of the whole membrane.

Název v anglickém jazyce

Charge of a transmembrane peptide alters its interaction with lipid membranes.

Popis výsledku anglicky

Transmembrane (TM) proteins interact closely with the surrounding membrane lipids. Lipids in the vicinity of TM proteins were reported to have hindered mobility, which has been associated with lipids being caught up in the rough surface of the TM domains. These reports, however, neglect one important factor that largely influences the membrane behavior electrostatics of the TM peptides that are usually positively charged at their cytosolic end. Here, we study on the example of a neutral and a positively charged WALP peptide, how the charge of a TM peptide influences the membrane. We investigate both its dynamics and mechanics by: (i) time dependent fluorescent shift in combination with classical and FRET generalized polarization to evaluate the mobility of lipids at short and long-range distance from the peptide, (ii) atomic force microscopy to observe the mechanical stability of the peptide-containing membranes, and (iii) molecular dynamics simulations to analyze the peptide-lipid interactions. We show that both TM peptides lower lipid mobility in their closest surroundings. The peptides cause lateral heterogeneity in lipid mobility, which in turn prevents free lipid rearrangement and lowers the membrane ability to seal ruptures after mechanical indentations. Introduction of a positive charge to the peptide largely enhances these effects, affecting the whole membrane. We thus highlight that unspecific peptide-lipid interactions, especially the electrostatics, should not be overlooked as they have a great impact on the mechanics and dynamics of the whole membrane.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10403 - Physical chemistry

Projekt

<a href="/cs/project/GX19-26854X" target="_blank" >GX19-26854X: Souhra lipidů, iontů a bílkovin a její role v dynamice a funkci buněčných membrán</a><br>

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2024

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Colloids and Surfaces B-Biointerfaces

ISSN

0927-7765

e-ISSN

1873-4367

Svazek periodika

235

Číslo periodika v rámci svazku

MAR 2024

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

10

Strana od-do

113765

Kód UT WoS článku

001179895200001

EID výsledku v databázi Scopus

2-s2.0-85184063912