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

Result code in 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>

Alternative codes found

RIV/61388963:_____/24:00582943

Result on the web

<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>

Result language

angličtina

Original language name

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

Original language description

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.

Czech name

—

Czech description

—

Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

—

OECD FORD branch

10403 - Physical chemistry

Project

<a href="/en/project/GX19-26854X" target="_blank" >GX19-26854X: Concert of lipids, ions, and proteins in cell membrane dynamics and function</a><br>

Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2024

Confidentiality

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

Name of the periodical

Colloids and Surfaces B-Biointerfaces

ISSN

0927-7765

e-ISSN

1873-4367

Volume of the periodical

235

Issue of the periodical within the volume

MAR 2024

Country of publishing house

NL - THE KINGDOM OF THE NETHERLANDS

Number of pages

10

Pages from-to

113765

UT code for WoS article

001179895200001

EID of the result in the Scopus database

2-s2.0-85184063912