Molecular dynamics simulations unveil the aggregation patterns and salting out of polyarginines at zwitterionic POPC bilayers in solutions of various ionic strengths

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F24%3A00601191" target="_blank" >RIV/61388963:_____/24:00601191 - isvavai.cz</a>

Alternative codes found

RIV/60461373:22340/24:43930801

Result on the web

<a href="https://doi.org/10.1016/j.csbj.2024.11.004" target="_blank" >https://doi.org/10.1016/j.csbj.2024.11.004</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.csbj.2024.11.004" target="_blank" >10.1016/j.csbj.2024.11.004</a>

Result language

angličtina

Original language name

Molecular dynamics simulations unveil the aggregation patterns and salting out of polyarginines at zwitterionic POPC bilayers in solutions of various ionic strengths

Original language description

This study employs molecular dynamics (MD) simulations to investigate the adsorption and aggregation behavior of simple polyarginine cellpenetrating peptides (CPPs), specifically modeled as R9 peptides, at zwitterionic phosphocholine POPC membranes under varying ionic strengths of two peptide concentrations and two concentrations of NaCl and CaCl2. The results reveal an intriguing phenomenon of R9 aggregation at the membrane, which is dependent on the ionic strength indicating a saltingout effect. As the peptide concentration and ionic strength increase, peptide aggregation also increases, with aggregate lifetimes and sizes showing a corresponding rise, accompanied by the total decrease of adsorbed peptides at the membrane surface. Notably, in high ionic strength environments, large R9 aggregates, such as octamers, are also observed occasionally. The saltingout, typically uncommon for short positively charged peptides, is attributed to the unique properties of arginine amino acid, specifically by its side chain containing amphiphilic guanidinium (Gdm+) ion which makes both intermolecular hydrophobic likecharge Gdm+ – Gdm+ and saltbridge Gdm+ – C-terminus interactions, where the former are increased with the ionic strength, and the latter decreased due to electrostatic screening. The aggregation behavior of R9 peptides at membranes can also linked to their CPP translocation properties, suggesting that aggregation may aid in translocation across cellular membranes.

Czech name

—

Czech description

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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/EH22_008%2F0004617" target="_blank" >EH22_008/0004617: Energy conversion and storage</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

Computational and Structural Biotechnology Journal

ISSN

2001-0370

e-ISSN

2001-0370

Volume of the periodical

23

Issue of the periodical within the volume

December

Country of publishing house

NL - THE KINGDOM OF THE NETHERLANDS

Number of pages

9

Pages from-to

3897-3905

UT code for WoS article

001361756500001

EID of the result in the Scopus database

2-s2.0-85208124578