Počet záznamů: 1  

Ionic Strength and Solution Composition Dictate the Adsorption of Cell-Penetrating Peptides onto Phosphatidylcholine Membranes

  1. 1.
    SYSNO ASEP0561693
    Druh ASEPJ - Článek v odborném periodiku
    Zařazení RIVJ - Článek v odborném periodiku
    Poddruh JČlánek ve WOS
    NázevIonic Strength and Solution Composition Dictate the Adsorption of Cell-Penetrating Peptides onto Phosphatidylcholine Membranes
    Tvůrce(i) Nguyen, Man Thi Hong (UOCHB-X) ORCID
    Biriukov, Denys (UOCHB-X) ORCID, RID
    Tempra, Carmelo (UOCHB-X) ORCID
    Baxová, Katarína (UOCHB-X)
    Martinez-Seara, Hector (UOCHB-X) RID, ORCID
    Evci, Huseyin (UFCH-W)
    Singh, Vandana (UFCH-W)
    Šachl, Radek (UFCH-W) RID, ORCID
    Hof, Martin (UFCH-W) RID, ORCID
    Jungwirth, Pavel (UOCHB-X) RID, ORCID
    Javanainen, Matti (UOCHB-X) RID, ORCID
    Vazdar, Mario (UOCHB-X) ORCID
    Zdroj.dok.Langmuir. - : American Chemical Society - ISSN 0743-7463
    Roč. 38, č. 37 (2022), s. 11284-11295
    Poč.str.12 s.
    Jazyk dok.eng - angličtina
    Země vyd.US - Spojené státy americké
    Klíč. slovalinear constraint solver ; particle mesh Ewald ; molecular dynamics
    Obor OECDPhysical chemistry
    CEPGX19-26854X GA ČR - Grantová agentura ČR
    Způsob publikováníOpen access
    Institucionální podporaUOCHB-X - RVO:61388963 ; UFCH-W - RVO:61388955
    UT WOS000855771400001
    EID SCOPUS85137926123
    DOI10.1021/acs.langmuir.2c01435
    AnotaceAdsorption of arginine-rich positively charged peptides onto neutral zwitterionic phosphocholine (PC) bilayers is a key step in the translocation of those potent cell-penetrating peptides into the cell interior. In the past, we have shown both theoretically and experimentally that polyarginines adsorb to the neutral PC-supported lipid bilayers in contrast to polylysines. However, comparing our results with previous studies showed that the results often do not match even at the qualitative level. The adsorption of arginine-rich peptides onto 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) may qualitatively depend on the actual experimental conditions where binding experiments have been performed. In this work, we systematically studied the adsorption of R9 and K9 peptides onto the POPC bilayer, aided by molecular dynamics (MD) simulations and fluorescence cross-correlation spectroscopy (FCCS) experiments. Using MD simulations, we tested a series of increasing peptide concentrations, in parallel with increasing Na+ and Ca2+ salt concentrations, showing that the apparent strength of adsorption of R9 decreases upon the increase of peptide or salt concentration in the system. The key result from the simulations is that the salt concentrations used experimentally can alter the picture of peptide adsorption qualitatively. Using FCCS experiments with fluorescently labeled R9 and K9, we first demonstrated that the binding of R9 to POPC is tighter by almost 2 orders of magnitude compared to that of K9. Finally, upon the addition of an excess of either Na+ or Ca2+ ions with R9, the total fluorescence correlation signal is lost, which implies the unbinding of R9 from the PC bilayer, in agreement with our predictions from MD simulations.
    PracovištěÚstav organické chemie a biochemie
    Kontaktasep@uochb.cas.cz ; Kateřina Šperková, Tel.: 232 002 584 ; Jana Procházková, Tel.: 220 183 418
    Rok sběru2023
    Elektronická adresahttps://doi.org/10.1021/acs.langmuir.2c01435
Počet záznamů: 1  

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