Enhanced translocation of amphiphilic peptides across membranes
by transmembrane proteins.

J 2021

Enhanced translocation of amphiphilic peptides across membranes by transmembrane proteins.

BARTOŠ, Ladislav; Ivo KABELKA a Robert VÁCHA

Základní údaje

Originální název

Enhanced translocation of amphiphilic peptides across membranes by transmembrane proteins.

Autoři

BARTOŠ, Ladislav ; Ivo KABELKA a Robert VÁCHA

Vydání

Biophysical Journal, New York, USA, Cell Press, 2021, 0006-3495

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10610 Biophysics

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 3.699

Kód RIV

RIV/00216224:14740/21:00118993

Organizační jednotka

Středoevropský technologický institut

DOI

https://doi.org/10.1016/j.bpj.2021.04.005

UT WoS

000658195300019

EID Scopus

2-s2.0-85105361272

Klíčová slova anglicky

CELL-PENETRATING PEPTIDESMOLECULAR-DYNAMICSFORCE-FIELDEXTENSION

Štítky

14312020, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 29. 4. 2022 08:15, Mgr. Michal Petr

Anotace

V originále

Cell membranes are phospholipid bilayers with a large number of embedded transmembrane proteins. Some of these proteins, such as scramblases, have properties that facilitate lipid flip-flop from one membrane leaflet to another. Scramblases and similar transmembrane proteins could also affect the translocation of other amphiphilic molecules, including cell-penetrating or antimicrobial peptides. We studied the effect of transmembrane proteins on the translocation of amphiphilic peptides through the membrane. Using two very different models, we consistently demonstrate that transmembrane proteins with a hydrophilic patch enhance the translocation of amphiphilic peptides by stabilizing the peptide in the membrane. Moreover, there is an optimum amphiphilicity because the peptide could become overstabilized in the transmembrane state, in which the peptide-protein dissociation is hampered, limiting the peptide translocation. The presence of scramblases and other proteins with similar properties could be exploited for more efficient transport into cells. The described principles could also be utilized in the design of a drug-delivery system by the addition of a translocation-enhancing peptide that would integrate into the membrane.

Návaznosti

GA17-11571S, projekt VaV

Název: Amfifilní peptidy na fosfolipidových membránách

Investor: Grantová agentura ČR, Amphiphilic Peptides at Phospholipid Membranes

GA20-20152S, projekt VaV

Název: Proteinová přitažlivost a selektivita pro buněčné membrány

Investor: Grantová agentura ČR, Protein Affinity and Selectivity to Cellular Membranes

LL2007, projekt VaV

Název: Peptidoví zabijáci bakterií (Akronym: PeptideKillers)

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Peptide Killers of Bacteria

LM2015085, projekt VaV

Název: CERIT Scientific Cloud (Akronym: CERIT-SC)

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, CERIT Scientific Cloud

90070, velká výzkumná infrastruktura

Název: IT4Innovations

Citovat

BARTOŠ, Ladislav; Ivo KABELKA a Robert VÁCHA. Enhanced translocation of amphiphilic peptides across membranes by transmembrane proteins. Biophysical Journal. New York, USA: Cell Press, 2021, roč. 120, č. 11, s. 2296-2305. ISSN 0006-3495. Dostupné z: https://doi.org/10.1016/j.bpj.2021.04.005.

@article{1773101,
   author = {Bartoš, Ladislav and Kabelka, Ivo and Vácha, Robert},
   article_location = {New York, USA},
   article_number = {11},
   doi = {https://doi.org/10.1016/j.bpj.2021.04.005},
   keywords = {CELL-PENETRATING PEPTIDESMOLECULAR-DYNAMICSFORCE-FIELDEXTENSION},
   language = {eng},
   issn = {0006-3495},
   journal = {Biophysical Journal},
   title = {Enhanced translocation of amphiphilic peptides across membranes by transmembrane proteins.},
   url = {https://www.sciencedirect.com/science/article/pii/S0006349521003003?via%3Dihub},
   volume = {120},
   year = {2021}
}

TY  - JOUR
ID  - 1773101
AU  - Bartoš, Ladislav - Kabelka, Ivo - Vácha, Robert
PY  - 2021
TI  - Enhanced translocation of amphiphilic peptides across membranes by transmembrane proteins.
JF  - Biophysical Journal
VL  - 120
IS  - 11
SP  - 2296-2305
EP  - 2296-2305
PB  - Cell Press
SN  - 00063495
KW  - CELL-PENETRATING PEPTIDESMOLECULAR-DYNAMICSFORCE-FIELDEXTENSION
UR  - https://www.sciencedirect.com/science/article/pii/S0006349521003003?via%3Dihub
N2  - Cell membranes are phospholipid bilayers with a large number of embedded transmembrane proteins. Some of these proteins, such as scramblases, have properties that facilitate lipid flip-flop from one membrane leaflet to another. Scramblases and similar transmembrane proteins could also affect the translocation of other amphiphilic molecules, including cell-penetrating or antimicrobial peptides. We studied the effect of transmembrane proteins on the translocation of amphiphilic peptides through the membrane. Using two very different models, we consistently demonstrate that transmembrane proteins with a hydrophilic patch enhance the translocation of amphiphilic peptides by stabilizing the peptide in the membrane. Moreover, there is an optimum amphiphilicity because the peptide could become overstabilized in the transmembrane state, in which the peptide-protein dissociation is hampered, limiting the peptide translocation. The presence of scramblases and other proteins with similar properties could be exploited for more efficient transport into cells. The described principles could also be utilized in the design of a drug-delivery system by the addition of a translocation-enhancing peptide that would integrate into the membrane.
ER  -

BARTOŠ, Ladislav; Ivo KABELKA a Robert VÁCHA. Enhanced translocation of amphiphilic peptides across membranes by transmembrane proteins. \textit{Biophysical Journal}. New York, USA: Cell Press, 2021, roč.~120, č.~11, s.~2296-2305. ISSN~0006-3495. Dostupné z: https://doi.org/10.1016/j.bpj.2021.04.005.

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