Optimal conditions for opening of membrane pore by amphiphilic
peptides

J 2015

Optimal conditions for opening of membrane pore by amphiphilic peptides

KABELKA, Ivo a Robert VÁCHA

Základní údaje

Originální název

Optimal conditions for opening of membrane pore by amphiphilic peptides

Autoři

KABELKA, Ivo (203 Česká republika, domácí) a Robert VÁCHA (203 Česká republika, garant, domácí)

Vydání

JOURNAL OF CHEMICAL PHYSICS, Melville (USA), AMER INST PHYSICS, 2015, 0021-9606

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10403 Physical chemistry

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 2.894

Kód RIV

RIV/00216224:14740/15:00081581

Organizační jednotka

Středoevropský technologický institut

DOI

https://doi.org/10.1063/1.4933229

UT WoS

000370412900021

EID Scopus

2-s2.0-84945296530

Klíčová slova anglicky

PORE FORMATION; ANTIMICROBIAL PEPTIDES; PHOSPHOLIPID MEMBRANE; COMPUTER SIMULATION; COARSE GRAINED; MONTE CARLO

Štítky

podil, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 5. 4. 2016 16:08, Mgr. Eva Špillingová

Anotace

V originále

Amphiphilic peptides can interact with biological membranes and severely affect their barrier and signaling functions. These peptides, including antimicrobial peptides, can self-assemble into transmembrane pores that cause cell death. Despite their medical importance, the conditions required for pore formation remain elusive. Monte Carlo simulations with coarse-grained models enabled us to calculate the free energies of pore opening under various conditions. In agreement with oriented circular dichroism experiments, a high peptide-to-lipid ratio was found to be necessary for spontaneous pore assembly. The peptide length has a non-monotonic impact on pore formation, and the optimal length matches with the membrane thickness. Furthermore, the hydrophobicity of the peptide ends and the mutual positions of peptides on the membrane play a role.

Návaznosti

ED1.1.00/02.0068, projekt VaV

Název: CEITEC - central european institute of technology

GA14-12598S, projekt VaV

Název: Samouspořádané systémy amfifilních peptiů (Akronym: SAAP)

Investor: Grantová agentura ČR, Self-assembly of amphiphilic peptides with helical character

286154, interní kód MU

Název: SYLICA - Synergies of Life and Material Sciences to Create a New Future (Akronym: SYLICA)

Investor: Evropská unie, SYLICA - Synergies of Life and Material Sciences to Create a New Future, Kapacity

Citovat

KABELKA, Ivo a Robert VÁCHA. Optimal conditions for opening of membrane pore by amphiphilic peptides. JOURNAL OF CHEMICAL PHYSICS. Melville (USA): AMER INST PHYSICS, 2015, roč. 143, č. 24, s. nestránkováno, 6 s. ISSN 0021-9606. Dostupné z: https://doi.org/10.1063/1.4933229.

@article{1335966,
   author = {Kabelka, Ivo and Vácha, Robert},
   article_location = {Melville (USA)},
   article_number = {24},
   doi = {https://doi.org/10.1063/1.4933229},
   keywords = {PORE FORMATION; ANTIMICROBIAL PEPTIDES; PHOSPHOLIPID MEMBRANE; COMPUTER SIMULATION; COARSE GRAINED; MONTE CARLO},
   language = {eng},
   issn = {0021-9606},
   journal = {JOURNAL OF CHEMICAL PHYSICS},
   title = {Optimal conditions for opening of membrane pore by amphiphilic peptides},
   url = {http://scitation.aip.org/content/aip/journal/jcp/143/24/10.1063/1.4933229},
   volume = {143},
   year = {2015}
}

TY  - JOUR
ID  - 1335966
AU  - Kabelka, Ivo - Vácha, Robert
PY  - 2015
TI  - Optimal conditions for opening of membrane pore by amphiphilic peptides
JF  - JOURNAL OF CHEMICAL PHYSICS
VL  - 143
IS  - 24
SP  - nestránkováno
EP  - nestránkováno
PB  - AMER INST PHYSICS
SN  - 00219606
KW  - PORE FORMATION
KW  - ANTIMICROBIAL PEPTIDES
KW  - PHOSPHOLIPID MEMBRANE
KW  - COMPUTER SIMULATION
KW  - COARSE GRAINED
KW  - MONTE CARLO
UR  - http://scitation.aip.org/content/aip/journal/jcp/143/24/10.1063/1.4933229
L2  - http://scitation.aip.org/content/aip/journal/jcp/143/24/10.1063/1.4933229
N2  - Amphiphilic peptides can interact with biological membranes and severely affect their barrier and signaling functions. These peptides, including antimicrobial peptides, can self-assemble into transmembrane pores that cause cell death. Despite their medical importance, the conditions required for pore formation remain elusive. Monte Carlo simulations with coarse-grained models enabled us to calculate the free energies of pore opening under various conditions. In agreement with oriented circular dichroism experiments, a high peptide-to-lipid ratio was found to be necessary for spontaneous pore assembly. The peptide length has a non-monotonic impact on pore formation, and the optimal length matches with the membrane thickness. Furthermore, the hydrophobicity of the peptide ends and the mutual positions of peptides on the membrane play a role.
ER  -

KABELKA, Ivo a Robert VÁCHA. Optimal conditions for opening of membrane pore by amphiphilic peptides. \textit{JOURNAL OF CHEMICAL PHYSICS}. Melville (USA): AMER INST PHYSICS, 2015, roč.~143, č.~24, s.~nestránkováno, 6 s. ISSN~0021-9606. Dostupné z: https://doi.org/10.1063/1.4933229.

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