2020
Magainin 2 and PGLa in Bacterial Membrane Mimics II: Membrane Fusion and Sponge Phase Formation.
KABELKA, Ivo, Michael PACHLER, Sylvain PRÉVOST, Ilse LETOFSKY-PAPST, Karl LOHNER et. al.Základní údaje
Originální název
Magainin 2 and PGLa in Bacterial Membrane Mimics II: Membrane Fusion and Sponge Phase Formation.
Autoři
KABELKA, Ivo (203 Česká republika, domácí), Michael PACHLER, Sylvain PRÉVOST, Ilse LETOFSKY-PAPST, Karl LOHNER, Georg PABST a Robert VÁCHA (203 Česká republika, garant, domácí)
Vydání
Biophysical Journal, Cambridge, USA, Cell Press, 2020, 0006-3495
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
Impakt faktor
Impact factor: 4.033
Kód RIV
RIV/00216224:14740/20:00114044
Organizační jednotka
Středoevropský technologický institut
UT WoS
000511291400010
Klíčová slova anglicky
X-RAY-SCATTERING; FORCE-FIELD; PEPTIDES; DYNAMICS; CURVATURE; MECHANISM; TRANSITIONS; VALIDATION; POTENTIALS; EXTENSION
Štítky
Příznaky
Mezinárodní význam, Recenzováno
Změněno: 19. 2. 2023 22:08, prof. RNDr. Robert Vácha, PhD.
Anotace
V originále
We studied the synergistic mechanism of equimolar mixtures of magainin 2 (MG2a) and PGLa in phosphatidylethanolamine/phosphatidylglycerol mimics of Gram-negative cytoplasmic membranes. In a preceding article of this series, we reported on the early onset of parallel heterodimer formation of the two antimicrobial peptides already at low concentrations and the resulting defect formation in the membranes. Here, we focus on the structures of the peptide-lipid aggregates occurring in the synergistic regime at elevated peptide concentrations. Using a combination of calorimetric, scattering, electron microscopic, and in silico techniques, we demonstrate that the two peptides, even if applied individually, transform originally large unilamellar vesicles into multilamellar vesicles with a collapsed interbilayer spacing resulting from peptide-induced adhesion. Interestingly, the adhesion does not lead to a peptide-induced lipid separation of charged and charge-neutral species. In addition to this behavior, equimolar mixtures of MG2a and PGLa formed surface-aligned fibril-like structures, which induced adhesion zones between the membranes and the formation of transient fusion stalks in molecular dynamics simulations and a coexisting sponge phase observed by small-angle x-ray scattering. The previously reported increased leakage of lipid vesicles of identical composition in the presence of MG2a/PGLa mixtures is therefore related to a peptide-induced cross-linking of bilayers.
Návaznosti
GA17-11571S, projekt VaV |
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LM2015085, projekt VaV |
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LQ1601, projekt VaV |
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MUNI/G/1100/2016, interní kód MU |
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90042, velká výzkumná infrastruktura |
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90070, velká výzkumná infrastruktura |
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