Journal
LANGMUIR
Volume 35, Issue 16, Pages 5501-5508Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.langmuir.8b04195
Keywords
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Funding
- Netherlands Organization for Scientific Research (NWO) via a ChemThem grant
- Deutsche Forschungsgemeinschaft (DFG) [FOR 1145]
- European Union's Horizon 2020 research and innovation programme under a Marie Sklodowska-Curie Grant [705857]
- NWO VICI grant [724.014.001]
- Marie Curie Actions (MSCA) [705857] Funding Source: Marie Curie Actions (MSCA)
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Liposomal membrane fusion is an important tool to study complex biological fusion mechanisms. We use lipidated derivatives of the specific heterodimeric coiled coil pair E: (EIAALEK)(3) and K: (KIAALKE)(3) to study and control the fusion of liposomes. In this model system, peptides are tethered to their liposomes via a poly(ethylene glycol) (PEG) spacer and a lipid anchor. The efficiency of the fusion mechanism and function of the peptides is highly affected by the PEG-spacer length and the lipid anchor type. Here, the influence of membrane-fusogen distance on the peptide-membrane interactions and the peptide secondary structures is studied with Langmuir film balance and infrared reflection absorption spectroscopy. We found that the introduction of a spacer to monolayer-tethered peptide E changes its conformation from solvated random coils to homo-oligomers. In contrast, the described peptide-monolayer interaction of peptide K is not affected by the PEG-spacer length. Furthermore, the coexistence of different conformations when both lipopeptides E and K are present at the membrane surface is demonstrated empirically, which has many implications for the design of effective fusogenic recognition units and the field of artificial membrane fusion.
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