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231225s2019 xx |||||o 00| ||eng c |
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|a 10.1021/acs.langmuir.8b04195
|2 doi
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|a pubmed24n0984.xml
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|a (DE-627)NLM29530538X
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|a (NLM)30908063
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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|a Daudey, Geert A
|e verfasserin
|4 aut
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|a Influence of Membrane-Fusogen Distance on the Secondary Structure of Fusogenic Coiled Coil Peptides
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|c 2019
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
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|2 rdacarrier
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|a Date Completed 28.07.2020
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|a Date Revised 11.10.2023
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a 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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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Peptides
|2 NLM
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|a Polyethylene Glycols
|2 NLM
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|a 3WJQ0SDW1A
|2 NLM
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|a Schwieger, Christian
|e verfasserin
|4 aut
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|a Rabe, Martin
|e verfasserin
|4 aut
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|a Kros, Alexander
|e verfasserin
|4 aut
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|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1992
|g 35(2019), 16 vom: 23. Apr., Seite 5501-5508
|w (DE-627)NLM098181009
|x 1520-5827
|7 nnns
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|g volume:35
|g year:2019
|g number:16
|g day:23
|g month:04
|g pages:5501-5508
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|u http://dx.doi.org/10.1021/acs.langmuir.8b04195
|3 Volltext
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|d 35
|j 2019
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|h 5501-5508
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