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Influence of Membrane–Fusogen Distance on the Secondary Structure of Fusogenic Coiled Coil Peptides

[Image: see text] 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...

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Autores principales: Daudey, Geert A., Schwieger, Christian, Rabe, Martin, Kros, Alexander
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2019
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6484379/
https://www.ncbi.nlm.nih.gov/pubmed/30908063
http://dx.doi.org/10.1021/acs.langmuir.8b04195
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author Daudey, Geert A.
Schwieger, Christian
Rabe, Martin
Kros, Alexander
author_facet Daudey, Geert A.
Schwieger, Christian
Rabe, Martin
Kros, Alexander
author_sort Daudey, Geert A.
collection PubMed
description [Image: see text] 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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spelling pubmed-64843792019-04-29 Influence of Membrane–Fusogen Distance on the Secondary Structure of Fusogenic Coiled Coil Peptides Daudey, Geert A. Schwieger, Christian Rabe, Martin Kros, Alexander Langmuir [Image: see text] 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. American Chemical Society 2019-03-25 2019-04-23 /pmc/articles/PMC6484379/ /pubmed/30908063 http://dx.doi.org/10.1021/acs.langmuir.8b04195 Text en Copyright © 2019 American Chemical Society This is an open access article published under a Creative Commons Non-Commercial No Derivative Works (CC-BY-NC-ND) Attribution License (http://pubs.acs.org/page/policy/authorchoice_ccbyncnd_termsofuse.html) , which permits copying and redistribution of the article, and creation of adaptations, all for non-commercial purposes.
spellingShingle Daudey, Geert A.
Schwieger, Christian
Rabe, Martin
Kros, Alexander
Influence of Membrane–Fusogen Distance on the Secondary Structure of Fusogenic Coiled Coil Peptides
title Influence of Membrane–Fusogen Distance on the Secondary Structure of Fusogenic Coiled Coil Peptides
title_full Influence of Membrane–Fusogen Distance on the Secondary Structure of Fusogenic Coiled Coil Peptides
title_fullStr Influence of Membrane–Fusogen Distance on the Secondary Structure of Fusogenic Coiled Coil Peptides
title_full_unstemmed Influence of Membrane–Fusogen Distance on the Secondary Structure of Fusogenic Coiled Coil Peptides
title_short Influence of Membrane–Fusogen Distance on the Secondary Structure of Fusogenic Coiled Coil Peptides
title_sort influence of membrane–fusogen distance on the secondary structure of fusogenic coiled coil peptides
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6484379/
https://www.ncbi.nlm.nih.gov/pubmed/30908063
http://dx.doi.org/10.1021/acs.langmuir.8b04195
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