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Peptides at the Interface: Self-Assembly of Amphiphilic Designer Peptides and Their Membrane Interaction Propensity

[Image: see text] Self-assembling amphiphilic designer peptides have been successfully applied as nanomaterials in biomedical applications. Understanding molecular interactions at the peptide–membrane interface is crucial, since interactions at this site often determine (in)compatibility. The presen...

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Autores principales: Kornmueller, Karin, Lehofer, Bernhard, Meindl, Claudia, Fröhlich, Eleonore, Leitinger, Gerd, Amenitsch, Heinz, Prassl, Ruth
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2016
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5111122/
https://www.ncbi.nlm.nih.gov/pubmed/27741400
http://dx.doi.org/10.1021/acs.biomac.6b01089
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author Kornmueller, Karin
Lehofer, Bernhard
Meindl, Claudia
Fröhlich, Eleonore
Leitinger, Gerd
Amenitsch, Heinz
Prassl, Ruth
author_facet Kornmueller, Karin
Lehofer, Bernhard
Meindl, Claudia
Fröhlich, Eleonore
Leitinger, Gerd
Amenitsch, Heinz
Prassl, Ruth
author_sort Kornmueller, Karin
collection PubMed
description [Image: see text] Self-assembling amphiphilic designer peptides have been successfully applied as nanomaterials in biomedical applications. Understanding molecular interactions at the peptide–membrane interface is crucial, since interactions at this site often determine (in)compatibility. The present study aims to elucidate how model membrane systems of different complexity (in particular single-component phospholipid bilayers and lipoproteins) respond to the presence of amphiphilic designer peptides. We focused on two short anionic peptides, V(4)WD(2) and A(6)YD, which are structurally similar but showed a different self-assembly behavior. A(6)YD self-assembled into high aspect ratio nanofibers at low peptide concentrations, as evidenced by synchrotron small-angle X-ray scattering and electron microscopy. These supramolecular assemblies coexisted with membranes without remarkable interference. In contrast, V(4)WD(2) formed only loosely associated assemblies over a large concentration regime, and the peptide promoted concentration-dependent disorder on the membrane arrangement. Perturbation effects were observed on both membrane systems although most likely induced by different modes of action. These results suggest that membrane activity critically depends on the peptide’s inherent ability to form highly cohesive supramolecular structures.
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spelling pubmed-51111222016-11-21 Peptides at the Interface: Self-Assembly of Amphiphilic Designer Peptides and Their Membrane Interaction Propensity Kornmueller, Karin Lehofer, Bernhard Meindl, Claudia Fröhlich, Eleonore Leitinger, Gerd Amenitsch, Heinz Prassl, Ruth Biomacromolecules [Image: see text] Self-assembling amphiphilic designer peptides have been successfully applied as nanomaterials in biomedical applications. Understanding molecular interactions at the peptide–membrane interface is crucial, since interactions at this site often determine (in)compatibility. The present study aims to elucidate how model membrane systems of different complexity (in particular single-component phospholipid bilayers and lipoproteins) respond to the presence of amphiphilic designer peptides. We focused on two short anionic peptides, V(4)WD(2) and A(6)YD, which are structurally similar but showed a different self-assembly behavior. A(6)YD self-assembled into high aspect ratio nanofibers at low peptide concentrations, as evidenced by synchrotron small-angle X-ray scattering and electron microscopy. These supramolecular assemblies coexisted with membranes without remarkable interference. In contrast, V(4)WD(2) formed only loosely associated assemblies over a large concentration regime, and the peptide promoted concentration-dependent disorder on the membrane arrangement. Perturbation effects were observed on both membrane systems although most likely induced by different modes of action. These results suggest that membrane activity critically depends on the peptide’s inherent ability to form highly cohesive supramolecular structures. American Chemical Society 2016-10-14 2016-11-14 /pmc/articles/PMC5111122/ /pubmed/27741400 http://dx.doi.org/10.1021/acs.biomac.6b01089 Text en Copyright © 2016 American Chemical Society This is an open access article published under a Creative Commons Attribution (CC-BY) License (http://pubs.acs.org/page/policy/authorchoice_ccby_termsofuse.html) , which permits unrestricted use, distribution and reproduction in any medium, provided the author and source are cited.
spellingShingle Kornmueller, Karin
Lehofer, Bernhard
Meindl, Claudia
Fröhlich, Eleonore
Leitinger, Gerd
Amenitsch, Heinz
Prassl, Ruth
Peptides at the Interface: Self-Assembly of Amphiphilic Designer Peptides and Their Membrane Interaction Propensity
title Peptides at the Interface: Self-Assembly of Amphiphilic Designer Peptides and Their Membrane Interaction Propensity
title_full Peptides at the Interface: Self-Assembly of Amphiphilic Designer Peptides and Their Membrane Interaction Propensity
title_fullStr Peptides at the Interface: Self-Assembly of Amphiphilic Designer Peptides and Their Membrane Interaction Propensity
title_full_unstemmed Peptides at the Interface: Self-Assembly of Amphiphilic Designer Peptides and Their Membrane Interaction Propensity
title_short Peptides at the Interface: Self-Assembly of Amphiphilic Designer Peptides and Their Membrane Interaction Propensity
title_sort peptides at the interface: self-assembly of amphiphilic designer peptides and their membrane interaction propensity
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5111122/
https://www.ncbi.nlm.nih.gov/pubmed/27741400
http://dx.doi.org/10.1021/acs.biomac.6b01089
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