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Cationic amphipathic peptides accumulate sialylated proteins and lipids in the plasma membrane of eukaryotic host cells

Cationic antimicrobial peptides (CAMPs) selectively target bacterial membranes by electrostatic interactions with negatively charged lipids. It turned out that for inhibition of microbial growth a high CAMP membrane concentration is required, which can be realized by the incorporation of hydrophobic...

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Autores principales: Weghuber, Julian, Aichinger, Michael C., Brameshuber, Mario, Wieser, Stefan, Ruprecht, Verena, Plochberger, Birgit, Madl, Josef, Horner, Andreas, Reipert, Siegfried, Lohner, Karl, Henics, Tamás, Schütz, Gerhard J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier Pub. Co 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3161180/
https://www.ncbi.nlm.nih.gov/pubmed/21718688
http://dx.doi.org/10.1016/j.bbamem.2011.06.007
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author Weghuber, Julian
Aichinger, Michael C.
Brameshuber, Mario
Wieser, Stefan
Ruprecht, Verena
Plochberger, Birgit
Madl, Josef
Horner, Andreas
Reipert, Siegfried
Lohner, Karl
Henics, Tamás
Schütz, Gerhard J.
author_facet Weghuber, Julian
Aichinger, Michael C.
Brameshuber, Mario
Wieser, Stefan
Ruprecht, Verena
Plochberger, Birgit
Madl, Josef
Horner, Andreas
Reipert, Siegfried
Lohner, Karl
Henics, Tamás
Schütz, Gerhard J.
author_sort Weghuber, Julian
collection PubMed
description Cationic antimicrobial peptides (CAMPs) selectively target bacterial membranes by electrostatic interactions with negatively charged lipids. It turned out that for inhibition of microbial growth a high CAMP membrane concentration is required, which can be realized by the incorporation of hydrophobic groups within the peptide. Increasing hydrophobicity, however, reduces the CAMP selectivity for bacterial over eukaryotic host membranes, thereby causing the risk of detrimental side-effects. In this study we addressed how cationic amphipathic peptides—in particular a CAMP with Lysine–Leucine–Lysine repeats (termed KLK)—affect the localization and dynamics of molecules in eukaryotic membranes. We found KLK to selectively inhibit the endocytosis of a subgroup of membrane proteins and lipids by electrostatically interacting with negatively charged sialic acid moieties. Ultrastructural characterization revealed the formation of membrane invaginations representing fission or fusion intermediates, in which the sialylated proteins and lipids were immobilized. Experiments on structurally different cationic amphipathic peptides (KLK, 6-MO-LF11-322 and NK14-2) indicated a cooperation of electrostatic and hydrophobic forces that selectively arrest sialylated membrane constituents.
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spelling pubmed-31611802011-10-01 Cationic amphipathic peptides accumulate sialylated proteins and lipids in the plasma membrane of eukaryotic host cells Weghuber, Julian Aichinger, Michael C. Brameshuber, Mario Wieser, Stefan Ruprecht, Verena Plochberger, Birgit Madl, Josef Horner, Andreas Reipert, Siegfried Lohner, Karl Henics, Tamás Schütz, Gerhard J. Biochim Biophys Acta Article Cationic antimicrobial peptides (CAMPs) selectively target bacterial membranes by electrostatic interactions with negatively charged lipids. It turned out that for inhibition of microbial growth a high CAMP membrane concentration is required, which can be realized by the incorporation of hydrophobic groups within the peptide. Increasing hydrophobicity, however, reduces the CAMP selectivity for bacterial over eukaryotic host membranes, thereby causing the risk of detrimental side-effects. In this study we addressed how cationic amphipathic peptides—in particular a CAMP with Lysine–Leucine–Lysine repeats (termed KLK)—affect the localization and dynamics of molecules in eukaryotic membranes. We found KLK to selectively inhibit the endocytosis of a subgroup of membrane proteins and lipids by electrostatically interacting with negatively charged sialic acid moieties. Ultrastructural characterization revealed the formation of membrane invaginations representing fission or fusion intermediates, in which the sialylated proteins and lipids were immobilized. Experiments on structurally different cationic amphipathic peptides (KLK, 6-MO-LF11-322 and NK14-2) indicated a cooperation of electrostatic and hydrophobic forces that selectively arrest sialylated membrane constituents. Elsevier Pub. Co 2011-10 /pmc/articles/PMC3161180/ /pubmed/21718688 http://dx.doi.org/10.1016/j.bbamem.2011.06.007 Text en © 2011 Elsevier B.V. https://creativecommons.org/licenses/by-nc-nd/3.0/ Open Access under CC BY-NC-ND 3.0 (https://creativecommons.org/licenses/by-nc-nd/3.0/) license
spellingShingle Article
Weghuber, Julian
Aichinger, Michael C.
Brameshuber, Mario
Wieser, Stefan
Ruprecht, Verena
Plochberger, Birgit
Madl, Josef
Horner, Andreas
Reipert, Siegfried
Lohner, Karl
Henics, Tamás
Schütz, Gerhard J.
Cationic amphipathic peptides accumulate sialylated proteins and lipids in the plasma membrane of eukaryotic host cells
title Cationic amphipathic peptides accumulate sialylated proteins and lipids in the plasma membrane of eukaryotic host cells
title_full Cationic amphipathic peptides accumulate sialylated proteins and lipids in the plasma membrane of eukaryotic host cells
title_fullStr Cationic amphipathic peptides accumulate sialylated proteins and lipids in the plasma membrane of eukaryotic host cells
title_full_unstemmed Cationic amphipathic peptides accumulate sialylated proteins and lipids in the plasma membrane of eukaryotic host cells
title_short Cationic amphipathic peptides accumulate sialylated proteins and lipids in the plasma membrane of eukaryotic host cells
title_sort cationic amphipathic peptides accumulate sialylated proteins and lipids in the plasma membrane of eukaryotic host cells
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3161180/
https://www.ncbi.nlm.nih.gov/pubmed/21718688
http://dx.doi.org/10.1016/j.bbamem.2011.06.007
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