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Morphology, Biophysical Properties and Protein-Mediated Fusion of Archaeosomes

As variance from standard phospholipids of eubacteria and eukaryotes, archaebacterial diether phospholipids contain branched alcohol chains (phytanol) linked to glycerol exclusively with ether bonds. Giant vesicles (GVs) constituted of different species of archaebacterial diether phospholipids and g...

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Autores principales: Šuštar, Vid, Zelko, Jasna, Lopalco, Patrizia, Lobasso, Simona, Ota, Ajda, Ulrih, Nataša Poklar, Corcelli, Angela, Kralj-Iglič, Veronika
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3391208/
https://www.ncbi.nlm.nih.gov/pubmed/22792173
http://dx.doi.org/10.1371/journal.pone.0039401
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author Šuštar, Vid
Zelko, Jasna
Lopalco, Patrizia
Lobasso, Simona
Ota, Ajda
Ulrih, Nataša Poklar
Corcelli, Angela
Kralj-Iglič, Veronika
author_facet Šuštar, Vid
Zelko, Jasna
Lopalco, Patrizia
Lobasso, Simona
Ota, Ajda
Ulrih, Nataša Poklar
Corcelli, Angela
Kralj-Iglič, Veronika
author_sort Šuštar, Vid
collection PubMed
description As variance from standard phospholipids of eubacteria and eukaryotes, archaebacterial diether phospholipids contain branched alcohol chains (phytanol) linked to glycerol exclusively with ether bonds. Giant vesicles (GVs) constituted of different species of archaebacterial diether phospholipids and glycolipids (archaeosomes) were prepared by electroformation and observed under a phase contrast and/or fluorescence microscope. Archaebacterial lipids and different mixtures of archaebacterial and standard lipids formed GVs which were analysed for size, yield and ability to adhere to each other due to the mediating effects of certain plasma proteins. GVs constituted of different proportions of archaeal or standard phosphatidylcholine were compared. In nonarchaebacterial GVs (in form of multilamellar lipid vesicles, MLVs) the main transition was detected at T(m) = 34. 2°C with an enthalpy of ΔH = 0.68 kcal/mol, whereas in archaebacterial GVs (MLVs) we did not observe the main phase transition in the range between 10 and 70°C. GVs constituted of archaebacterial lipids were subject to attractive interaction mediated by beta 2 glycoprotein I and by heparin. The adhesion constant of beta 2 glycoprotein I – mediated adhesion determined from adhesion angle between adhered GVs was in the range of 10(−8) J/m(2). In the course of protein mediated adhesion, lateral segregation of the membrane components and presence of thin tubular membranous structures were observed. The ability of archaebacterial diether lipids to combine with standard lipids in bilayers and their compatibility with adhesion-mediating molecules offer further evidence that archaebacterial lipids are appropriate for the design of drug carriers.
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spelling pubmed-33912082012-07-12 Morphology, Biophysical Properties and Protein-Mediated Fusion of Archaeosomes Šuštar, Vid Zelko, Jasna Lopalco, Patrizia Lobasso, Simona Ota, Ajda Ulrih, Nataša Poklar Corcelli, Angela Kralj-Iglič, Veronika PLoS One Research Article As variance from standard phospholipids of eubacteria and eukaryotes, archaebacterial diether phospholipids contain branched alcohol chains (phytanol) linked to glycerol exclusively with ether bonds. Giant vesicles (GVs) constituted of different species of archaebacterial diether phospholipids and glycolipids (archaeosomes) were prepared by electroformation and observed under a phase contrast and/or fluorescence microscope. Archaebacterial lipids and different mixtures of archaebacterial and standard lipids formed GVs which were analysed for size, yield and ability to adhere to each other due to the mediating effects of certain plasma proteins. GVs constituted of different proportions of archaeal or standard phosphatidylcholine were compared. In nonarchaebacterial GVs (in form of multilamellar lipid vesicles, MLVs) the main transition was detected at T(m) = 34. 2°C with an enthalpy of ΔH = 0.68 kcal/mol, whereas in archaebacterial GVs (MLVs) we did not observe the main phase transition in the range between 10 and 70°C. GVs constituted of archaebacterial lipids were subject to attractive interaction mediated by beta 2 glycoprotein I and by heparin. The adhesion constant of beta 2 glycoprotein I – mediated adhesion determined from adhesion angle between adhered GVs was in the range of 10(−8) J/m(2). In the course of protein mediated adhesion, lateral segregation of the membrane components and presence of thin tubular membranous structures were observed. The ability of archaebacterial diether lipids to combine with standard lipids in bilayers and their compatibility with adhesion-mediating molecules offer further evidence that archaebacterial lipids are appropriate for the design of drug carriers. Public Library of Science 2012-07-06 /pmc/articles/PMC3391208/ /pubmed/22792173 http://dx.doi.org/10.1371/journal.pone.0039401 Text en Šuštar et al. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Šuštar, Vid
Zelko, Jasna
Lopalco, Patrizia
Lobasso, Simona
Ota, Ajda
Ulrih, Nataša Poklar
Corcelli, Angela
Kralj-Iglič, Veronika
Morphology, Biophysical Properties and Protein-Mediated Fusion of Archaeosomes
title Morphology, Biophysical Properties and Protein-Mediated Fusion of Archaeosomes
title_full Morphology, Biophysical Properties and Protein-Mediated Fusion of Archaeosomes
title_fullStr Morphology, Biophysical Properties and Protein-Mediated Fusion of Archaeosomes
title_full_unstemmed Morphology, Biophysical Properties and Protein-Mediated Fusion of Archaeosomes
title_short Morphology, Biophysical Properties and Protein-Mediated Fusion of Archaeosomes
title_sort morphology, biophysical properties and protein-mediated fusion of archaeosomes
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3391208/
https://www.ncbi.nlm.nih.gov/pubmed/22792173
http://dx.doi.org/10.1371/journal.pone.0039401
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