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X-ray reflectivity study of the heat shock protein Hsp70 interaction with an artificial cell membrane model

Membrane-bound heat shock protein 70 (Hsp70) apart from its intracellular localization was shown to be specifically expressed on the plasma membrane surface of tumor but not normal cells. Although the association of Hsp70 with lipid membranes is well documented the exact mechanisms for chaperone mem...

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Autores principales: Makky, Ali, Czajor, Julian, Konovalov, Oleg, Zhakhov, Alexander, Ischenko, Alexander, Behl, Ankita, Singh, Shailja, Abuillan, Wasim, Shevtsov, Maxim
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10628213/
https://www.ncbi.nlm.nih.gov/pubmed/37932378
http://dx.doi.org/10.1038/s41598-023-46066-3
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author Makky, Ali
Czajor, Julian
Konovalov, Oleg
Zhakhov, Alexander
Ischenko, Alexander
Behl, Ankita
Singh, Shailja
Abuillan, Wasim
Shevtsov, Maxim
author_facet Makky, Ali
Czajor, Julian
Konovalov, Oleg
Zhakhov, Alexander
Ischenko, Alexander
Behl, Ankita
Singh, Shailja
Abuillan, Wasim
Shevtsov, Maxim
author_sort Makky, Ali
collection PubMed
description Membrane-bound heat shock protein 70 (Hsp70) apart from its intracellular localization was shown to be specifically expressed on the plasma membrane surface of tumor but not normal cells. Although the association of Hsp70 with lipid membranes is well documented the exact mechanisms for chaperone membrane anchoring have not been fully elucidated. Herein, we addressed the question of how Hsp70 interacts with negatively charged phospholipids in artificial lipid compositions employing the X-ray reflectivity (XRR) studies. In a first step, the interactions between dioleoylphosphatidylcholine (DOPC) in the presence or absence of dioleoylphosphatidylserine (DOPS) and Hsp70 had been assessed using Quartz crystal microbalance measurements, suggesting that Hsp70 adsorbs to the surface of DOPC/DOPS bilayer. Atomic force microscopy (AFM) imaging demonstrated that the presence of DOPS is required for stabilization of the lipid bilayer. The interaction of Hsp70 with DOPC/DOPS lipid compositions was further quantitatively determined by high energy X-ray reflectivity. A systematic characterization of the chaperone-lipid membrane interactions by various techniques revealed that artificial membranes can be stabilized by the electrostatic interaction of anionic DOPS lipids with Hsp70.
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spelling pubmed-106282132023-11-08 X-ray reflectivity study of the heat shock protein Hsp70 interaction with an artificial cell membrane model Makky, Ali Czajor, Julian Konovalov, Oleg Zhakhov, Alexander Ischenko, Alexander Behl, Ankita Singh, Shailja Abuillan, Wasim Shevtsov, Maxim Sci Rep Article Membrane-bound heat shock protein 70 (Hsp70) apart from its intracellular localization was shown to be specifically expressed on the plasma membrane surface of tumor but not normal cells. Although the association of Hsp70 with lipid membranes is well documented the exact mechanisms for chaperone membrane anchoring have not been fully elucidated. Herein, we addressed the question of how Hsp70 interacts with negatively charged phospholipids in artificial lipid compositions employing the X-ray reflectivity (XRR) studies. In a first step, the interactions between dioleoylphosphatidylcholine (DOPC) in the presence or absence of dioleoylphosphatidylserine (DOPS) and Hsp70 had been assessed using Quartz crystal microbalance measurements, suggesting that Hsp70 adsorbs to the surface of DOPC/DOPS bilayer. Atomic force microscopy (AFM) imaging demonstrated that the presence of DOPS is required for stabilization of the lipid bilayer. The interaction of Hsp70 with DOPC/DOPS lipid compositions was further quantitatively determined by high energy X-ray reflectivity. A systematic characterization of the chaperone-lipid membrane interactions by various techniques revealed that artificial membranes can be stabilized by the electrostatic interaction of anionic DOPS lipids with Hsp70. Nature Publishing Group UK 2023-11-06 /pmc/articles/PMC10628213/ /pubmed/37932378 http://dx.doi.org/10.1038/s41598-023-46066-3 Text en © The Author(s) 2023 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Article
Makky, Ali
Czajor, Julian
Konovalov, Oleg
Zhakhov, Alexander
Ischenko, Alexander
Behl, Ankita
Singh, Shailja
Abuillan, Wasim
Shevtsov, Maxim
X-ray reflectivity study of the heat shock protein Hsp70 interaction with an artificial cell membrane model
title X-ray reflectivity study of the heat shock protein Hsp70 interaction with an artificial cell membrane model
title_full X-ray reflectivity study of the heat shock protein Hsp70 interaction with an artificial cell membrane model
title_fullStr X-ray reflectivity study of the heat shock protein Hsp70 interaction with an artificial cell membrane model
title_full_unstemmed X-ray reflectivity study of the heat shock protein Hsp70 interaction with an artificial cell membrane model
title_short X-ray reflectivity study of the heat shock protein Hsp70 interaction with an artificial cell membrane model
title_sort x-ray reflectivity study of the heat shock protein hsp70 interaction with an artificial cell membrane model
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10628213/
https://www.ncbi.nlm.nih.gov/pubmed/37932378
http://dx.doi.org/10.1038/s41598-023-46066-3
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