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Interaction of two imidazolium gemini surfactants with two model proteins BSA and HEWL
Gemini surfactants and their interactions with proteins have gained considerable scientific interest, especially when amyloidogenic proteins are taken into account. In this work, the influence of two selected dicationic (gemini) surfactants (3,3′-[1,8-(2,7-dioxaoctane)]bis(1-dodecylimidazolium) chlo...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer Berlin Heidelberg
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4575695/ https://www.ncbi.nlm.nih.gov/pubmed/26412930 http://dx.doi.org/10.1007/s00396-015-3671-z |
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author | Gospodarczyk, W. Kozak, M. |
author_facet | Gospodarczyk, W. Kozak, M. |
author_sort | Gospodarczyk, W. |
collection | PubMed |
description | Gemini surfactants and their interactions with proteins have gained considerable scientific interest, especially when amyloidogenic proteins are taken into account. In this work, the influence of two selected dicationic (gemini) surfactants (3,3′-[1,8-(2,7-dioxaoctane)]bis(1-dodecylimidazolium) chloride and 3,3′-[1,12-(2,11-dioxadodecane)]bis(1-dodecylimidazolium) chloride) on two model proteins, bovine serum albumin (BSA) and hen egg white lysozyme (HEWL), have been investigated. A pronounced and sophisticated influence on BSA structure has been revealed, including a considerable change of protein radius of gyration as well as substantial alteration of its secondary structure. Radius of gyration has been found to rise significantly with addition of surfactants and to fall down for high surfactants concentration. Similarly, a remarkable fall of secondary structure (α-helix content) has been observed, followed by its partial retrieval for high surfactants concentration. A strong aggregation of BSA has been observed for a confined range of surfactants concentrations as well. In case of HEWL-gemini system, on the other hand, the protein-surfactant interaction was found to be weak. Molecular mechanisms explaining such behaviour of protein-surfactant systems have been proposed. The differences of properties of both studied surfactants have also been discussed. |
format | Online Article Text |
id | pubmed-4575695 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Springer Berlin Heidelberg |
record_format | MEDLINE/PubMed |
spelling | pubmed-45756952015-09-24 Interaction of two imidazolium gemini surfactants with two model proteins BSA and HEWL Gospodarczyk, W. Kozak, M. Colloid Polym Sci Original Contribution Gemini surfactants and their interactions with proteins have gained considerable scientific interest, especially when amyloidogenic proteins are taken into account. In this work, the influence of two selected dicationic (gemini) surfactants (3,3′-[1,8-(2,7-dioxaoctane)]bis(1-dodecylimidazolium) chloride and 3,3′-[1,12-(2,11-dioxadodecane)]bis(1-dodecylimidazolium) chloride) on two model proteins, bovine serum albumin (BSA) and hen egg white lysozyme (HEWL), have been investigated. A pronounced and sophisticated influence on BSA structure has been revealed, including a considerable change of protein radius of gyration as well as substantial alteration of its secondary structure. Radius of gyration has been found to rise significantly with addition of surfactants and to fall down for high surfactants concentration. Similarly, a remarkable fall of secondary structure (α-helix content) has been observed, followed by its partial retrieval for high surfactants concentration. A strong aggregation of BSA has been observed for a confined range of surfactants concentrations as well. In case of HEWL-gemini system, on the other hand, the protein-surfactant interaction was found to be weak. Molecular mechanisms explaining such behaviour of protein-surfactant systems have been proposed. The differences of properties of both studied surfactants have also been discussed. Springer Berlin Heidelberg 2015-07-08 2015 /pmc/articles/PMC4575695/ /pubmed/26412930 http://dx.doi.org/10.1007/s00396-015-3671-z Text en © The Author(s) 2015 Open Access This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. |
spellingShingle | Original Contribution Gospodarczyk, W. Kozak, M. Interaction of two imidazolium gemini surfactants with two model proteins BSA and HEWL |
title | Interaction of two imidazolium gemini surfactants with two model proteins BSA and HEWL |
title_full | Interaction of two imidazolium gemini surfactants with two model proteins BSA and HEWL |
title_fullStr | Interaction of two imidazolium gemini surfactants with two model proteins BSA and HEWL |
title_full_unstemmed | Interaction of two imidazolium gemini surfactants with two model proteins BSA and HEWL |
title_short | Interaction of two imidazolium gemini surfactants with two model proteins BSA and HEWL |
title_sort | interaction of two imidazolium gemini surfactants with two model proteins bsa and hewl |
topic | Original Contribution |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4575695/ https://www.ncbi.nlm.nih.gov/pubmed/26412930 http://dx.doi.org/10.1007/s00396-015-3671-z |
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