ArticleColloid and polymer science
Interaction of two imidazolium gemini surfactants with two model proteins BSA and HEWL.
Article in Colloid and polymer science. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Gemini Surfactants: Advances in Applications and Prospects for the Future.Molecules (Basel, Switzerland) · 2025Review
- Do Ionic Liquids Exhibit the Required Characteristics to Dissolve, Extract, Stabilize, and Purify Proteins? Past-Present-Future Assessment.Chemical reviews · 2024Review
- A Systematic Approach: Molecular Dynamics Study and Parametrisation of Gemini Type Cationic Surfactants.International journal of molecular sciences · 2021Article
- Molecular Interaction of Amino Acid-Based Gemini Surfactant with Human Serum Albumin: Tensiometric, Spectroscopic, and Molecular Docking Study.ACS omega · 2019Article
- Aggregation and conformational stability evaluation of myoglobin in the presence of ionic surfactant.Saudi pharmaceutical journal : SPJ : the official publication of the Saudi Pharmaceutical Society · 2018Article
- Anticancer Drug Camptothecin Test in 3D Hydrogel Networks with HeLa cells.Scientific reports · 2017Article
Corrections and comments
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Authors and funding
2 authors.
Funding
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Abstract
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.
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