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.
Highlights
Protein-surfactant systems have potential applications in wide range of industrial aspects, including the following: drug delivery, cosmetics, food industry and preparation of pharmaceutical substances, as well as in biotechnology and biosciences [1,2,3]
The aim of our work was to find out the characteristics of interactions between model proteins (BSA and hen egg white lysozyme (HEWL)) and two novel gemini surfactants: 3,3′-[1,8-(2,7dioxaoctane)]bis(1-dodecylimidazolium) chloride and 3,3′-[1,12-(2,11-dioxadodecane)]bis(1dodecylimidazolium) chloride
The study revealed a strong impact of both gemini surfactants on bovine serum albumin (BSA) molecule
Summary
Protein-surfactant systems have potential applications in wide range of industrial aspects, including the following: drug delivery, cosmetics, food industry and preparation of pharmaceutical substances, as well as in biotechnology and biosciences [1,2,3]. Proteins are known to attach diverse surfactant molecules, giving protein-surfactant complexes, where hydrophobic parts of surfactant molecules tend to bind interior hydrophobic residues of proteins [5]. Studying these phenomena can help in understanding the effect of surfactants on protein denaturation, solubilisation and renaturation processes [6, 7]. A very important phenomenon is protein aggregation, which can be responsible for many serious human diseases (including number of neurodegenerative diseases) and it is often regarded as undesired effect in biotechnology [8,9,10]. Its molecular mechanism is still not entirely deciphered and poses challenge [11]
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