Mechanism of Gemini Disulfide Detergent Mediated Oxidative Refolding of Lysozyme in a New Artificial Chaperone System |
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Authors: | Marc Potempa Mathias Hafner Christian Frech |
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Institution: | (1) Institute for Biochemistry, University of Applied Sciences, Mannheim, Germany;(2) Institute of Molecular Biology and Cell Culture Technology, University of Applied Sciences, Mannheim, Germany; |
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Abstract: | Gemini surfactants are a new class of surfactants that consist of two hydrophilic head groups and two hydrophobic tails separated
by a spacer group. As the properties of geminis are different to their monomeric counterparts, a large number of applications
have been investigated. Here we report on the use of a new class of gemini detergents containing a disulfide bond in the spacer
(Det-SS-Det) for protein refolding. Using lysozyme as a model protein we could demonstrate that the disulfide gemini detergents
allow oxidative refolding of the protein in the absence of any external redox system in an “artificial chaperone system”.
Refolding kinetics using gemini disulfide detergents differing in their hydrophobicity were analysed to determine the folding
and aggregation rate constants. The results point to an important role of the transiently formed mixed disulfides between
the protein and the detergent (Prot-SS-Det) in the oxidative refolding process of lysozyme. |
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