[en] A new technique associating the detergent Sodium Dodecyl Sulphate (SDS) and an alcohol-type co-solvent has been set up, showing an unexpected efficiency to refold several types of soluble or membrane proteins. The present contribution deepens the fundamental knowledge on the phenomena underlying this process, considering the refolding of two model peptides featuring the main protein secondary structures: alpha-helix and beta-sheet. Their refolding was monitored by fluorescence and circular dichroism, and it turns out that: (i) 100% recovery of the folded structure is observed for both peptides, (ii) the highest the SDS concentration, the more co-solvent to be added to recover the peptides' native structures, (iii) a high alcohol concentration is required to alter the SDS denaturing properties, (iv) the co-solvent performance relies on its specific lipophilic-hydrophilic balanced character, (v) the size of the micelle formed by the detergent does not enter the process critical parameters, and (vi) increasing the salt concentration up to 1 M NaCl has a beneficial impact on the process efficiency. These mechanistic aspects will help us to improve the method and extend its application. Copyright (c) 2016 European Peptide Society and John Wiley & Sons, Ltd.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Michaux, Catherine; Université de Namur
Roussel, Guillaume; Université de Namur - UNamur
Lopes-Rogrigues, M.; Université de Namur - UNamur
Matagne, André ; Université de Liège > Département des sciences de la vie > Enzymologie et repliement des protéines
Perpète, Eric; Université de Namur - UNamur
Language :
English
Title :
Unravelling the mechanisms of a protein refolding process based on the association of detergents and co-solvents.
Publication date :
2016
Journal title :
Journal of Peptide Science
ISSN :
1075-2617
eISSN :
1099-1387
Publisher :
John Wiley & Sons, Hoboken, United States - New Jersey
Peer reviewed :
Peer Reviewed verified by ORBi
Commentary :
Copyright (c) 2016 European Peptide Society and John Wiley & Sons, Ltd.
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