Reference : Peptide-surfactant interactions: A combined spectroscopic and molecular dynamics simu...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
Peptide-surfactant interactions: A combined spectroscopic and molecular dynamics simulation approach
Roussel, G. [Department of Physiology and Biophysics, University of California, D340 Medical Sciences I, Irvine, CA, United States]
Caudano, Y. [Research Centre in Physics of Matter and Radiation (PMR), University of Namur, 61 Rue de Bruxelles, Namur, Belgium]
Matagne, André mailto [Université de Liège - ULiège > Département des sciences de la vie > Enzymologie et repliement des protéines >]
Sansom, M. S. [Department of Biochemistry, University of Oxford, South Park Road, Oxford, United Kingdom]
Perpète, E. A. [Laboratory of Physical Chemistry of Biomolecules, Unité de Chimie Physique Théorique et Structurale (UCPTS), University of Namur, 61, Rue de Bruxelles, Namur, Belgium]
Michaux, Charles [Université de Liège - ULiège > Département des productions animales (DPA) > Nutrition des animaux domestiques >]
Spectrochimica Acta. Part A, Molecular and Biomolecular Spectroscopy
Elsevier B.V.
Yes (verified by ORBi)
[en] Molecular dynamics ; Peptides ; SDS ; Spectroscopy ; Surfactant ; Dyes ; Proteins ; Surface active agents ; Computational approach ; Critical aggregation concentration ; Different mechanisms ; Molecular dynamics simulations ; Native structures ; Secondary structures ; Surfactant interaction ; Tertiary structures
[en] In the present contribution, we report a combined spectroscopic and computational approach aiming to unravel at atomic resolution the effect of the anionic SDS detergent on the structure of two model peptides, the α-helix TrpCage and the β-stranded TrpZip. A detailed characterization of the specific amino acids involved is performed. Monomeric (single molecules) and micellar SDS species differently interact with the α-helix and β-stranded peptides, emphasizing the different mechanisms occurring below and above the critical aggregation concentration (CAC). Below the CAC, the α-helix peptide is fully unfolded, losing its hydrophobic core and its Asp-Arg salt bridge, while the β-stranded peptide keeps its native structure with its four Trp well oriented. Above the CAC, the SDS micelles have the same effect on both peptides, that is, destabilizing the tertiary structure while keeping their secondary structure. Our studies will be helpful to deepen our understanding of the action of the denaturant SDS on peptides and proteins. © 2017 Elsevier B.V.
Université de Namur; Fonds De La Recherche Scientifique - FNRS

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