Peptide-surfactant interactions: A combined spectroscopic and molecular dynamics simulation approach

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Résumé

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.

langueAnglais
Pages464-470
Nombre de pages7
journalSpectrochimica acta Part A-Molecular and Biomolecular Spectroscopy
Volume190
Les DOIs
étatPublié - 5 févr. 2018

Empreinte digitale

peptides
surfactants
molecular dynamics
simulation
interactions
Surface-Active Agents
Molecular dynamics
Peptides
Computer simulation
Surface active agents
helices
Agglomeration
detergents
amino acids
micelles
salts
proteins
molecules
Micelles
Detergents

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    title = "Peptide-surfactant interactions: A combined spectroscopic and molecular dynamics simulation approach",
    abstract = "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.",
    keywords = "Molecular dynamics, Peptides, SDS, Spectroscopy, Surfactant",
    author = "Guillaume Roussel and Yves Caudano and André Matagne and Sansom, {Mark S.} and Perpète, {Eric A.} and Catherine Michaux",
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    AU - Roussel,Guillaume

    AU - Caudano,Yves

    AU - Matagne,André

    AU - Sansom,Mark S.

    AU - Perpète,Eric A.

    AU - Michaux,Catherine

    PY - 2018/2/5

    Y1 - 2018/2/5

    N2 - 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.

    AB - 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.

    KW - Molecular dynamics

    KW - Peptides

    KW - SDS

    KW - Spectroscopy

    KW - Surfactant

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    U2 - 10.1016/j.saa.2017.09.056

    DO - 10.1016/j.saa.2017.09.056

    M3 - Article

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    JO - Spectrochimica acta Part A-Molecular and Biomolecular Spectroscopy

    T2 - Spectrochimica acta Part A-Molecular and Biomolecular Spectroscopy

    JF - Spectrochimica acta Part A-Molecular and Biomolecular Spectroscopy

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