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

Research output: Contribution to journalArticle

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.

Original languageEnglish
Pages (from-to)464-470
Number of pages7
JournalSpectrochimica acta Part A-Molecular and Biomolecular Spectroscopy
Volume190
DOIs
Publication statusPublished - 5 Feb 2018

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

Keywords

  • Molecular dynamics
  • Peptides
  • SDS
  • Spectroscopy
  • Surfactant

Cite this

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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 Andr{\'e} Matagne and Sansom, {Mark S.} and Perp{\`e}te, {Eric A.} and Catherine Michaux",
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T1 - Peptide-surfactant interactions: A combined spectroscopic and molecular dynamics simulation approach

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

VL - 190

SP - 464

EP - 470

JO - Spectrochimica acta Part A-Molecular and Biomolecular Spectroscopy

JF - Spectrochimica acta Part A-Molecular and Biomolecular Spectroscopy

SN - 1386-1425

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