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.
| langue | Anglais |
|---|---|
| Pages | 464-470 |
| Nombre de pages | 7 |
| journal | Spectrochimica acta Part A-Molecular and Biomolecular Spectroscopy |
| Volume | 190 |
| Les DOIs | |
| état | Publié - 5 févr. 2018 |
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Peptide-surfactant interactions: A combined spectroscopic and molecular dynamics simulation approach. / Roussel, Guillaume; Caudano, Yves; Matagne, André; Sansom, Mark S.; Perpète, Eric A.; Michaux, Catherine.
Dans: Spectrochimica acta Part A-Molecular and Biomolecular Spectroscopy, Vol 190, 05.02.2018, p. 464-470.Résultats de recherche: Contribution à un journal/une revue › Article
TY - JOUR
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
UR - http://www.scopus.com/inward/record.url?scp=85029798264&partnerID=8YFLogxK
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
T2 - Spectrochimica acta Part A-Molecular and Biomolecular Spectroscopy
JF - Spectrochimica acta Part A-Molecular and Biomolecular Spectroscopy
SN - 1386-1425
ER -