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

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

Abstract :

[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.

Disciplines :

Biochemistry, biophysics & molecular biology

Author, co-author :

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 ; 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

Title :

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

Publication date :

2018

Journal title :

Spectrochimica Acta. Part A, Molecular and Biomolecular Spectroscopy

ISSN :

1386-1425

Publisher :

Elsevier B.V.

Volume :

190

Pages :

464-470

Peer reviewed :

Peer Reviewed verified by ORBi

Funders :

F.R.S.-FNRS - Fonds de la Recherche Scientifique [BE]
UNamur - Université de Namur [BE]

Available on ORBi :

since 13 February 2018

Statistics

Number of views

74 (8 by ULiège)

Number of downloads

5 (5 by ULiège)

More statistics

Scopus citations^®

Scopus citations^®
without self-citations

OpenCitations

Bibliography

Andersen, K.K., Oliveira, C.L., Larsen, K.L., Poulsen, F.M., Callisen, T.H., Westh, P., Pedersen, J.S., Otzen, D., J. Mol. Biol. 391 (2009), 207–226.
Barth, A., Biochim. Biophys. Acta 1767 (2007), 1073–1101.
Bennion, B.J., Daggett, V., Proc. Natl. Acad. Sci. U. S. A. 100 (2003), 5142–5147.
Berendsen, H.J.C., Postma, J.P.M., van Gunsteren, W.F., DiNola, A., Haak, J.R., J. Chem. Phys. 81 (1984), 3684–3690.
Bhairi, S.M., A Guide to the Properties and Uses of Detergents in Biology and Biochemistry San Diego, CA. 2001.
Bhuyan, A., Biopolymers 93 (2010), 186–199.
Chamani, J., J. Colloid Interface Sci. 299 (2006), 636–646.
Chamani, J., Moosavi-Movahedi, A.A., Rajabi, O., Gharanfoli, M., Momen-Heravi, M., Hakimelahi, G.H., Neamati-Baghsiah, A., Varasteh, A.R., J. Colloid Interface Sci. 293 (2006), 52–60.
Chen, J., Su, T., Mou, C.Y., J. Phys. Chem. 12 (1986), 2418–2421.
Cochran, A.G., Skelton, N.J., Starovasnik, M.A., Proc. Natl. Acad. Sci. U. S. A. 98 (2001), 5578–5583.
Darden, T., York, D., Pedersen, L., J. Chem. Phys., 98, 1993, 10089.
Daura, X., Mark, A.E., Van Gunsteren, W., J. Comput. Chem. 19 (1998), 535–547.
Day, R., Paschek, D., Garcia, A.E., Proteins 78 (2010), 1889–1899.
Dempsey, C.E., Piggot, T.J., Mason, P.E., Biochemistry 44 (2005), 775–781.
Gudiksen, K.L., Gitlin, I., Whitesides, G.M., Proc. Natl. Acad. Sci. U. S. A. 103 (2006), 7968–7972.
Hayashi, S., Ikeda, S., J. Phys. Chem. 84 (1980), 744–751.
Hess, B., Kutzner, C., van der Spoel, D., Lindahl, E., J. Theory Comput. 4 (2008), 435–447.
Heyda, J., Ko, M., Bedn, L., Thompson, G., Konvalinka, J., Jungwirth, P., J. Phys. Chem. B 115 (2011), 8910–8924.
Huang, R., Wu, L., McElheny, D., Bour, P., Roy, A., Keiderling, T.A., J. Phys. Chem. B 113 (2009), 5661–5674.
Hudaky, P., Straner, P., Farkas, V., Varadi, G., Toth, G., Perczel, A., Biochemistry 47 (2008), 1007–1016.
Humphrey, W., Dalke, A., Schulten, K., J. Mol. Graph. 14 (1996), 33–38.
Iavarone, A.T., Parks, J.H., J. Am. Chem. Soc. 127 (2005), 8606–8607.
Iavarone, A.T., Patriksson, A., van der Spoel, D., Parks, J.H., J. Am. Chem. Soc. 129 (2007), 6726–6735.
Jain, N., Trabelsi, S., Guillot, S., McLoughlin, D., Langevin, D., Letellier, P., Turmine, M., Langmuir 20 (2004), 8496–8503.
Kong, J., Yu, S., Acta Biochim. Biophys. 39 (2007), 549–559.
Langham, A.A., Waring, A.J., Kaznessis, Y.N., BMC Biochem., 8, 2007, 11.
Manning, M., Colon, W., Biochemistry 43 (2004), 11248–11254.
Mattice, W.L., Riser, J.M., Clark, D.S., Biochemistry 15 (1976), 4264–4272.
McMillan, A.W., Kier, B.L., Shu, I., Byrne, A., Andersen, N.H., Parson, W.W., J. Phys. Chem. B 117 (2013), 1790–1809.
Mei, Y., Wei, C., Yip, Y.M., Ho, C.Y., Zhang, J.Z.H., Zhang, D., Theor. Chem. Accounts, 131, 2012, 1168.
Michaux, C., Roussel, G., Lopes-Rodrigues, M., Matagne, A., Perpète, E.A., J. Pept. Sci. 22 (2016), 485–491.
Mok, K.H., Kuhn, L.T., Goez, M., Day, I.J., Lin, J.C., Andersen, N.H., Hore, P.J., Nature 447 (2007), 106–109.
Muñoz, V., Ghirlando, R., Blanco, F.J., Jas, G.S., Hofrichter, J., Eaton, W.A., Biochemistry 45 (2006), 7023–7035.
Naidu, K.T., Prabhu, N.P., J. Phys. Chem. B 115 (2011), 14760–14767.
Neidigh, J.W., Fesinmeyer, R.M., Andersen, N.H., Nat. Struct. Biol. 9 (2002), 425–430.
Nielsen, M.M., Andersen, K.K., Westh, P., Otzen, D.E., Biophys. J. 92 (2007), 3674–3685.
Otzen, D.E., Biophys. J. 83 (2002), 2219–2230.
Otzen, D.E., Oliveberg, M., J. Mol. Biol. 315 (2002), 1231–1240.
Patil, S.M., Xu, S., Sheftic, S.R., Alexandrescu, A.T., J. Biol. Chem. 284 (2009), 11982–11991.
Roussel, G., Michaux, C., Perpete, E.A., J. Mol. Model., 20, 2014, 2469.
Roussel, G., Rouse, S.L., Sansom, M.S., Michaux, C., Perpete, E.A., Colloids Surf. B Biointerfaces, 114, 2014, 357.
Rovó, P., Farkas, V., Hegyi, O., Szolomájer-Csikós, O., Tóth, G.K., Perczel, A., J. Pept. Sci. 17 (2011), 610–619.
Schibli, D.J., Hwang, P.M., Vogel, H.J., Biochemistry 38 (1999), 16749–16755.
Schneider, G.F., Shaw, B.F., Lee, A., Carillho, E., George, M., J. Am. Chem. Soc. 130 (2008), 17384–17393.
Seshasayee, A.S.N., Theor. Biol. Med. Model., 2, 2005, 7.
Settanni, G., Fersht, A.R., Biophys. J. 94 (2008), 4444–4453.
Shaw, B.F., Schneider, G.F., Arthanari, H., Narovlyansky, M., Moustakas, D., Durazo, A., Wagner, G., Whitesides, G.M., J. Am. Chem. Soc. 133 (2011), 17681–17695.
Streicher, W.W., Makhatadze, G.I., Biochemistry 46 (2007), 2876–2880.
Takekiyo, T., Wu, L., Yoshiruma, Y., Shimizu, A., Keiderling, T.A., Biochemistry 48 (2009), 1543–1552.
Tian, J., Sethi, A., Anunciado, D., Vu, D.M., Gnanakaran, S., J. Phys. Chem. B 116 (2012), 4417–4424.
Turro, N.J., Lei, X., Langmuir 11 (1995), 2525–2533.
Wafer, L.N.R., Streicher, W.W., Makhatadze, G.I., Proteins 78 (2010), 1376–1381.
Wei, S.Y., Wu, J.M., Kuo, Y.Y., Chen, H.L., Yip, B.S., Tzeng, S.R., Cheng, J.W., J. Bacteriol. 188 (2006), 328–334.
Wu, L., McElheny, D., Huang, R., Keiderling, T.A., Biochemistry 48 (2009), 10362–10371.
Wu, L., McElheny, D., Takekiyo, T., Keiderling, T.A., Biochemistry 49 (2010), 4705–4714.
Xu, Y., Oyola, R., Gai, F., J. Chem. Soc. 9 (2003), 15388–15394.
Yang, W.Y., Pitera, J.W., Swope, W.C., Gruebele, M., J. Mol. Biol. 336 (2004), 241–251.
Zhou, R., Proc. Natl. Acad. Sci. U. S. A. 100 (2003), 13280–13285.