Publications récentes

    118. Potvin-Fournier, K., Valois-Paillard, G., Lefèvre, T., Cantin, L., Salesse, C., Auger, M. 2017. Membrane fluidity is a driving force for recoverin myristoyl immobilization in zwitterionic lipids, Biochem. Biophys. Res. Comm., 10.1016/j.bbrc.2017.07.005.
    117. Auger, M. 2017. Membrane solid-state in Canada: A historical perspective, Biochim. Biophys. Acta, 10.1016/j.bbapap.2017.06.019.
    116. Gagnon, M.-C., Strandberg, E., Grau-Campistany, A., Wadhwani, P., Reichert, J.; Bürck, J., Rabanal, F., Auger, M., Paquin, J.-F., Ulrich, A.S. 2017. Influence of length and charge on the activity of α-helical amphipathic antimicrobial peptides, Biochemistry, 56, 1680-1695.
    115. Fillion, M. Goudreault, M., Voyer, N., Bechinger, B., Auger, M., 2016. Amphiphilicity is a key determinant in the membrane interactions of synthetic 14-mer cationic peptide analogs, Biochemistry, 55, 6919-6930.
    114. Godbout, R., Légaré, S., Auger, M., Carpentier, C., Otis, F., Auger, M., Lagüe, P., Voyer, N., 2016. Membrane assembly and ion transport ability of a fluorinated nanopore, PLOS ONE, 11, E0166587.
    113. Duque, A. Gauthier, L., Simard, M., Jean, J., Gendreau, I., Morin, A., Auger, M., Soucy, J., Pouliot, R., 2016. A 3D-psoriatic skin model for dermatological testing: The impact of culture conditions, Biochem. Biophys. Rep., 8, 268-276.
    112. Dionne, J., Lefèvre, T., Auger, M., 2016. Major ampullate spider silk with indistinguishable spidroin dope conformations lead to different fiber molecular structures, Int. J. Molec. Sci., 17, E1353.
    111. Potvin-Fournier, K., Lefèvre, T., Picard-Lafond, A., Marcotte, C., Dufresne, C., Cantin, L., Salesse, C., Auger, M., 2016. Discriminating lipid- from protein-calcium binding to understand the interaction between recoverin and phosphatidylglycerol model membranes, Biochemistry, 55, 3481-3491.
    110. Lefèvre, T., Auger, M., 2016. Spider silk as a blueprint for greener materials: a review, Int. Mater. Rev., 61, 127-153.
    109. Lefèvre, T., Auger, M., 2016. Spider silk-inspired materials and sustainability: a perspective, Materials Technology: Advanced Performance Materials, 31, 384-399.
    108. Robert, E., Lefèvre, T., Fillion, M., Martial, B., Dionne, J., Auger, M., 2015. Mimicking and understanding the agglutination effect of the antimicrobial peptide thanatin using model phospholipid vesicles, Biochemistry,54, 3932–3941.
    107. Tremblay, M.-L., Xu, L., Lefèvre, T., Sarker, M., Orrell, K.E., Leclerc, J., Meng, Q., Pézolet, M., Auger, M., Liu, X.-Q., Rainey, J.K., 2015. Spider wrapping silk fibre architecture arising from its modular soluble protein precursor, Sci. Rep., DOI: 10.1038/srep11502.
    106. Leroy, M., Lefèvre, T., Pouliot, R., Auger, M., Laroche, G., 2015. Using infrared and Raman microspectroscopies to compare ex vivo involved psoriatic skin with normal human skin, J. Biomed. Opt., 20(6), 067004. DOI:10.1117/1.JBO.20.6.067004.
    105. Rhéault, J.-F., Gagné, E., Guertin, M., Lamoureux, G., Auger, M., Lagüe, P., 2015. Molecular model of hemoglobin N from Mycobacterium tuberculosis bound to lipid bilayers: a combined spectroscopic and computational study, Biochemistry, 54, 2073-2084.
    104. Huot, A., Lefèvre, T., Rioux-Dubé, J.-F., Nault, A.-P., Auger, M., Pézolet, M., 2015. Effect of mechanical deformation on the structure of regenerated B. mori silk fibroin films as revealed by Raman and infrared spectroscopy, Appl. Spectrosc., 69, 689-698.
    103. Ayata, R.E., Chabaud, S., Auger, M., Pouliot, R., 2015. Behaviour of endothelial cells in a tridimensional in vitro environment, Biomed. Res. Int., 630461, DOI: 10.1155/2015/630461.
    102. Fillion, M., Auger, M., 2015. Oriented samples: a tool for determining the membrane topology and the mechanism of action of cationic antimicrobial peptides by solid-state NMR, Biophys. Rev., DOI: 10.1007/s12551-015-0167-5.
    101. Proulx, M., Aubin, K., Lagueux, J., Audet, P., Auger, M., Fortin, M.-A., Fradette, J., 2015. Magnetic resonance imaging of human tissue-engineered adipose substitutes, Tissue Eng. Part. C., 21, 693-704.
    100. Fillion, M., Valois-Paillard, G., Lorin, A., Noël, M., Voyer, N., Auger, M., 2015. Membrane interactions of synthetic peptides with antimicrobial potential: Effect of electrostatic interactions and amphiphilicity, Probiotics & Antimicro. Prot., 7, 66-74.
    99.   Gauthier, M., Leclerc, J., Lefévre, T., Gagné, S.M., Auger, M., 2014. Effect of pH on the structure of the recombinant C-terminal domain of Nephila clavipes dragline silk protein, Biomacromolecules, 15, 4447-4454.
    98.   Ayata, R.E., Bouhout, S., Auger, M., Pouliot, R., 2014. Study of in vitro capillary-like structures in psoriatic skin substitutes, BioResearch Open Access, 3, 197-205.
    97.   Bédard, L., Lefèvre, T., Morin-Michaud, É., Auger, M., 2014. Besides fibrillization: the role of the peptide fragment 71-82 on the structural and assembly behavior of α-synuclein, Biochemistry, 53, 6463-6472.
    96.   Gagnon, M.-C., Turgeon, B., Savoie, J.-D., Parent, J.-F., Auger, M., Paquin, J.-F., 2014. Evaluation of the effect of fluorination on the property of monofluorinated dimyristoylphosphatidylcholines, Org. Biomol. Chem., 12, 5126-5135.
    95.   Leroy, M., Labbé, J.-F., Ouellet, M., Jean, J., Lefèvre, T., Laroche, G., Auger, M., Pouliot, R., 2014. A comparative study between human skin substitutes and normal human skin using Raman microspectroscopy, Acta Biomater., 10, 2703-2711.
    94.  Fillion, M., Noël, M., Lorin, A., Voyer, N., Auger, M., 2014. Investigation of the mechanism of action of novel amphipatic peptides: Insights from solid-state NMR studies of oriented lipid bilayers, Biochim. Biophys. Acta, 1838, 2173-2179.
    93.   Potvin-Fournier, K., Lefèvre, T., Picard-Lafond, A.,Valois-Paillard, G., Cantin, L., Salesse, C., Auger, M., 2014. The thermal stability of recoverin depends on calcium binding and its myristoyl moiety as revealed by infrared spectroscopy, Biochemistry, 53, 48-56.
    92.   Leroy, M., Lafleur, M., Auger, M., Laroche, G., Pouliot, R., 2013. Characterization of the structure of human skin substitutes by infrared microspectroscopy, Anal. Bioanal. Chem., 405, 8709-8718.
    91.   Leclerc, J., Lefèvre, T., Gauthier, M., Gagné, S., Auger, M., 2013. Hydrodynamical properties of recombinant spider silk proteins: Effects of pH, salts and shear, and implications for the spinning process, 99, 582-593.
    90.   Otis, F., Auger, M., Voyer, M., 2013. Exploiting peptide nanostructures to construct functional artificial ion channels, Acc. Chem. Res., 46, 2934-2943.
    89.  Labbé, J.-F., Lefèvre, T., Guay-Bégin, A.-A., Auger, M., 2013. Structure and membrane interactions of the beta-amyloid fragment 25-35 as viewed by spectroscopic approaches, Phys. Chem. Chem. Phys., 15, 7228-7239.
    88.   Paquet-Mercier, F., Lefèvre, T., Auger, M., Pézolet, M., 2013. Evidences by infrared spectroscopy of the presence of two types of β-sheets in major ampullate spider silk and silkworm silk, Soft Matter, 9, 208-215.
    87.   Lorin, A., Noël, M., Provencher, M.-E., Turcotte, V., Cardinal, S., Lagüe, P., Voyer, N., Auger, M., 2012. Determining the mode of action involved in the antimicrobial activity of synthetic peptides from FTIR and solid-state NMR experiments, Biophys. J., 103, 1470-1479.
    86.  Guimond-Tremblay, J., Gagnon, M.-C., Pineault-Maltais, J.-A., Turcotte, V., Auger, M., Paquin, J.-F., 2012. Synthesis and properties of monofluorinated dimyristoylphosphatidylcholine derivatives: Potential fluorinated probes for the study of membrane topology, Org. Biomol. Chem., 10, 1145-1148.
    85.   Leclerc, J., Lefèvre, T., Pottier, F., Morency, L.-P., Lapointe-Verreault, C., Gagné, S., Auger, M., 2012. Structure and pH-induced alterations of recombinant and natural spider silk proteins in solution , Biopolymers, 97, 337-346
    84.  Lorin, A., Noël, M., Provencher, M.-E., Turcotte, V., Masson, C., Voyer, N., et Auger, M., 2011. Revisiting peptide amphiphilicity for membrane pore formation, Biochemistry, 50, 9409-9420.
    83.  Cloutier, I., Leclerc,. J., Lefèvre, T., Auger, M., 2011. Solid-state NMR spectroscopy reveals distinctive protein dynamics in closely-related spider silks, Can. J. Chem., 89, 1047-1054.
    82.  Thibeault, D., Auger, M., Morin, J.-F., 2010. Synthesis of fluorine-containing molecular rotors and their assembly on gold nanoparticles, Eur. J. Org. Chem., 3049-3067.
    81.  Ouellet, M., Voyer, N., Auger, M., 2010. Solid-state NMR study of the membrane interaction of a 21-mer cytotoxic model peptide, Biochim. Biophys. Acta, 1798, 235-243.
    80.  Cloutier, I., Paradis-Bleau, C., Giroux, A.-M., Pigeon, X., Arseneault, M., Levesque, R.C., Auger, M., 2010. Biophysical studies of the interactions of the phage φKZ gp144 lytic transglycosylase with model membranes, Eur. Biophys. J., 39, 263-276.
    79.  Giguère, J.-B., Thibeault, D., Cronier, F., Marois, J.-S., Auger, M., Morin, J.-F., 2009. Synthesis of [2]- and [3]rotaxanes through Sonogashira coupling, 50, 5497-5500.
    78.  Labbé, J.-F., Cronier, F., C.-Gaudreault, R., Auger, M., 2009. Spectroscopic characterization of DMPC/DOTAP cationic liposomes and their interaction with DNA and drugs, Chem. Phys. Lipids, 159, 91-101.
    77.  Le Bouch, N., Auger, M., Leclerc, M., 2008. Structure and segmental motions in a substituted polythiophene: a solid-state NMR study, Macromol. Chem. Phys., 209, 2455-2462.
    76.  Fournier, I., Barwicz, J., Auger, M., Tancrède, P., 2008. The chain conformational order of ergosterol- or cholesterol-containing DPPC bilayers as modulated by Amphotericin B: a FTIR study, Chem. Phys. Lipids, 151, 41-50.
    75.  Ouellet, M., Auger, M., 2008. Structure and membrane interactions of antimicrobial peptides as viewed by solid-state NMR spectroscopy, Ann. Rep. NMR Spectrosc., 63, 1-21.
    74.  Lefèvre, T., Leclerc, J., Rioux-Dubé, J.F., Buffeteau, T., Paquin, M.-C., Rousseau, M.-E., Cloutier, I., Auger, M., Gagné, S.M., Boudreault, S., Cloutier, C., Pézolet, M., 2007. Conformation of spider silk proteins in situ in the intact major ampullate gland and in solution, Biomacromolecules, 8, 2342-2344.
    73.  Bernard, G., Auger, M., Soucy, J., Pouliot, R., 2007. Physical characterization of the stratum corneum of an in vitro psoriatic skin model by ATR-FTIR and Raman spectroscopies, Biochim. Biophys. Acta, 1770, 1317-1323.
    72.  Ouellet, M., Doucet, J.-D., Voyer, N., Auger, M., 2007. Membrane topology of a 14-mer model amphipathic peptide: A solid-state NMR spectroscopy study, Biochemistry, 46, 6597-6606.
    71.  Cronier, F., Patenaude, A., C.-Gaudreault, R., Auger, M., 2007. Membrane composition modulates the interaction between a new class of antineoplastic agents derived from chloroethylurea and lipid bilayers : A solid-state NMR and FTIR spectroscopic study, Chem. Phys. Lipids, 146, 125-135.
    70.  Paradis-Bleau, C., Cloutier, I., Sanschagrin, F., Lemieux, L., Laroche, J., Otis, F., Auger, M., Garnier, A., Levesque, R.C., 2007. Autotranslocation and lysis mechanism of the Pseudomonas aeruginosa bacteriophage φKZ endolysin, FEMS Microbiology Letters, 266, 201-209.
    69.  Ouellet, M., Otis, F., Voyer, N., Auger, M., 2006. Biophysical studies of the interactions between 14-mer and 21-mer model amphipathic peptides and membranes: insights on their modes of action, Biochimi. Biophys. Acta, 1758, 1235-1244.
    68.  Ouellet, M., Bernard, G., Voyer, N., Auger, M., 2006. Insights on the interactions of synthetic amphipathic peptides with model membranes as revealed by 31P and 2H solid-state NMR and infrared spectroscopies, Biophys. J., 90, 4071-4084.
    67.  Marcotte, I., Bélanger, A., Auger, M., 2006. The orientation effect of gramicidin A on bicelles and Eu3+-doped bicelles as studied by solid-state NMR and FTIR spectroscopy, Chem. Phys. Lipids, 139, 137-149.

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