Publications récentes

2017
    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.
2016
    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.
2015
    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.
2014
    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.
2013
    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.
2012
    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
2011
    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.
2010
    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.
2009
    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.
2008
    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.
2007
    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.
2006
    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.

Liste complète des publications en format pdf