Publications récentes

2017
    121. Dionne, J., Lefèvre, T., Bilodeau, P., Lamarre, M., Auger, M., 2017. A quantitative analysis of the supercontraction-induced molecular disorientation of major ampullate spider silk, Phys. Chem. Chem. Phys., 10.1039/C7CP05739C.
    120. Xu, L., Lefèvre, T., Orrell, K.E., Meng, Q., Auger, M., Rainey, J.K., Liu, X.-Q., 2017. Structural and mechanical roles for the C-terminal non-repetitive domain become apparent in recombinant spider aciniform silk, Biomacromolecules, 18, 3678-3686.
    119. Gagnon, M.-C., Dautrey, S., Bertrand, X., Auger, M., Paquin, J.-F., 2017. A flexible synthetic approach to phosphatidylglycerols, Eur. J. Org. Chem., 6401-6407.
    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., 490, 1268-1273.
    117. Auger, M. 2017. Membrane solid-state in Canada: A historical perspective, Biochim. Biophys. Acta, 1865, 1483-1489.
    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

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