References of "lecommandoux, Sébastien"
     in
Bookmark and Share    
Peer Reviewed
See detailDesign of biocompatible and responsive hydrogels and nanogels made from poly(2-oxazoline)s
Legros, Camille ULg; Gillet, Marie-Claire ULg; tam, Michael et al

Conference (2014, August 12)

Detailed reference viewed: 22 (3 ULg)
Peer Reviewed
See detailpH and redox responsive hydrogel and nanogels made from poly(2-ethyl-2-oxazoline)
Legros, Camille ULg; Gillet, Marie-Claire ULg; Tam, Michael et al

Conference (2013, November 19)

Detailed reference viewed: 13 (7 ULg)
Full Text
Peer Reviewed
See detailpH and redox responsive hydrogels and nanogels made from poly(2-ethyl-2-oxazoline)
Legros, Camille ULg; De Pauw-Gillet, Marie-Claire ULg; Tam, Kam Chiu et al

in Polymer Chemistry (2013)

Detailed reference viewed: 20 (6 ULg)
See detailUNFOLDING SYNTHETIC PEPTIDES BY AFM AT THE SINGLE-MOLECULE LEVEL
Willet, Nicolas ULg; Hinterdorfer, Peter; lecommandoux, Sébastien et al

Conference (2012, September)

The aim of this study is to investigate the mechanochemical behavior of homopolypeptides able to change their conformation is a stimuli-responsive way. The peptidic secondary structures were studied in ... [more ▼]

The aim of this study is to investigate the mechanochemical behavior of homopolypeptides able to change their conformation is a stimuli-responsive way. The peptidic secondary structures were studied in detail by atomic force microscopy (AFM) at the single-molecule level. Synthetic copolymers containing a polypeptide block were prepared by N-carboxyanhydride amino acid ring-opening polymerization. The polymer chains were grafted as a dilute brush onto gold surfaces and their mechanochemical behavior was then studied by AFM single-molecule force spectroscopy (SMFS). The investigated polypeptide blocks were based on poly(L-glutamic acid), which undergoes a transition from alpha-helix to random coil. This can be induced by external stimuli (pH, ionic strength, temperature) or simply by applying a force. We were able to study the mechanically driven unfolding of the peptide by stretching-release cycles of the biomacromolecule. Stretching the helical peptide resulted in original features in the force-distance traces. Plateaus that are specific for the helical conformation were detected, quantified and discussed. Pulling-relaxing SMFS experiments will eventually lead to a better understanding of the force-induced unfolding of an alpha-helix and the reversibility of the phenomenon. [less ▲]

Detailed reference viewed: 24 (1 ULg)
See detailUNFOLDING SYNTHETIC PEPTIDES BY AFM AT THE SINGLE-MOLECULE LEVEL
Willet, Nicolas ULg; Hinterdorfer, Peter; Lecommandoux, Sébastien et al

Poster (2012, September)

The aim of this study is to investigate the mechanochemical behavior of homopolypeptides able to change their conformation is a stimuli-responsive way. The peptidic secondary structures were studied in ... [more ▼]

The aim of this study is to investigate the mechanochemical behavior of homopolypeptides able to change their conformation is a stimuli-responsive way. The peptidic secondary structures were studied in detail by atomic force microscopy (AFM) at the single-molecule level. Synthetic copolymers containing a polypeptide block were prepared by N-carboxyanhydride amino acid ring-opening polymerization. The polymer chains were grafted as a dilute brush onto gold surfaces and their mechanochemical behavior was then studied by AFM single-molecule force spectroscopy (SMFS). The investigated polypeptide blocks were based on poly(L-glutamic acid), which undergoes a transition from alpha-helix to random coil. This can be induced by external stimuli (pH, ionic strength, temperature) or simply by applying a force. We were able to study the mechanically driven unfolding of the peptide by stretching-release cycles of the biomacromolecule. Stretching the helical peptide resulted in original features in the force-distance traces. Plateaus that are specific for the helical conformation were detected, quantified and discussed. Pulling-relaxing SMFS experiments will eventually lead to a better understanding of the force-induced unfolding of an alpha-helix and the reversibility of the phenomenon. [less ▲]

Detailed reference viewed: 29 (1 ULg)
Peer Reviewed
See detailMechanochemical Study of Conformational Transitions in a Single Synthetic Peptide Chain
Willet, Nicolas ULg; Hinterdorfer, Peter; Lecommandoux, Sébastien et al

Poster (2012, June 05)

The aim of this study is to investigate the mechanochemical behavior of homopolypeptides able to change their conformation is a stimuli-responsive way. The peptidic secondary structures were studied in ... [more ▼]

The aim of this study is to investigate the mechanochemical behavior of homopolypeptides able to change their conformation is a stimuli-responsive way. The peptidic secondary structures were studied in detail by atomic force microscopy (AFM) at the single-molecule level. Synthetic copolymers containing a polypeptide block were prepared by N-carboxyanhydride amino acid ring-opening polymerization. The polymer chains were grafted as a dilute brush onto gold surfaces via disulfide end-groups. Their mechanochemical behavior was then studied by AFM single-molecule force spectroscopy (SMFS). The investigated polypeptide blocks were based on poly(L-glutamic acid), which undergoes a transition from alpha-helix to random coil. This can be induced by external stimuli (pH, ionic strength, temperature) or simply by applying a force. We were able to study the mechanically driven unfolding of the peptide by stretching-release cycles of the biomacromolecule. Stretching the helical peptide resulted in original features in the force-distance traces. Plateaus that are specific for the helical conformation were detected, quantified and discussed. Pulling-relaxing SMFS experiments eventually led to a better understanding of the force induced unfolding of an alpha-helix and the reversibility of the phenomenon. [less ▲]

Detailed reference viewed: 61 (0 ULg)
See detailMechanochemistry of a single polypeptide molecule: Study of force-induced conformational transitions
Willet, Nicolas ULg; Hinterdorfer, Peter; Lecommandoux, Sébastien et al

Conference (2011, August)

The aim of this study is to investigate the mechanochemical behavior of homopolypeptides able to change their conformation is a stimuli-responsive way. The peptidic secondary structures were studied in ... [more ▼]

The aim of this study is to investigate the mechanochemical behavior of homopolypeptides able to change their conformation is a stimuli-responsive way. The peptidic secondary structures were studied in detail by atomic force microscopy (AFM) at the single-molecule level. Synthetic copolymers containing a polypeptide block were prepared by N-carboxyanhydride amino acid ring-opening polymerization. The polymer chains were grafted as a dilute brush onto gold surfaces via disulfide end-groups. Their mechanochemical behavior was then studied by AFM single-molecule force spectroscopy (SMFS). The investigated polypeptide blocks were based on poly(L-glutamic acid), which undergoes a transition from alpha-helix to random coil. This can be induced by external stimuli (pH, ionic strength, temperature) or simply by applying a force. We were able to study the mechanically driven unfolding of the peptide by stretching-release cycles of the biomacromolecule. Stretching the helical peptide resulted in original features in the force-distance traces. Plateaus that are specific for the helical conformation were detected, quantified and discussed. Pulling-relaxing SMFS experiments eventually led to a better understanding of the force induced unfolding of a alpha-helix and the reversibility of the phenomenon. [less ▲]

Detailed reference viewed: 62 (3 ULg)
Full Text
See detailMechanochemical Study of a Single Polypeptide Molecule: Force-Induced Conformational Transition
Willet, Nicolas ULg; Hinterdorfer, Peter; Lecommandoux, Sébastien et al

Conference (2011, June)

Detailed reference viewed: 13 (0 ULg)