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See detailPhysisorbed poly(ethylene oxide) is a robust tether for AFM-based single-molecule force spectroscopy
Willet, Nicolas ULg; Lussis, Perrine ULg; Giamblanco, Nicoletta et al

Conference (2014, December 01)

Atomic force microscopy (AFM)-based single-molecule force spectroscopy is a prevalent tool for the exploration of individual (bio)molecules, providing exquisite information on many molecular-level ... [more ▼]

Atomic force microscopy (AFM)-based single-molecule force spectroscopy is a prevalent tool for the exploration of individual (bio)molecules, providing exquisite information on many molecular-level processes. For example, proteins, DNA, polysaccharides, supramolecular polymers and polyelectrolytes have been investigated, revealing details about the strength of intramolecular interactions, folding and unfolding pathways, mechanics, conformational changes, reactivity, kinetics, etc. For each particular system under investigation, the experimental design is a decisive phase that often involves a multistep chemical protocol, including grafting, derivatization, coupling, (de-)protection, and other functionalization reactions. Procedures of sample preparation are often complex and time-consuming. Hence, there is a need for new general platforms allowing for straightforward sample preparation adapted to single-molecule studies, i.e. a tight attachment to both the substrate and the tip, and a low density to favor single-molecule detection. We report here on the use of poly(ethylene oxide) (PEO) as a tether to probe various properties of individual molecules. The polymeric linker acts as a handle that stably binds to the AFM tip. The simple adsorption of poly(ethylene oxide) to the tip is versatile and provides an appropriate system configuration for the investigation of many different biological and synthetic molecular systems. To attest for this versatility and adequacy with advanced single-molecule investigation, we present different examples of PEO-mediated studies about the unfolding of a synthetic peptide, the mechanochemical behavior of a molecular machine and finally the stability of a metallo-supramolecular complexed polymer. All the requirements for the study of peptide conformation, tiny molecular machines or metallo-supramolecular interactions in solution are here fulfilled. More generally, this method based on non-covalent sorption of PEO on an AFM tip, can be implemented in a wide range of solvents, for the study of many intra- or intermolecular phenomena at the single-molecule level over orders of magnitude of force loading rates. Connecting PEO tethers to a very broad variety of (bio)molecules is a facile and versatile route. The commercial availability of many different functional PEOs makes this tethering strategy even more accessible. [less ▲]

Detailed reference viewed: 9 (2 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: 30 (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: 62 (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)
See detailMolecular recognition force spectroscopy
Willet, Nicolas ULg; Lamprecht, Constanze; Rankl, Christian et al

in Duwez, Anne-Sophie; Willet, Nicolas (Eds.) Molecular manipulation with atomic force microscopy (2011)

This chapter describes the state of the art in molecular recognition force spectroscopy performed by AFM. The different aspects of the topic are discussed, as the appropriate techniques for the ... [more ▼]

This chapter describes the state of the art in molecular recognition force spectroscopy performed by AFM. The different aspects of the topic are discussed, as the appropriate techniques for the functionalization of cantilever tips and for the preparation of (biological) samples. The principles of single-molecule force spectroscopy are then explained, together with exciting and recent examples on synthetic and biological samples. Finally, the main techniques to map molecular recognition interactions are reviewed and discussed in terms of performances. Novel and interesting applications illustrate the use of these imaging methods. [less ▲]

Detailed reference viewed: 25 (4 ULg)