Reference : UNFOLDING SYNTHETIC PEPTIDES BY AFM AT THE SINGLE-MOLECULE LEVEL
Scientific congresses and symposiums : Unpublished conference
Physical, chemical, mathematical & earth Sciences : Physics
Physical, chemical, mathematical & earth Sciences : Chemistry
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/131578
UNFOLDING SYNTHETIC PEPTIDES BY AFM AT THE SINGLE-MOLECULE LEVEL
English
Willet, Nicolas mailto [Université de Liège - ULg > Département de chimie (sciences) > Département de chimie (sciences) >]
Hinterdorfer, Peter [Johannes Kepler University Linz > > > >]
lecommandoux, Sébastien [Université Bordeaux 1 > > > >]
Duwez, Anne-Sophie mailto [Université de Liège - ULg > Département de chimie (sciences) > Nano-chimie et systèmes moléculaires >]
Sep-2012
No
No
International
Sofia School of Protein Science: Structure and dynamics of biological macromolecules
9-14 September 2012
FEBS
Sofia
Bulgaria
[en] AFM ; single-molecule ; force spectroscopy ; peptide ; folding ; conformation
[en] 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.
Researchers ; Students
http://hdl.handle.net/2268/131578

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