|Reference : Mechanochemical Study of Conformational Transitions in a Single Synthetic Peptide Chain|
|Scientific congresses and symposiums : Poster|
|Life sciences : Biochemistry, biophysics & molecular biology|
Physical, chemical, mathematical & earth Sciences : Chemistry
Physical, chemical, mathematical & earth Sciences : Physics
Physical, chemical, mathematical & earth Sciences : Multidisciplinary, general & others
|Mechanochemical Study of Conformational Transitions in a Single Synthetic Peptide Chain|
|Willet, Nicolas [Université de Liège - ULg > Département de chimie (sciences) > Nano-chimie et systèmes moléculaires >]|
|Hinterdorfer, Peter [Johannes Kepler University Linz > Biophysics Institute > > >]|
|Lecommandoux, Sébastien [Université Bordeaux 1 > LCPO > > >]|
|Duwez, Anne-Sophie [Université de Liège - ULg > Département de chimie (sciences) > Nano-chimie et systèmes moléculaires >]|
|Gordon Research Conference: Biopolymers|
|June 3-8, 2012|
|Angel E. Garcia|
|Enrique De La Cruz|
|Rhode Island, USA|
|[en] AFM ; Single-molecule ; 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 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.
|Researchers ; Students|
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