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 : Multidisciplinary, general & others
Physical, chemical, mathematical & earth Sciences : Physics
Physical, chemical, mathematical & earth Sciences : Chemistry
http://hdl.handle.net/2268/126075
Mechanochemical Study of Conformational Transitions in a Single Synthetic Peptide Chain
English
Willet, Nicolas mailto [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 mailto [Université de Liège - ULg > Département de chimie (sciences) > Nano-chimie et systèmes moléculaires >]
5-Jun-2012
Yes
No
International
Gordon Research Conference: Biopolymers
June 3-8, 2012
GRC
Angel E. Garcia
Enrique De La Cruz
Newport
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.
NanoChem
Researchers ; Students
http://hdl.handle.net/2268/126075

There is no file associated with this reference.

Bookmark and Share SFX Query

All documents in ORBi are protected by a user license.