Reference : UNFOLDING SYNTHETIC PEPTIDES BY AFM AT THE SINGLE-MOLECULE LEVEL

	Document type :	Scientific congresses and symposiums : Poster
	Discipline(s) :	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
	To cite this reference:	http://hdl.handle.net/2268/131568

Title :	UNFOLDING SYNTHETIC PEPTIDES BY AFM AT THE SINGLE-MOLECULE LEVEL
Language :	English
Author, co-author :	Willet, Nicolas [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 [Université de Liège - ULg > Département de chimie (sciences) > Nano-chimie et systèmes moléculaires >]
Publication date :	Sep-2012
On invitation :	No
Audience :	International
Event name :	Sofia School of Protein Science: Structure and dynamics of biological macromolecules
Event date :	9-14 September 2012
Event organizer :	FEBS (Federation of European Biochemical Societies)
Event place (city) :	Sofia
Event country :	Bulgaria
Keywords :	[en] AFM ; Force spectroscopy ; Folding ; Peptide ; Single-Molecule ; Conformation
Abstract :	[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.
Target :	Researchers ; Students
Permalink :	http://hdl.handle.net/2268/131568
Other URL :	http://febs2012.com/

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