APS March Meeting 2013
Volume 58, Number 1
Monday–Friday, March 18–22, 2013;
Baltimore, Maryland
Session T11: Invited Session: Self-Assembly, Physical Properties and Functionalities of Amyloid Fibrils
8:00 AM–11:00 AM,
Thursday, March 21, 2013
Room: 310
Sponsoring
Units:
DPOLY DBIO
Chair: Raffaele Mezzenga, ETH-Zurich
Abstract ID: BAPS.2013.MAR.T11.2
Abstract: T11.00002 : Molecular Self-Assembly of Short Aromatic Peptides: From Biology to Nanotechnology and Material Science
8:36 AM–9:12 AM
Preview Abstract
Abstract
Author:
Ehud Gazit
(Tel Aviv University)
The formation of ordered amyloid fibrils is the hallmark of several diseases
of unrelated origin. In spite of grave clinical consequence, the mechanism
of amyloid formation is not fully understood. We have suggested, based on
experimental and bioinformatic analysis, that aromatic interactions may
provide energetic contribution as well as order and directionality in the
molecular-recognition and self-association processes that lead to the
formation of these assemblies. This is in line with the well-known central
role of aromatic-stacking interactions in self-assembly processes. Our works
on the mechanism of aromatic peptide self-assembly, lead to the discovery
that the diphenylalanine recognition motif self-assembles into peptide
nanotubes with a remarkable persistence length. Other aromatic
homodipeptides could self-assemble in nano-spheres, nano-plates,
nano-fibrils and hydrogels with nano-scale order. We demonstrated that the
peptide nanostructures have unique chemical, physical and mechanical
properties including ultra-rigidity as aramides, semi-conductive,
piezoelectric and non-linear optic properties. We also demonstrated the
ability to use these peptide nanostructures as casting mold for the
fabrication of metallic nano-wires and coaxial nano-cables. The application
of the nanostructures was demonstrated in various fields including
electrochemical biosensors, tissue engineering, and molecular imaging.
Finally, we had developed ways for depositing of the peptide nanostructures
and their organization. We had use inkjet technology as well as vapour
deposition methods to coat surface and from the peptide ``nano-forests''. We
recently demonstrated that even a single phenylalanine amino-acid can form
well-ordered fibrilar assemblies.\\[4pt]
References:
Reches, M. and Gazit, E. (2003) Casting Metal Nanowires within Discrete
Self-Assembled Peptide Nanotubes. \textbf{Science} \textit{300}, 625-627.
Reches, M. and Gazit, E. (2006) Controlled Patterning of Aligned
Self-Assembled Peptide Nanotubes. \textbf{Nature Nanotechnol.}
\textit{1}, 195-200.
Adler-Abramovich L., Aronov D., Beker P., Yevnin M., Stempler S., Buzhansky
L., Rosenman G. and Gazit E. (2009) Self-Assembled Arrays of Peptide
Nanotubes by Vapour Deposition. \textbf{Nature Nanotechnol.}
\textit{4}, 849-854.
Carny, O., Shalev, D., and Gazit, E. (2006) Fabrication of Coaxial Metal
Nanowires Using Self-Assembled Peptide Nanotube Scaffold.
\textbf{Nano Lett.}\textit{ 6}, 1594-1597. (Featured in the \textit{Research Highlights} of
\textbf{Nature Nanotechnol.}; doi:10.1038/nnano.2006.23).
Amdursky, N., Molotskii, M., Gazit, E., and Rosenman, G. (2010) Elementary
Building Blocks of Self-Assembled Peptide Nanotubes. \textbf{J.
Am. Chem. Soc.} \textit{132}, 15632-1563. (Featured in the \textit{News and Views} of
\textbf{Nature} \textit{468}, 516-517).
Adler-Abramovich, L., Vaks, L., Carny, O., Trudler, D., Magno, A., Caflisch,
A., Frenkel, D. and Gazit, E. (2012) Phenylalanine Assembly into Toxic
Fibrils Suggests Amyloid Etiology in Phenylketonuria.
\textbf{Nature Chem. Biol.} \textit{8}, 701--706.
To cite this abstract, use the following reference: http://meetings.aps.org/link/BAPS.2013.MAR.T11.2