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Polymers and Self Assembly: From Biology to Nanomaterials Poster Session I
20-POS
Board 20
Highly Oriented, Epitaxially Generated Beta-amyloid-based Nanoarray for
Nanobiotechnological Applications
Róbert Nagy
1
, Gábor Olajos
2
, Vivien Hársfalvi
1
, Ünige Murvai
1
, Lívia Fülöp
3
, Botond Penke
3
,
Tamás Martinek
2
,
Miklós S. Kellermayer
1
.
1
Semmelweis University, Budapest, Hungary,
3
University of Szeged, Szeged,
Hungary.
2
University of Szeged, Szeged, Hungary,
The self-assembly of biomolecular systems are of fundamental appeal for nanobiotechnological
applications. However, the lack of easy chemical access and nano- to micro-scale structural order
often hinders the nanotechnological use of conventional biomolecules. We have previously
shown that the amyloid beta 25-35 peptide (Aß25-35) forms a trigonally oriented network on
mica by epitaxial mechanisms. To enhance the chemical reactivity and the structural complexity
of this nano-network, here we synthesized and utilized a chemically accessible mutant and
various Aß-foldamer chimeras. Oriented network of amyloid fibrils was generated by incubating
mutant, Aß25-34_N27C peptides or its wild-type mixtures on mica at varying KCl
concentrations. To functionalize the fibrils we used maleimido-nanogold (1.4 nm). As evidenced
by high-resolution atomic-force microscopy, we were able to tune the average length of the
amyloid fibrils by adjusting the peptide and KCl concentrations. In the nanogold-labeled amyloid
network spherical particles of 1.4-nm diameter lined up along the oriented fibrils, demonstrating
that the fibrils can indeed be chemically addressed and functionalized. The Aß-foldamer
chimeras were conjugates of an Aß25-29 peptide and a 2-aminocyclopentane-carbonic acid
hexamer located at the N- and C-terminals, respectively. We found that the Aß-foldamer
chimeras formed, on a time-scale of minutes, trigonally oriented network on mica in which the
individual fibrils reached lengths up to several microns. Apparently the Aß component is
responsible for the oriented surface binding and epitaxis, while the foldamer enhances the
assembly of extended fibrils. In sum, the oriented amyloid-based network may be used towards
the construction of functional biomolecular nanoarrays with complex, tunable geometries and
properties.