Protein-Assisted Synthesis of Metallic and Semiconductor Nanowires
Protein-Assisted
Synthesis of Metallic and Semiconductor Nanowires
Scientific
Achievement
For
the first time, the a-synuclein protein nanofibers
were used for biotemplated synthesis of Pd, Au and Cu ordered
nanoparticle
chains. Palladium
catalysis is required
for the synthesis of Au and Cu ordered nanoparticle chains. Exposing Pd and Au
solutions to elemental Cu,
in the presence of a-synuclein
protein fibers and a reducing agent leads to formation of Cu
nanoparticle
chains. The
chemical analysis of the
samples has been performed at EMC, on a FEI Tecnai F20ST transmission
electron
microscope. These
experiments came as a
proof that indeed Cu was deposited on the protein fibrils. The results can be
expanded to designing
bottom-up strategies for nanomaterials synthesis by bio-templated
synthesis of
other peptides and proteins with the capacity to self-assemble into
fibrillar
structures with exposed negatively charged groups.
These nanostructures have potential
applications in nanophotonic devices, ultrahigh-density storage media,
or
quantum dot arrays.
Significance
The
proposed research project
is, through its objectives, the first
study that investigates the capacity of a model fibril
forming protein, a-synuclein, to function as a
scaffold for controlled design of both
metallic and semiconducting nanowires.
The proposed research developed a generic nanowire or
wire-like
nanoparticle assemblies (WLNA) fabrication method, applicable for a
large array
of metallic and semiconducting compounds, on an a-synuclein
model protein
fiber scaffold. It
designed a generic
synthesis and processing technique that will allow for the design of
nanowires
and WLNA with tunable dimensions and therefore with controllable
properties. The
interdisciplinary character of the
proposed research has a great beneficial impact on students’ training. The work has been
published in Nanotechnology
19, 275602 (2008) and J. of Nanoscience
and Nanotechnology 8
(2), 973-978 (2008).
Performers
R. Colby, S.
Padalkar, L. Stanciu (Purdue U.); N. J. Zaluzec
(Argonne-MSD)

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