DOI: 10.1039/C3CC49268K
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ChemComm
Upon oxidation of the gel, the fibrillar structure is lost as is
demonstrated in Fig. 2c and 2d. Partial oxidation of the gel
component of the bioorganometallic conjugate. There is
evidence that this structural rearragement results from loss of
the -sheet interactions between adjacent peptide segments.
45 This study demonstrates that redox, as a stimulus, may serve
as a versatile tool to control the self-assembly of peptides,
which may enable us to develop new redox-active functional
biomaterials in the near future.
Notes and references
50 * Department of Physical and Environmental Sciences, University of
Toronto Scarborough, 1265 Military Trail, Toronto, M1C 1A4, Canada
and Department of Chemistry, University of Toronto, 80 St. George
Street, Toronto, Ontario M5S 3H6, Canada.
55 † Electronic Supplementary Information (ESI) available.
1
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Fig. 2 TEM images of self-assembled Fc-peptide 1: (a) with out (b)
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2
3
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In conclusion, the results demonstrate that the Fc-
conjugate of A18–20 engages in intermolecular H-bonding,
giving rise to an induced Fc-based CD signal and it forms an
organogel upon ultrasonication. In addition, the Fc-peptide
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