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Terahertz spectroscopy of fibrillar self-assembling peptides (1)

Project Member(s): Dowd, A.

Funding or Partner Organisation: Australian Synchrotron Research Program (Australian Synchrotron Beamline)

Start year: 2014

Summary: This covers 2 trips to the Synchrotron Facility in Melbourne - one in 2014, one in 2015 (both for the same project) We propose a pilot study to evaluate the applicability of far-infrared spectroscopy for the characterization of the secondary and tertiary structure of hierarchical fibrillar self-assembled structures based on synthetic peptides. The primary aim of the proposed work is to detect and correlate the hydrogen bonding structure to known morphological features of the peptide fibres, and thus confirm the primary and secondary self-assembly motifs, the first being exclusively H-bonding and the second a combination of H-bonding and van der Waals interactions.


Seoudi, RS, Dowd, A, Smith, BJ & Mechler, A 2016, 'Structural analysis of bioinspired nano materials with synchrotron far IR spectroscopy', PHYSICAL CHEMISTRY CHEMICAL PHYSICS, vol. 18, no. 16, pp. 11467-11473.
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Seoudi, RS, Dowd, A, Del Borgo, M, Kulkarni, K, Perlmutter, P, Aguilar, M-I & Mechler, A 2015, 'Amino acid sequence controls the self-assembled superstructure morphology of N-acetylated tri-β3-peptides', Pure and Applied Chemistry, vol. 87, no. 9-10, pp. 1021-1028.
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Keywords: Vibrational Spectroscopy, Far Infared, Terahertz, peptide structure, nanotechnology, foldamers

FOR Codes: Physical Chemistry (incl. Structural, Materials Engineering, Condensed Matter Physics, Industrial Chemicals and Related Products not elsewhere classified