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Updated: Jul 9, 2026

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
Published on: November 21, 2013
Optical fingerprinting of peptides using two-dimensional infrared spectroscopy: proof of principle
Frédéric Fournier1, Elizabeth M Gardner, Rui Guo
1Molecular Dynamics Research Group, Department of Chemistry, Imperial College London, London SW7 2AZ, UK. f.fournier@imperial.ac.uk
Abstract:
We employ a particular form of two-dimensional infrared four-wave mixing (2DIR FWM) as a vibrational spectroscopic tool to quantify the amino acid content of a number of peptides. Vibrational features corresponding to ring modes of the aromatic groups of phenylalanine (Phe) and tyrosine (Tyr), as well as a methylene mode that is used as an internal reference, are identified. We show that the ratios of the integrated intensities, and the amplitudes, of the aromatic peaks of Phe and Tyr relative to the methylene integrated intensity, and amplitude, are proportional to the actual ratio of Phe and Tyr to CH(2) in the samples within a precision of +/-12.5%. This precision is shown to be sufficient to use this form of 2DIR spectroscopy as a possible proteins fingerprinting tool.
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