Optical fingerprinting of peptides using two-dimensional infrared spectroscopy: Proof of principle

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 we...

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Bibliographic Details
Published in:Analytical biochemistry 2008-03, Vol.374 (2), p.358-365
Main Authors: Fournier, Frédéric, Gardner, Elizabeth M., Guo, Rui, Donaldson, Paul M., Barter, Laura M.C., Palmer, D. Jason, Barnett, Chris J., Willison, Keith R., Gould, Ian R., Klug, David R.
Format: Article
Language:English
Subjects:
2DIR
Amino acid
Amino Acids - analysis
Optics and Photonics
Peptide Mapping - methods
Peptides
Phenylalanine
Protein fingerprinting
Proteomics
Sensitivity and Specificity
Spectrophotometry, Infrared - methods
Two-dimensional infrared spectroscopy
Tyrosine
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Summary: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.
ISSN:0003-2697
1096-0309
DOI:10.1016/j.ab.2007.11.009