Metabolic Fingerprinting with Fourier Transform Infrared Spectroscopy
Fourier transform infrared (FT-IR) spectroscopy is a rapid, reagent-less, non-destructive, analytical technique whose continuing development is resulting in manifold applications in the biosciences. The principle of FT-IR lies in the fact that when a sample is interrogated with light (or electromagnetic radiation), chemical bonds absorb at specific wavelengths and vibrate in one of a number of ways. These absorptions/vibrations can then be correlated to the bonds or functional groups of molecules. Because of its chemical information content and spectral richness (defined as numbers of clearly defined peaks) the major wavenumber region of interest is the mid-infrared, usually defined as 4000–600 cm-1 (see Table 1). The infrared spectra of proteins, as a prominent example, exhibit strong amide I absorption bands at 1653 cm-1 associated with characteristic stretching of C=O and C-N and bending of the N-H bond (Stuart, 1997).
KeywordsCholesterol Sugar Arthritis Manifold Dopamine
Unable to display preview. Download preview PDF.
- Fox S. WHO to convene on worldwide risk of BSE and vCJD. Infect Med 18: 69–69 (2001).Google Scholar
- Helm D, Labischinski H, Schallehn G, Naumann D. Classification and identification of bacteria by Fourier-transform infrared spectroscopy. J Gen Microbiol 137: 69–79 (1990).Google Scholar
- Rempel SP, Manisch HH. Biomedical applications of near-infrared spectroscopy: a review. Can J Anal Sci Spectr 44: 171–179 (1999).Google Scholar
- Stuart B. Biological Applications of Infrared Spectroscopy. John Wiley and Sons, Chichester (1997).Google Scholar