Infrared Spectroscopy - Life and Biomedical Sciences

Infrared and Raman Spectroscopic Studies of Molecular Disorders in Skin Cancer

“…This band is not observed in Raman spectra appearing only as a shoulder, as shown in Figure 2. The high intensity FT-IR band at 1,650 cm -1 is assigned to vC=O of amide I of the peptide bond (-NHCO-) of proteins (7)(8)(9)(10)(11)(12)(22)(23)(24)(25)(26) and is a 'marker band' for α-helical peptide bond. This band is split upon deconvolution into three bands at 1,690 cm -1 , 1,650 cm -1 and 1,633 cm -1 due to the presence of a β-sheet (↓↑, anti-parallel structure), α-helix and random coil protein structure, respectively for MM, indicating that the secondary structure of proteins changed from α-helix to β-sheet and random coil upon cancer formation.…”

“…Vibrational spectroscopies [infrared (IR) absorption and Raman scattering] have gained great attention from the medical community as interesting tools for the non-invasive (non-destructive) characterization and identification of the molecular features of cancer tissues (7)(8)(9)(10). IR spectroscopy is based on the changes of dipole moment of molecules during their interaction with the IR radiation (11,12), while Raman is based on the change of electric polarizability of the molecules (13,14). Both methods reveal information not only on the characteristic functional groups, such as CH, NH OH, C-O-C and PO 2 of lipid chains, proteins, glycans, DNA, but also on the changes of the surrounding environment induced by disease (8)(9)(10)(11)(12)(13)(14)(15)(16)(17)(18)(19).…”

“…IR spectroscopy is based on the changes of dipole moment of molecules during their interaction with the IR radiation (11,12), while Raman is based on the change of electric polarizability of the molecules (13,14). Both methods reveal information not only on the characteristic functional groups, such as CH, NH OH, C-O-C and PO 2 of lipid chains, proteins, glycans, DNA, but also on the changes of the surrounding environment induced by disease (8)(9)(10)(11)(12)(13)(14)(15)(16)(17)(18)(19).…”

Infrared Spectroscopic Study and Mathematical Simulations of Carotid Atherosclerosis

“…In the infrared spectral region between 4,000-3,000 cm −1 , the characteristic stretching vibrational modes of the stretching vibration of vNH groups derive mostly from proteins and the stretching vibrations of OH groups of organic molecules and from water molecules of the cells (11)(12)(13)(14). It is observed that in the spectra originating from the inorganic phase, this band is almost absent, as expected, since the sample was not rich in organic components which contain these groups.…”

“…ATR-FT-IR spectroscopy is a simple, fast and a non-destructive technique which requires small amounts of sample (micrograms or microliters), without any preparation of the sample and can be applied in medicine (6)(7)(8)(9)(10)(11). IR spectroscopy has been shown to be a very sensitive method for evaluating the secondary protein structure of human tissues and other components, including DNA, lipids and phospholipids, all in a single spectrum (12)(13)(14)(15). IR spectroscopic analysis provides characteristic 'fingerprint region bands' or 'marker bands' of the tissue of each patient and can differentiate normal from malignant tissues, as well as progression of disease, and can also characterize deposits at the very early stages of the disease (7)(8)(9)(10)(11).…”