Role of Infrared Spectroscopy in Proteomics and Subsequently the Biomarker Analysis

A.      Saeed; C.      W. Huck; J.      Pallua; V.      A. Huck-Pezzei; L.      Bittner; C.      Pezzei; S.      Schonbichler; A.      M. Qureshi; G.      K. Bonn; M.      Najam-ul-Haq

Abstract

During recent years, various bio-analytical tools are being utilized in the study of peptides and proteins in the field of proteomics. Particularly, the matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) is an extensively used tool for investigating the different aspects. Although the results and achievements made through this tool are remarkable, however, the technique is quite complex, hard to interpret and routine analyses of bulk samples are quite expensive and not always commercially viable. IR spectroscopy is an established analytical tool evolved as a replacement/ assistance for certain investigations in proteomics. It is used in various mass ranges of peptides and proteins. This role of IR and NIR is elaborated in this review. The modified materials in their different derivatized forms are used in binding the peptides and proteins out of complex biofluids and analyzed with IR and NIR spectrophotometers. However, a strategy of desalting, pre-concentration can be applied before IR investigations to minimize the stray absorptions. Silica is modified in different ways to bind the serum entities and is employed in the proteome identifications.

Keywords: Biomarkers, infrared spectroscopy, mass spectrometry, near-infrared, proteomics, peptides, matrix-assisted laser desorption/ionization mass spectrometry, spectroscopy, Protein Analysis Tools, Protein, 2D-PAGE, "Multidimensional liquid chromatography", myoglobin