Alternative profiling platform based on MELDI and its applicability in clinical proteomics.
The presence of numerous proteomics data and their results in literature reveal the importance and influence of proteins and peptides on human cell cycle. For instance, the proteomic profiling of biological samples, such as serum, plasma or cells, and their organelles, carried out by surface-enhanced laser desorption/ionization mass spectrometry, has led to the discovery of numerous key proteins involved in many biological disease processes. However, questions still remain regarding the reproducibility, bioinformatic artifacts and cross-validations of such experimental set-ups. The authors have developed a material-based approach, termed material-enhanced laser desorption/ionization mass spectrometry (MELDI-MS), to facilitate and improve the robustness of large-scale proteomic experiments. MELDI-MS includes a fully automated protein-profiling platform, from sample preparation and analysis to data processing involving state-of-the-art methods, which can be further improved. Multiplexed protein pattern analysis, based on material morphology, physical characteristics and chemical functionalities provides a multitude of protein patterns and allows prostate cancer samples to be distinguished from non-prostate cancer samples. Furthermore, MELDI-MS enables not only the analysis of protein signatures, but also the identification of potential discriminating peaks via capillary liquid chromatography mass spectrometry. The optimized MELDI approach offers a complete proteomics platform with improved sensitivity, selectivity and short sample preparation times.
Najam-ul-Haq
Muhammad
M
Institute of Analytical Chemistry & Radiochemistry, Leopold-Franzens University, Innrain 52a, Innsbruck, Austria. csaf1592@uibk.ac.at
Rainer
Matthias
M
Trojer
Lukas
L
Feuerstein
Isabel
I
Vallant
Rainer Markus
RM
Huck
Christian W
CW
Bakry
Rania
R
Bonn
Günther Karl
GK
D002851:Chromatography, High Pressure Liquid; D019295:Computational Biology; D013058:Mass Spectrometry / Q000379:methods*; D011506:Proteins / Q000737:chemistry*; D040901:Proteomics; D015203:Reproducibility of Results; D012680:Sensitivity and Specificity
D011506:Proteins