Quantitative matrix-assisted laser desorption ionization-fourier transform ion cyclotron resonance (MALDI-FT-ICR) peptide profiling and identification of multiple-sclerosis-related proteins
We introduce a matrix-assisted laser desorption ionization-Fourier transform ion cyclotron resonance (MALDI-FT-ICR) method for quantitative peptide profiling, using peak height as a measure for abundance. Relative standard deviations in peak height of peptides spiked over 3 orders of magnitude in concentration were below 10% and allowed for accurate comparisons between multiple sclerosis and controls. Application on a set of 163 cerebrospinal fluid (CSF) samples showed significantly differential abundant peptides, which were subsequently identified into proteins (e.g., chromogranin A, clusterin, and complement C3). © 2009 American Chemical Society.
|Keywords||Cerebrospinal fluid, Clinically isolated syndrome, Differentially abundant peptides, Innate immunity, Multiple sclerosis, Proteomics, adult, amino acid sequence, article, chromogranin A, clusterin, complement component C3, controlled study, enzyme linked immunosorbent assay, female, human, ion cyclotron resonance mass spectrometry, major clinical study, male, matrix assisted laser desorption ionization fourier transform ion cyclotron resonance, matrix assisted laser desorption ionization time of flight mass spectrometry, multiple sclerosis, peptide analysis, priority journal|
|Persistent URL||dx.doi.org/10.1021/pr8010155, hdl.handle.net/1765/16460|
|Journal||Journal of Proteome Research|
Stoop, M.P, Dekker, L.J.M, Titulaer, M.K, Lamers, R.J.A.N, Burgers, P.C, Smitt, P.A, … Hintzen, R.Q. (2009). Quantitative matrix-assisted laser desorption ionization-fourier transform ion cyclotron resonance (MALDI-FT-ICR) peptide profiling and identification of multiple-sclerosis-related proteins. Journal of Proteome Research, 8(3), 1404–1414. doi:10.1021/pr8010155