Top-down MS of post-translationally modified proteins

The analysis of misfolded proteins related to amyloid diseases is a longstanding research focus at the MSR:

  • Li, X.; Yu, X.; Costello, C. E.; Lin, C.; O’Connor, P. B. Top-down study of beta2-microglobulin deamidation. Anal. Chem. 2012, 84, 6150-7. Pubmed Link

  • Theberge, R.; Infusini, G.; Tong, W.; McComb, M. E.; Costello, C. E. Top-Down Analysis of Small Plasma Proteins Using an LTQ-Orbitrap. Potential for Mass Spectrometry-Based Clinical Assays for Transthyretin and Hemoglobin. Int J Mass Spectrom 2011, 300, 130-142. Pubmed Link

  • Theberge, R.; Dikler, S.; Heckendorf, C.; Chui, D. H.; Costello, C. E.; McComb, M. E. MALDI-ISD Mass Spectrometry Analysis of Hemoglobin Variants: a Top-Down Approach to the Characterization of Hemoglobinopathies. J Am Soc Mass Spectrom 2015, 26, 1299-310. Pubmed Link

We demonstrated feasibility of top-down MS of glycoproteins:

  • Gault, J.; Malosse, C.; Machata, S.; Millien, C.; Podglajen, I.; Ploy, M. C.; Costello, C. E.; Dumenil, G.; Chamot-Rooke, J. Complete posttranslational modification mapping of pathogenic Neisseria meningitidis pilins requires top-down mass spectrometry. Proteomics 2014, 14, 1141-51. Pubmed Link

  • Bourgoin-Voillard, S.; Leymarie, N.; Costello, C. E. Top-down tandem mass spectrometry on RNase A and B using a Qh/FT-ICR hybrid mass spectrometer. Proteomics 2014, 14, 1174-84. Pubmed Link