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Identification of multiple proteoforms biomarkers on clinical samples by routine Top-Down approaches

Top-Down approaches have an extremely high biological relevance, especially when it comes to biomarker discovery, but the necessary pre-fractionation constraints are not easily compatible with the robustness requirements and the size of clinical sample cohorts. We have demonstrated that intact prote...

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Detalles Bibliográficos
Autores principales: Vialaret, Jerome, Schmit, Pierre-Olivier, Lehmann, Sylvain, Gabelle, Audrey, Wood, Jason, Bern, Marshall, Paape, Rainer, Suckau, Detlev, Kruppa, Gary, Hirtz, Christophe
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5996497/
https://www.ncbi.nlm.nih.gov/pubmed/29900270
http://dx.doi.org/10.1016/j.dib.2018.03.114
Descripción
Sumario:Top-Down approaches have an extremely high biological relevance, especially when it comes to biomarker discovery, but the necessary pre-fractionation constraints are not easily compatible with the robustness requirements and the size of clinical sample cohorts. We have demonstrated that intact protein profiling studies could be run on UHR-Q-ToF with limited pre-fractionation (Schmit et al., 2017) [1]. The dataset presented herein is an extension of this research. Proteoforms known to play a role in the pathophysiology process of Alzheimer's disease were identified as candidate biomarkers. In this article, mass spectrometry performance of these candidates are demonstrated.