Dr Theodora Katsila, Head of the Biomarker Discovery: Translational Research Laboratory (PLEION Lab) at the Institute of Chemical Biology  (ICB/NHRF), participated in the 25th Human Proteome Organizat...

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ABSTRACT Top-down proteomics and top-down mass spectrometry approaches provide direct characterization of proteoforms; the specific molecular forms of proteins, including post-translational modifications, truncations, alternative splicing, and sequence variants. To date, most top-down studies have been performed under denaturing conditions, losing critical information about protein folding and noncovalent protein-protein and protein-ligand interactions. However, recent efforts to apply non-denaturing, or native, ionization to top-down mass spectrometry and top-down proteomics have shown substantial promise for characterizing these higher-order and more transient interactions. This review covers progress over the last 35 years in non-denaturing top-down approaches and addresses the inherent strengths and challenges of the technique. We cover three major areas of applications: (1) Ligand binding and drug discovery, (2) Structural biology, and (3) Proteomics aspects and bioinformatics.

The field has evolved and grown extensively over the past decade as far as the various methods employed, the range of applications, and the differing organizations that are pursuing proteoform knowledge and knowhow.