Mass Spectrometry Reviews· 2026Q1· Review
Keeping It Native: Non‐Denaturing Approaches to Top‐Down Protein Mass Spectrometry
- 0citations
- Q1SCImago
- 2026year
Short summary
Non-denaturing mass spectrometry can now directly characterize protein variants (proteoforms) and their transient interactions, overcoming limitations of traditional denaturing methods.
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Key points
- Non-denaturing mass spectrometry directly characterizes protein variants (proteoforms) and their transient interactions.
- This method preserves information on protein folding, protein-protein binding, and protein-ligand interactions, unlike denaturing approaches.
- Applications span ligand binding and drug discovery, structural biology, and proteomics with bioinformatics.
AI-generated from the title and abstract; the full text is not read.
Abstract
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 authors' abstract, as published at the source. Mass Spectrometry Reviews, 2026 · DOI ↗
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Field: Spectroscopy
SpectroscopyChemistry