Journal
MOLECULES
Volume 21, Issue 8, Pages -Publisher
MDPI AG
DOI: 10.3390/molecules21080984
Keywords
native MS; fragment-based drug discovery; noncovalent interaction; protein-ligand complex; fragment-based screening; binding stoichiometry; binding specificity; binding affinity; structure-activity relationship
Funding
- National Health and Medical Research Council (NHMRC) [APP1046715]
- Australian Research Committee (ARC) [LP120100485]
- Bill & Melinda Gates Foundation Grand Challenges Explorations Grant [Phase II OPP1035218 GCE]
- Griffith University International Postgraduate Research Scholarship
- Griffith University Postgraduate Research Scholarship
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The advent of native mass spectrometry (MS) in 1990 led to the development of new mass spectrometry instrumentation and methodologies for the analysis of noncovalent protein-ligand complexes. Native MS has matured to become a fast, simple, highly sensitive and automatable technique with well-established utility for fragment-based drug discovery (FBDD). Native MS has the capability to directly detect weak ligand binding to proteins, to determine stoichiometry, relative or absolute binding affinities and specificities. Native MS can be used to delineate ligand-binding sites, to elucidate mechanisms of cooperativity and to study the thermodynamics of binding. This review highlights key attributes of native MS for FBDD campaigns.
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