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Detection of protein drug complexes under native conditions in the low nM range using Magnetic Resonance Mass Spectrometry (MRMS)
EP38425
Poster Title: Detection of protein drug complexes under native conditions in the low nM range using Magnetic Resonance Mass Spectrometry (MRMS)
Submitted on 08 Mar 2022
Author(s): Matthias Witt, 1 Yongwei Wang 2 Michael Greig, 3 Jia Liu, 4 Changqiang Ke 4 and Yang Ye 4
Affiliations: 1 Bruker Daltonics GmbH & Co. KG, Bremen, Germany 2 Bruker Daltonics Corporation, Shanghai, China 3 Bruker Daltonics Inc, Billerica, MA, USA 4 Shanghai Institute of Materia Medica, CAS
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Abstract: Native mass spectrometric measurements of non covalent protein ligand binding have been reported for more than 25 years [1 3]. This technique combines electrospray ionization(ESI) and gentle desolvation . Magnetic resonance mass spectrometry (MRMS) is a technique to analyze intact biomolecular complexes at high mass resolution by native mass spectrometry (MS). It has been developed as a screening assay for drug discovery as both a primary and secondary screening tool. Native MS offers key advantages for detection of μM to low nM affinity complexes due to high sensitivity for proteins up to 100 kDa . This technique does not require modifications of the protein target and more importantly, it is the only biological assay which allows direct visualization of all molecules (target, substrates, products, byproducts, co factors, isoforms) of interest in solution including the detection of non specific interactions.Summary: Magnetic resonance mass spectrometry (MRMS) is a technique to analyze intact biomolecular complexes at high mass resolution by native mass spectrometry (MS). It has been developed as a screening assay for drug discovery as both a primary and secondary screening tool. References: [1] Ganem B, TsyrLi Y, Henion JD (1991). J. Am. Chem. Soc ., 113, 6294 6296;
[2] Hofner G, Wanner K (2003). J. Angew . Chem. Int. Ed. Engl. 42, 5235 5237;
[3] Chrysanthopoulos PK, Mujumdar P, Woods LA, Dolezal O, Ren B, Peat TS, Poulsen SA (2017) J. Med. Chem., 60, 7333 7349; [4] Iyer R, Barrese AA, Parakh S, Parker CN, Tripp BC (2006, Journal of Biomolecular Screening, 11, 782.
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