scholarly journals Distinct classes of multi-subunit heterogeneity: analysis using Fourier Transform methods and native mass spectrometry

The Analyst ◽  
2020 ◽  
Vol 145 (13) ◽  
pp. 4688-4697 ◽  
Author(s):  
Sean P. Cleary ◽  
James S. Prell

A classification scheme for heterogeneous multi-subunit assemblies is presented along with theory and experimental demonstration of their characterization using mass spectrometry and Fourier-Transform analysis methods.

Planta Medica ◽  
2018 ◽  
Vol 84 (16) ◽  
pp. 1201-1212
Author(s):  
Ahad Khan ◽  
Anne Bresnick ◽  
Sean Cahill ◽  
Mark Girvin ◽  
Steve Almo ◽  
...  

AbstractNative mass spectrometry detection of ligand-protein complexes allowed rapid detection of natural product binders of apo and calcium-bound S100A4 (a member of the metal binding protein S100 family), T cell/transmembrane, immunoglobulin (Ig), and mucin protein 3, and T cell immunoreceptor with Ig and ITIM (immunoreceptor tyrosine-based inhibitory motif) domains precursor protein from extracts and fractions. Based on molecular weight common hits were detected binding to all four proteins. Seven common hits were identified as apigenin 6-C-β-D-glucoside 8-C-α-L-arabinoside, sweroside, 4′,5-dihydroxy-7-methoxyflavanone-6-C-rutinoside, loganin acid, 6-C-glucosylnaringenin, biochanin A 7-O-rutinoside and quercetin 3-O-rutinoside. Mass guided isolation and NMR identification of hits confirmed the mass accuracy of the ligand in the ligand-protein MS complexes. Thus, molecular weight ID from ligand-protein complexes by electrospray ionization Fourier transform mass spectrometry allowed rapid dereplication. Native mass spectrometry using electrospray ionization Fourier transform mass spectrometry is a tool for dereplication and metabolomics analysis.


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