Advantages of Molecular Weight Identification during Native MS Screening

Ahad Khan, Anne Bresnick, Sean Cahill, Mark Girvin, Steve Almo, Ronald Quinn

Research output: Contribution to journalArticlepeer-review

2 Scopus citations


Native 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.

Original languageEnglish (US)
Pages (from-to)1201-1212
Number of pages12
JournalPlanta Medica
Issue number16
StatePublished - May 9 2018


  • dereplication
  • ligand-protein complex
  • metabolomics
  • molecular weight
  • native mass spectrometry

ASJC Scopus subject areas

  • Analytical Chemistry
  • Molecular Medicine
  • Pharmacology
  • Pharmaceutical Science
  • Drug Discovery
  • Complementary and alternative medicine
  • Organic Chemistry


Dive into the research topics of 'Advantages of Molecular Weight Identification during Native MS Screening'. Together they form a unique fingerprint.

Cite this