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dc.contributor.authorKhan, Ahad
dc.contributor.authorBresnick, Anne
dc.contributor.authorCahill, Sean
dc.contributor.authorGirvin, Mark
dc.contributor.authorAlmo, Steve
dc.contributor.authorQuinn, Ronald
dc.date.accessioned2019-05-29T13:14:02Z
dc.date.available2019-05-29T13:14:02Z
dc.date.issued2018
dc.identifier.issn0032-0943
dc.identifier.doi10.1055/a-0608-4870
dc.identifier.urihttp://hdl.handle.net/10072/381928
dc.description.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.
dc.description.peerreviewedYes
dc.languageEnglish
dc.publisherGeorg Thieme Verlag KG
dc.publisher.placeGermany
dc.relation.ispartofpagefrom1201
dc.relation.ispartofpageto1212
dc.relation.ispartofissue16
dc.relation.ispartofjournalPlanta Medica
dc.relation.ispartofvolume84
dc.subject.fieldofresearchPlant Biology not elsewhere classified
dc.subject.fieldofresearchPlant Biology
dc.subject.fieldofresearchPharmacology and Pharmaceutical Sciences
dc.subject.fieldofresearchComplementary and Alternative Medicine
dc.subject.fieldofresearchcode060799
dc.subject.fieldofresearchcode0607
dc.subject.fieldofresearchcode1115
dc.subject.fieldofresearchcode1104
dc.titleAdvantages of Molecular Weight Identification during Native MS Screening
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
gro.facultyGriffith Sciences, School of Environment and Science
gro.hasfulltextNo Full Text
gro.griffith.authorQuinn, Ronald J.
gro.griffith.authorKhan, Md Ahad Ali AA.


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