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dc.contributor.authorPLET, Benoit
dc.contributor.authorDELCAMBRE, Adeline
dc.contributor.authorCHAIGNEPAIN, Stephane
dc.contributor.authorSCHMITTER, Jean-Marie
dc.date.accessioned2020-09-03T08:01:57Z
dc.date.available2020-09-03T08:01:57Z
dc.date.issued2015
dc.identifier.issn0040-4020
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/10936
dc.description.abstractEnEnergy Resolved Mass Spectrometry of peptide-polyphenol complexes was used to characterize the affinity of a selection of 21 polyphenols for peptides from human salivary basic Proline Rich Proteins (PRPb) having variable lengths. The affinity scale determined in the gas phase for a 14 amino acid long peptide is in agreement with results obtained in the liquid phase with the same PRPb probe immobilized on magnetic beads and those of sensory descriptive analysis of polyphenols astringency. (C) 2015 Elsevier Ltd. All rights reserved.
dc.language.isoen
dc.title.enAffinity ranking of peptide-polyphenol non-covalent assemblies by mass spectrometry approaches
dc.typeArticle de revue
dc.identifier.doi10.1016/j.tet.2015.02.015
dc.subject.halChimie/Matériaux
bordeaux.journalTetrahedron
bordeaux.page3007-3011
bordeaux.volume71
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN) - UMR 5248*
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN, UMR 5248)
bordeaux.issue20
bordeaux.institutionUniversité de Bordeaux
bordeaux.institutionBordeaux INP
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Tetrahedron&rft.date=2015&rft.volume=71&rft.issue=20&rft.spage=3007-3011&rft.epage=3007-3011&rft.eissn=0040-4020&rft.issn=0040-4020&rft.au=PLET,%20Benoit&DELCAMBRE,%20Adeline&CHAIGNEPAIN,%20Stephane&SCHMITTER,%20Jean-Marie&rft.genre=article


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