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dc.contributor.authorPedro, Liliana
dc.contributor.authorVan Voorhis, Wesley C
dc.contributor.authorQuinn, Ronald J
dc.date.accessioned2017-07-03T22:35:57Z
dc.date.available2017-07-03T22:35:57Z
dc.date.issued2016
dc.identifier.issn1044-0305
dc.identifier.doi10.1007/s13361-016-1417-x
dc.identifier.urihttp://hdl.handle.net/10072/100295
dc.description.abstractElectrospray ionization mass spectrometry (ESI-MS) binding studies between proteins and ligands under native conditions require that instrumental ESI source conditions are optimized if relative solution-phase equilibrium concentrations between the protein–ligand complex and free protein are to be retained. Instrumental ESI source conditions that simultaneously maximize the relative ionization efficiency of the protein–ligand complex over free protein and minimize the protein–ligand complex dissociation during the ESI process and the transfer from atmospheric pressure to vacuum are generally specific for each protein–ligand system and should be established when an accurate equilibrium dissociation constant (KD) is to be determined via titration. In this paper, a straightforward and systematic approach for ESI source optimization is presented. The method uses statistical design of experiments (DOE) in conjunction with response surface methodology (RSM) and is demonstrated for the complexes between Plasmodium vivax guanylate kinase (PvGK) and two ligands: 5′-guanosine monophosphate (GMP) and 5′-guanosine diphosphate (GDP). It was verified that even though the ligands are structurally similar, the most appropriate ESI conditions for KD determination by titration are different for each.
dc.description.peerreviewedYes
dc.languageEnglish
dc.language.isoeng
dc.publisherElsevier
dc.relation.ispartofpagefrom1520
dc.relation.ispartofpageto1530
dc.relation.ispartofjournalJournal of the American Society for Mass Spectrometry
dc.relation.ispartofvolume27
dc.subject.fieldofresearchAnalytical chemistry
dc.subject.fieldofresearchMedicinal and biomolecular chemistry
dc.subject.fieldofresearchMedicinal and biomolecular chemistry not elsewhere classified
dc.subject.fieldofresearchPhysical chemistry
dc.subject.fieldofresearchcode3401
dc.subject.fieldofresearchcode3404
dc.subject.fieldofresearchcode340499
dc.subject.fieldofresearchcode3406
dc.titleOptimization of Electrospray Ionization by Statistical Design of Experiments and Response Surface Methodology: Protein–Ligand Equilibrium Dissociation Constant Determinations
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
dcterms.licensehttp://creativecommons.org/licenses/by/4.0/
dc.description.versionVersion of Record (VoR)
gro.facultyGriffith Sciences, Griffith Institute for Drug Discovery
gro.rights.copyright© The Author(s) 2016. This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.
gro.hasfulltextFull Text
gro.griffith.authorQuinn, Ronald J.


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