Please use this identifier to cite or link to this item: http://doi.org/10.25358/openscience-6256
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dc.contributor.authorWenskowsky, Lea-
dc.contributor.authorWagner, Michael-
dc.contributor.authorReusch, Johannes-
dc.contributor.authorSchreuder, Herman-
dc.contributor.authorMatter, Hans-
dc.contributor.authorOpatz, Till-
dc.contributor.authorPetry, Stefan Matthias-
dc.date.accessioned2021-08-09T10:22:48Z-
dc.date.available2021-08-09T10:22:48Z-
dc.date.issued2020-
dc.identifier.urihttps://openscience.ub.uni-mainz.de/handle/20.500.12030/6266-
dc.description.abstractPhysiological processes rely on initial recognition events between cellular components and other molecules or modalities. Biomolecules can have multiple sites or mode of interaction with other molecular entities, so that a resolution of the individual binding events in terms of spatial localization as well as association and dissociation kinetics is required for a meaningful description. Here we describe a trichromatic fluorescent binding- and displacement assay for simultaneous monitoring of three individual binding sites in the important transporter and binding protein human serum albumin. Independent investigations of binding events by X-ray crystallography and time-resolved dynamics measurements (switchSENSE technology) confirm the validity of the assay, the localization of binding sites and furthermore reveal conformational changes associated with ligand binding. The described assay system allows for the detailed characterization of albumin-binding drugs and is therefore well-suited for prediction of drug-drug and drug-food interactions. Moreover, conformational changes, usually associated with binding events, can also be analyzed.en_GB
dc.language.isoengde
dc.rightsCC BY-NC-ND*
dc.rights.urihttps://creativecommons.org/licenses/by-nc-nd/4.0/*
dc.subject.ddc540 Chemiede_DE
dc.subject.ddc540 Chemistry and allied sciencesen_GB
dc.titleResolving binding events on the multifunctional human serum albuminen_GB
dc.typeZeitschriftenaufsatzde
dc.identifier.doihttp://doi.org/10.25358/openscience-6256-
jgu.type.dinitypearticleen_GB
jgu.type.versionPublished versionde
jgu.type.resourceTextde
jgu.organisation.departmentFB 09 Chemie, Pharmazie u. Geowissensch.de
jgu.organisation.number7950-
jgu.organisation.nameJohannes Gutenberg-Universität Mainz-
jgu.rights.accessrightsopenAccess-
jgu.journal.titleChemMedChemde
jgu.journal.volume15de
jgu.journal.issue9de
jgu.pages.start738de
jgu.pages.end743de
jgu.publisher.year2020-
jgu.publisher.nameWiley-VCHde
jgu.publisher.placeWeinheim u.a.de
jgu.publisher.urihttps://doi.org/10.1002/cmdc.202000069de
jgu.publisher.issn1860-7187de
jgu.organisation.placeMainz-
jgu.subject.ddccode540de
jgu.publisher.doi10.1002/cmdc.202000069
jgu.organisation.rorhttps://ror.org/023b0x485
Appears in collections:JGU-Publikationen

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