Authors:	Wenskowsky, Lea Wagner, Michael Reusch, Johannes Schreuder, Herman Matter, Hans Opatz, Till Petry, Stefan Matthias
Title:	Resolving binding events on the multifunctional human serum albumin
Online publication date:	9-Aug-2021
Year of first publication:	2020
Language:	english
Abstract:	Physiological 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.
DDC:	540 Chemie 540 Chemistry and allied sciences
Institution:	Johannes Gutenberg-Universität Mainz
Department:	FB 09 Chemie, Pharmazie u. Geowissensch.
Place:	Mainz
ROR:	https://ror.org/023b0x485
DOI:	http://doi.org/10.25358/openscience-6256
Version:	Published version
Publication type:	Zeitschriftenaufsatz
License:	CC BY-NC-ND
Information on rights of use:	https://creativecommons.org/licenses/by-nc-nd/4.0/
Journal:	ChemMedChem 15 9
Pages or article number:	738 743
Publisher:	Wiley-VCH
Publisher place:	Weinheim u.a.
Issue date:	2020
ISSN:	1860-7187
Publisher URL:	https://doi.org/10.1002/cmdc.202000069
Publisher DOI:	10.1002/cmdc.202000069
Appears in collections:	JGU-Publikationen