Keppler, Julia K., Sönnichsen, Frank, Lorenzen, Peter-Christian and Schwarz, Karin (2014) Differences in heat stability and ligand binding among beta-lactoglobulin genetic variants A, B and C using H-1 NMR and fluorescence quenching. Biochimica Et Biophysica Acta-Proteins and Proteomics, 1844 (6). pp. 1083-1093. DOI 10.1016/j.bbapap.2014.02.007.

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Abstract

The structure of beta-lactoglobulin (beta-LG) is well characterized, but the exact location of binding sites for retinol and (-)-epigallocatechingallate (EGCG) is still a subject of controversy. Here we report that the genetic beta-LG variants A, B and C have different numbers of binding sites for retinol (almost completely incorporated into the calyx), as well as for EGCG (exclusively bound on the surface), and beta-LG A with the most binding sites for EGCG, which include Tyr(20), Phe(151) and His(59). Upon heat related unfolding, new unspecific binding sites emerge, which are comparable in number and affinity for retinol and for EGCG, and in the three genetic variants A, B and C. The findings of our study provide new insights into the use of beta-Lo as nanotransporter. (C) 2014 Elsevier B.V. All rights reserved.

Document Type:	Article
Keywords:	β-Lactoglobulin, Genetic variant, Fluorescence quenching, Epigallocatechingallate binding, Retinol binding, Protein–ligand interactionProtein heat stability
Research affiliation:	Kiel University Kiel University > Kiel Marine Science OceanRep > The Future Ocean - Cluster of Excellence
Refereed:	Yes
Open Access Journal?:	No
Publisher:	Elsevier
Projects:	Future Ocean
Date Deposited:	30 Mar 2015 12:28
Last Modified:	23 Sep 2019 21:32
URI:	https://oceanrep.geomar.de/id/eprint/27743

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