Journal
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
Volume 1844, Issue 6, Pages 1083-1093Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbapap.2014.02.007
Keywords
beta-Lactoglobulin; Genetic variant; Fluorescence quenching; Epigallocatechingallate binding; Retinol binding; Protein-ligand interaction; Protein heat stability
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Funding
- BMBF
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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.
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