Differences in heat stability and ligand binding among ?-lactoglobulin genetic variants A, B and C using (1)H NMR and fluorescence quenching.
 

Differences in heat stability and ligand binding among ?-lactoglobulin genetic variants A, B and C using (1)H NMR and fluorescence quenching.

http://www.bionmr.com//www.ncbi.nlm....PubMedLink.gif Related Articles Differences in heat stability and ligand binding among ?-lactoglobulin genetic variants A, B and C using (1)H NMR and fluorescence quenching.

Biochim Biophys Acta. 2014 Feb 28;

Authors: Keppler JK, Sönnichsen FD, Lorenzen PC, Schwarz K

Abstract
The structure of ?-lactoglobulin (?-LG) is well characterized, but the exact location of binding sites for retinol and (-)-epigallocatechingallate (EGCG) are still a subject of controversy. Here we report that the genetic ?-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 ?-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 ?-LG as nanotransporter.


PMID: 24590114 [PubMed - as supplied by publisher]



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