Multi-site binding of epigallocatechin gallate to human serum albumin measured by NMR and isothermal titration calorimetry.
 

Multi-site binding of epigallocatechin gallate to human serum albumin measured by NMR and isothermal titration calorimetry.

http://www.bionmr.com//www.ncbi.nlm....d-highwire.gif http://www.bionmr.com//www.ncbi.nlm....pubmed-pmc.gif Related Articles Multi-site binding of epigallocatechin gallate to human serum albumin measured by NMR and isothermal titration calorimetry.

Biosci Rep. 2017 Jun 30;37(3):

Authors: Eaton JD, Williamson MP

Abstract
The affinity of epigallocatechin gallate (EGCG) for human serum albumin (HSA) was measured in physiological conditions using NMR and isothermal titration calorimetry (ITC). NMR estimated the Ka (self-dissociation constant) of EGCG as 50 mM. NMR showed two binding events: strong (n1=1.8 ± 0.2; Kd1 =19 ± 12 ?M) and weak (n2~20; Kd2 =40 ± 20 mM). ITC also showed two binding events: strong (n1=2.5 ± 0.03; Kd1 =21.6 ± 4.0 ?M) and weak (n2=9 ± 1; Kd2 =22 ± 4 mM). The two techniques are consistent, with an unexpectedly high number of bound EGCG. The strong binding is consistent with binding in the two Sudlow pockets. These results imply that almost all EGCG is transported in the blood bound to albumin and explains the wide tissue distribution and chemical stability of EGCG in vivo.


PMID: 28424370 [PubMed - indexed for MEDLINE]



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