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

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 μM) 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 μM) 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.

journal_name

Biosci Rep

journal_title

Bioscience reports

authors

Eaton JD,Williamson MP

doi

10.1042/BSR20170209

subject

Has Abstract

pub_date

2017-05-11 00:00:00

issue

3

eissn

0144-8463

issn

1573-4935

pii

BSR20170209

journal_volume

37

pub_type

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