albumin - publications

Predict more albumin - ligand interactions now!

1. Acta Pharmacol Sin. 2012 May;33(5):710-6. doi: 10.1038/aps.2012.8.

Stereoselective binding of mexiletine and ketoprofen enantiomers with human serum
albumin domains.

Shi D, Jin YX, Tang YH, Hu HH, Xu SY, Yu LS, Jiang HD, Zeng S.

Department of Drug Metabolism and Pharmaceutical Analysis, College of
Pharmaceutical Sciences, Zhejiang University, Hangzhou 310058, China.

AbstractAim:To investigate the stereoselective binding of mexiletine or
ketoprofen enantiomers with different recombinant domains of human serum albumin
(HSA).Methods:Three domains (HSA DOM I, II and III) were expressed in Pichia
pastoris GS115 cells. Blue Sepharose 6 Fast Flow was employed to purify the
recombinant HSA domains. The binding properties of the standard ligands,
digitoxin, phenylbutazone and diazepam, and the chiral drugs to HSA domains were
investigated using ultrafiltration. The concentrations of the standard ligands,
ketoprofen and mexiletine were analyzed with HPLC.Results:The recombinant HSA
domains were highly purified as shown by SDS-PAGE and Western blotting analyses.
The standard HSA ligands digitoxin, phenylbutazone and diazepam selectively binds
to DOM I, DOM II and DOM III, respectively. For the chiral drugs, R-ketoprofen
showed a higher binding affinity toward DOM III than S-ketoprofen, whereas
S-mexiletine bound to DOM II with a greater affinity than
R-mexiletine.Conclusion:The results demonstrate that HSA DOM III possesses the
chiral recognition ability for the ketoprofen enantiomers, whereas HSA DOM II
possesses that for the mexiletine enantiomers.

PMID: 22555373 [PubMed - in process]