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Reversible binding of ethacrynic acid to human serum albumin: Difference circular dichroism study
Author(s) -
Bertucci Carlo,
Nanni Barbara,
Salvadori Piero
Publication year - 1999
Publication title -
chirality
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.43
H-Index - 77
eISSN - 1520-636X
pISSN - 0899-0042
DOI - 10.1002/(sici)1520-636x(1999)11:1<33::aid-chir6>3.0.co;2-u
Subject(s) - chemistry , circular dichroism , human serum albumin , chirality (physics) , binding site , selectivity , albumin , serum albumin , stereochemistry , biochemistry , catalysis , chiral symmetry breaking , physics , quantum mechanics , nambu–jona lasinio model , quark
The reversible binding of ethacrynic acid was characterized by a difference circular dichroism method. A 2/1 stoichiometry was determined for the [drug]/[HSA] (human serum albumin) complex. The reversible binding of ethacrynic acid to HSA determines direct competition with ligands that selectivity bind to site II and to the fatty acid site. Furthermore, indirect competition was shown for ligands for site I (anticooperative) and to site III (cooperative). Chirality 11:33–38, 1999. © 1999 Wiley‐Liss, Inc.