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Application of affinity capillary electrophoresis for the determination of binding and thermodynamic constants of enediynes with bovine serum albumin
Author(s) -
ElShafey Ahmed,
Zhong Huijuan,
Jones Graham,
Krull Ira S.
Publication year - 2002
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/1522-2683(200203)23:6<945::aid-elps945>3.0.co;2-f
Subject(s) - bovine serum albumin , enediyne , capillary electrophoresis , chemistry , binding constant , electrophoresis , chromatography , serum albumin , carboxylic acid , analytical chemistry (journal) , binding site , stereochemistry , organic chemistry , biochemistry
The binding constants and thermodynamic properties of a series of novel enediyne compounds with bovine serum albumin (BSA) were determined. The enediynes were synthesized, characterized, and then studied by affinity capillary electrophoresis (ACE) methods to derive these recognition parameters. Change in electrophoretic mobility of BSA as a function of enediyne concentration was determined at 25°C providing binding constants of 1.76×10 5 , 1.14×10 5 , and 0.68×10 5 M –1 for enediynephenylalanine carboxylic acid, enediynephenylalanine methyl ester, and enediyne carboxylic acid, respectively. The binding constant for the enediynephenylalanine carboxylic acid was in good agreement with that obtained using conventional methodology. Binding constants for the interaction of enediynes with BSA decreased with an increase in temperature. Van't Hoff plots showed a direct correlation between intensity of the binding constant and the sign and magnitude of various thermodynamic parameters (Δ G , Δ S , and/or Δ H ).