The in Situ Acetylation of an Immobilized Human Serum Albumin Chiral Stationary Phase for High-Performance Liquid Chromatography in the Examination of Drug–Protein Binding Phenomena
作者： Terence A. G. Noctor , Irving W. Wainer
关键词: Derivatization 、 Human serum albumin 、 Chiral resolution 、 Chemical modification 、 High-performance liquid chromatography 、 Binding site 、 Albumin 、 Chemistry 、 Plasma protein binding 、 Chromatography
摘要: The in situ modification of an immobilized human serum albumin (HSA) high-performance liquid chromatographic chiral stationary phase by p-nitrophenyl acetate is reported. This procedure, which thought to affect primarily a single reactive tyrosine residue within the protein structure, influenced retention and enantioselectivity factors wide range solutes. For certain solutes, increases both capacity factor resolution were observed. Ultrafiltration studies on representative test solutes using free HSA, treated similar manner protein, gave results as observations, indicating that latter effects are not artifactual immobilization. effect HSA binding behavior drugs reportedly sharing site predominantly affected derivatization, namely, indole–benzodiazepine site, varied greatly. observation suggests area single, tightly structurally defined site.
springer.com
sci-hub.se 参考文章(14)
D. M. Johns, Binding to cellulose derivatives Springer, Dordrecht. pp. 166- 176 ,(1989) , 10.1007/978-94-009-0861-1_9
U Kragh-Hansen, Molecular aspects of ligand binding to serum albumin. Pharmacological Reviews. ,vol. 33, pp. 17- 53 ,(1981)
D. Carter, X. He, Structure of human serum albumin Science. ,vol. 249, pp. 302- 303 ,(1990) , 10.1126/SCIENCE.2374930
Klaus J. Fehske, Walter E. Müller, Uwe Wollert, A highly reactive tyrosine residue as part of the indole and benzodiazepine binding site of human serum albumin Biochimica et Biophysica Acta (BBA) - Protein Structure. ,vol. 577, pp. 346- 359 ,(1979) , 10.1016/0005-2795(79)90038-2
G.E. Means, Hua-Lin Wu, The reactive tyrosine residue of human serum albumin: Characterization of its reaction with diisopropylfluorophosphate Archives of Biochemistry and Biophysics. ,vol. 194, pp. 526- 530 ,(1979) , 10.1016/0003-9861(79)90647-7
Klaus J. Fehske, Walter E. Müller, Uwe Wollert, The location of drug binding sites in human serum albumin. Biochemical Pharmacology. ,vol. 30, pp. 687- 692 ,(1981) , 10.1016/0006-2952(81)90151-9
Enrico Domenici, Carlo Bertucci, Piero Salvadori, Sylvie Motellier, Irving W. Wainer, Immobilized serum albumin: rapid HPLC probe of stereoselective protein-binding interactions. Chirality. ,vol. 2, pp. 263- 268 ,(1990) , 10.1002/CHIR.530020412
E. Domenici, C. Bertucci, P. Salvadori, G. Félix, I. Cahagne, S. Motellier, I. W. Wainer, Synthesis and chromatographic properties of an HPLC chiral stationary phase based upon human serum albumin Chromatographia. ,vol. 29, pp. 170- 176 ,(1990) , 10.1007/BF02268706
T. A. G. Noctor, G. Felix, I. W. Wainer, Stereochemical resolution of enantiomeric 2-aryl propionic acid non-steroidal anti-inflammatory drugs on a human serum albumin based high-performance liquid chromatographic chiral stationary phase Chromatographia. ,vol. 31, pp. 55- 59 ,(1991) , 10.1007/BF02290496
K.J. Fehske, W.E. Müller, U. Wollert, Direct demonstration of the highly reactive tyrosine residue of human serum albumin located in fragment 299-585. Archives of Biochemistry and Biophysics. ,vol. 205, pp. 217- 221 ,(1980) , 10.1016/0003-9861(80)90101-0