Improved chromatographic performance of a modified human albumin based stationary phase.

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Bertucci C, Wainer IW

Improved chromatographic performance of a modified human albumin based stationary phase.

Chirality. 1997;9(4):335-40.

PubMed ID
9275312 [ View in PubMed
]
Abstract

Derivatization of the free cys34 in human serum albumin (HSA) anchored to a silica matrix has been performed by in situ reaction with ethacrynic acid. This modification, which is reported to occur under physiological conditions, gives rise in practice to a new column with different binding properties with respect to the column based on the native protein. Significant differences were observed in the binding of drugs known to bind to site I, (R)-(S)-warfarin and phenylbutazone, and to site II, 1,4-benzodiazepin-2-ones and nonsteroidal anti-inflammatory agents. In particular, the chromatographic retentions markedly decreased for most of the drugs, and, in the case of chiral compounds, significant differences were often observed in the behavior of the two enantiomers, with higher values of enantioselectivity obtained for some of the examined compounds. Furthermore, the noncovalent binding of ethacrynic acid to the protein modifies the binding properties of the albumin.

DrugBank Data that Cites this Article

Drug Carriers
DrugCarrierKindOrganismPharmacological ActionActions
DiazepamSerum albuminProteinHumans
No
Not AvailableDetails
Etacrynic acidSerum albuminProteinHumans
Unknown
Not AvailableDetails
FenoprofenSerum albuminProteinHumans
Unknown
Not AvailableDetails
IndomethacinSerum albuminProteinHumans
Unknown
Not AvailableDetails
KetazolamSerum albuminProteinHumans
Unknown
Not AvailableDetails
OxyphenbutazoneSerum albuminProteinHumans
Unknown
Not AvailableDetails
PiroxicamSerum albuminProteinHumans
Unknown
Not AvailableDetails
Salicylic acidSerum albuminProteinHumans
No
Other/unknown
Details
WarfarinSerum albuminProteinHumans
No
Binder
Regulator
Details