Protein binding of chloroquine enantiomers and desethylchloroquine.

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Ofori-Adjei D, Ericsson O, Lindstrom B, Sjoqvist F

Protein binding of chloroquine enantiomers and desethylchloroquine.

Br J Clin Pharmacol. 1986 Sep;22(3):356-8. doi: 10.1111/j.1365-2125.1986.tb02900.x.

PubMed ID

3768249 [ View in PubMed

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Abstract

The protein binding of racemic chloroquine, its enantiomers and desethylchloroquine to plasma, purified human albumin, and alpha 1-acid glycoprotein (alpha 1-AGP) was determined by equilibrium dialysis. The binding was not concentration dependent. (+)-Chloroquine bound more to plasma (66.6 +/- 1.9%) and albumin (45.9 +/- 0.8%) than (-)-chloroquine (48.5 +/- 2.4% and 35.3 +/- 0.6%, respectively). These differences were statistically significant. (-)-Chloroquine bound more to alpha 1-AGP (47.5 +/- 0.7%) than (+)-chloroquine (34.5 +/- 0.5%). The binding of desethylchloroquine to alpha 1-AGP is higher than to albumin (38.9 +/- 0.9% and 21.1 +/- 0.4%, respectively.

DrugBank Data that Cites this Article

Drugs

Chloroquine

Drug Carriers

Drug	Carrier	Kind	Organism	Pharmacological Action	Actions
Chloroquine	alpha1-acid glycoprotein (Protein Group)	Protein group	Humans	Unknown	Binder	Details
Chloroquine	Serum albumin	Protein	Humans	Unknown	Binder	Details