Binding position of azathioprine with bovine serum albumin determined by measuring nuclear magnetic resonance relaxation time.

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Tanaka M, Asahi Y, Masuda S, Ota T

Binding position of azathioprine with bovine serum albumin determined by measuring nuclear magnetic resonance relaxation time.

Chem Pharm Bull (Tokyo). 1991 Nov;39(11):2771-4. doi: 10.1248/cpb.39.2771.

PubMed ID

1799934 [ View in PubMed

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Abstract

The interaction between azathioprine (AZ) and bovine serum albumin (BSA) is mainly due to hydrophobic binding according to the dependence of the binding constant on the ionic strength obtained by equilibrium dialysis. The binding constant and partition coefficient of AZ were smaller than those of warfarin, phenylbutazone and ibuprofen. Little variation in the proton chemical shift of AZ was observed whether there was an absence or presence of BSA (7.25 x 10(-5) M). The spin-lattice relaxation time (T1) of AZ decreased in the presence of BSA to 6-22%. The spin-spin relaxation rate (1/T2) of AZ increased 16-24 times for the methyl group and the imidazole ring and 8-13 times for the purine ring in the presence of BSA. The ratio of the spin-spin relaxation rate of the free AZ to the bound AZ ((1/T2)b/(1/T2)f) of the methyl group and the imidazole ring was 2-3 times larger than that of the purine ring. The binding of AZ to BSA was concluded to be mainly at the methyl group on the imidazole ring of AZ.

DrugBank Data that Cites this Article

Drug Carriers

Drug	Carrier	Kind	Organism	Pharmacological Action	Actions
Azathioprine	Serum albumin	Protein	Humans	Unknown	Binder	Details