Binding Position of Azathioprine with Bovine Serum Albumin Determined by Measuring Nuclear Magnetic Resonance Rlaxation Time

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Description

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 (7.25×10^<-5> M). The spin-lattice relaxation time (T_1) of AZ decreased in the presence of BSA to 6-22%. The spin-spin relaxation rate (1/T_2) 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/T_2)_b/(1/T_2)_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.

Journal

  • Chem. Pharm. Bull.

    Chem. Pharm. Bull. 39 2771-2774, 1991

    The Pharmaceutical Society of Japan

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Details 詳細情報について

  • CRID
    1572824502321996544
  • NII Article ID
    110003628966
  • NII Book ID
    AA00602100
  • ISSN
    00092363
  • Text Lang
    en
  • Data Source
    • CiNii Articles

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