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Drug Binding to α1-Acid Glycoprotein Studied by Circular Dichroism

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Abstract

The interactions of acidic and basic drugs with α1-acid glycoprotein (α1-AGP) were investigated using circular dichroism (CD) measurements. Extrinsic Cotton effects were generated by the binding of drugs to α1-AGP. The CD data suggested the presence of a single binding site on the α1-AGP molecule. The induced ellipticities of the acidic drug–α1-AGP system decreased with increasing pH, while the ellipticities for the basic drugs increased with pH. The ellipticities for all drugs were reduced by the addition of fatty acids. Furthermore, the induced ellipticities decreased in the presence of cesium chloride for basic drugs bound to α1-AGP. The extrinsic Cotton effects therefore appear to result from hydrophobic interaction with α1-AGP for the acidic drugs and from hydrophobic and electrostatic interactions for the basic drugs.

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Authors and Affiliations

  1. Faculty of Pharmaceutical Sciences, Kumamoto University, Kumamoto, 862, Japan

    Masaki Otagiri

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  1. Masaki Otagiri
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  2. Ryuji Yamamichi
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  3. Toru Marayama
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  4. Teruko Imai
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  5. Ayaka Suenaga
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  6. Yorishige Imamura
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  7. Kazuhiko Kimachi
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Otagiri, M., Yamamichi, R., Marayama, T. et al. Drug Binding to α1-Acid Glycoprotein Studied by Circular Dichroism. Pharm Res 6, 156–159 (1989). https://doi.org/10.1023/A:1015936710919

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