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Drug-biomacromolecule interaction IX

Effects of pH and ionic strength on the binding of sulfaethidole to bovine serum albumin using circular dichroism

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Abstract

Binding of sulfaethidole to bovine serum albumin (BSA) was studied by circular dichroism. The effects of pH and ionic strength on the binding of sulfaethidole to BSA were investigated It was found that one primary binding site on the BSA was capable of inducing optical activity in the presence of sulfaethidole. Enhancement of the induced ellipticity of sulfaethidole upon addition to BSA was not much affected by the change of pH and ionic strength. Taking the effects of pH and ionic strength into consideration, it seems that the binding of sulfaethidole to BSA was not much affected by electrostatic and ionic interactions. Therefore, it might be assumed that the binding was mainly due to the hydrophobic interactions. Sulfaethidole seems to be a reasonable CD probe for the study of hydrophobic drug interactions.

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Literature Cited

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Authors and Affiliations

  1. College of Pharmacy, Seoul National University, 151, Seoul, Korea

    Chong-Kook Kim, Young Han Won & Sang Nim Kim

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  1. Chong-Kook Kim
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  2. Young Han Won
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  3. Sang Nim Kim
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Kim, CK., Won, Y.H. & Kim, S.N. Drug-biomacromolecule interaction IX. Arch. Pharm. Res. 7, 95–99 (1984). https://doi.org/10.1007/BF02856620

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  • DOI: https://doi.org/10.1007/BF02856620

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