Abstract
To investigate the protein binding characteristics of ibuprofenlysine, the effects of drug conentration, pH, ionic strength and protein concentration on the binding of drug to protein were studied by fluorescence probe method. The conformational change of protein was investigated by circular dichroism(CD) measurement. As the concentration of drug increases, the association constant decreases. These may be due to complex formation of the probe and drug, or the interaction of the protein-probe complex and drug. The association constant for ibuprofenlysine increased with increasing protein concentration. These findings suggest a sharing of one ibuprofenlysine molecule by more than one protein molecule in the binding. The binding between ibuprofenlysine and protein was dependent on pH and ionic strength. It seems that both hydrophobic binding and some electrostatic forces are involved in the binding of ibuprofenlysine to protein.
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This work was partly supported by the research grant from the Korea Science & Engineering Foundation in 1980.
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Kim, CK., Ahn, H.Y. Drug-biomacromolecule interaction I. Arch. Pharm. Res. 4, 99–107 (1981). https://doi.org/10.1007/BF02855752
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DOI: https://doi.org/10.1007/BF02855752