Binding of vinca alkaloid analogues to human serum albumin and to alpha 1-acid glycoprotein |
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Authors: | I Fitos J Visy M Simonyi |
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Institution: | Central Research Institute for Chemistry, Hungarian Academy of Sciences, Budapest. |
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Abstract: | The binding of a series of vinca alkaloid analogues having eburnane or indolo2,3-a]quinolizidine skeletons was studied with human serum albumin (HSA) by affinity chromatography and with alpha 1-acid glycoprotein by means of competition experiments. On HSA the binding occurs at the benzodiazepine-indole binding site via hydrophobic interaction and shows slight stereoselectivity preferring the trans isomers. The binding to alpha 1-AGP proved to be highly stereoselective in favour of the trans isomers having 3(S),16(R)eburnane or 1(R),12b(S)indolo2,3-a]quinolizidine absolute configurations. |
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