Authors: Carolina Jullian Muriel Alfaro Gerald ZapataTorres Claudio OleaAzar
Publish Date: 2010/08/14
Volume: 39, Issue: 8, Pages: 1168-1177
Abstract
The formation of the complexes of galangin GAL with native βcyclodextrin βCD and with its substituted counterparts such as dimethylβCD DMβCD and hydroxypropylβCD HPβCD was studied by fluorescence spectra in aqueous medium The binding association constants K a of the complexes were determined at different temperatures The formation constants obtained have the following trend upon complex formation at the three temperatures studied HPβCD DMβCD βCD The thermodynamic data for the inclusion of GAL in DMβCD and HPβCD indicated that is mainly enthalpy driven whereas for βCD it is an entropydriven processThe antioxidant ability studies of GAL and CD complexes showed practically no change in its activity when the βcyclodextrin complex is formed The decrease in the T eq observed for GALDMβCD and GALHPβCD in comparison with GALβCD could be due to effective protection of the phenol group in the cyclodextrin cavity which is in agreement with molecular modeling studies
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