Hydration of human and bovine serum albumin complexes with chlorophyllin investigated by differential ehf dielectrometry
Keywords:
serum albumin, chlorophyllin, serum albumin-chlorophyllin complex, hydration, EHF dielectrometryAbstract
This study is designed to examine the hydration effects accompanying the interaction between
chlorophyllin (CHLN), a potent inhibitor of experimental carcinogenesis, and human and bovine serum
albumins (HSA and BSA) in aqueous solutions using differential dielectric method. This method allows
studying both dielectric characteristics and hydration of the compounds under investigation. We show
that for both complexes the process of complex formation is accompanied by changes of dielectric
parameters. We also present calculations of the hydration of proteins and their complexes with ligand,
which were carried out basing on the model concepts. We found that formation of CHLN complex with
fatty acids free BSA is accompanied by a significant decrease of hydration while no notable hydration
changes takes place upon formation of CHLN complex with HSA containing fatty acids. The former
effect indicates that redistribution of free and bound water molecules takes place during the formation of
the complex. The possible causes of effects observed are discussed.
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