Interaction of alkylresorcinols with proteins.

Abstract

Alkylresorcinol homologs form stable monomolecular layers at air-water interface. Their interaction with proteins present in the subphase results in an increase of alkylresorcinol molecular packing in the extent dependent upon the protein studied. Strongest effects were observed for proteins with large hydrophobic regions, e.g. glycophorin or serum albumin. Interaction of proteins with alkylresorcinol monolayers is stronger than with phospholipids. A decrease and a shift of intrinsic protein fluorescence upon interaction with the compounds studied support their involvement in alteration of hydrophobic regions. For trypsin, 50% quenching was observed at the alkylresorcinol/trypsin ratio of 0.75. Concomitantly, an apparent inhibition of the enzymatic activity was noted. These results indicate that direct interaction of alkylresorcinols and modulation of enzymatic activities should be recognised as a significant part of the biological effect of these cereal bran components.