Interaction of human serum albumin with novel 3,9-disubstituted perylenes.

ABSTRACT: Human serum albumin (HSA) has been used as a model for the binding of a number of different ligands, including polyaromatic hydrocarbons, to proteins. In this case we have investigated the interaction of HSA with a novel set of perylene derivatives. Di-substituted perylene analogues have been synthesized as potentially useful organic photovoltaic materials. Their photophysical properties may make them viable for fuel cell applications too. However, these molecules are poorly soluble especially in aqueous solvents. Binding to water-soluble proteins may provide a way to solubilize them. At the same time one can study whether the photophysical processes initiated by the irradiation of a perylene ligand can cause conformational changes to the host protein. With the present study we demonstrate

SUBMITTER: Farooqi MJ 

PROVIDER: S-EPMC3871871 | biostudies-literature | 2013 Aug

REPOSITORIES: biostudies-literature