Interaction of polyamidoamine (PAMAM) succinamic acid dendrimers generation 4 with human serum albumin

Dendrimers, a relatively new group of highly branched three dimensional polymers, are intensively investigated to use them in biomedical and physicochemical sciences. Their specific architecture gives them the ability to interact with many different types of molecules. In our studies the interaction between PAMAM succinamic acid dendrimers generation 4 (PAMAM-SAH G4) and human serum albumin (HSA) was examined. Experiments showed that a single molecule of a HSA can bind approximately 6 particles of dendrimers. The fluorescence studies demonstrated that dendrimers lead to a decrease in protein fluorescence but changes in fluorescence anisotropy were not observed. Alterations in the spectrum of circular dichroism indicated changes in the secondary protein structure. The results clearly show that this generation of dendrimers possesses a strong ability to interact with human serum albumin.

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► PAMAM-SAH G4 dendrimers strongly interact with human serum albumin.
► PAMAM-SAH G4 dendrimers lead to denaturation of HSA structure.
► Single molecule of a HSA can bind approximately 6 particles of dendrimers.
► Interactions between PAMAM-SAH G4 dendrimers and HSA should be taken into consideration in the future studies concerning the use of these types of dendrimer molecules in medicine.