Dendrimers are a new class of highly branched polymers. They have three dimension structure and possess many interesting properties. PAMAM dendrimers could be used as a chelators for metal ions.

Cadmium ions are very toxicity. They are responsible for inflammatory reactions in respiratory system, liver, kidneys, possess carcinogenic and mutagenic properties and could react with human biopolymers structures like proteins or DNA.

In our exploration we were investigated the interaction between G3.5 PAMAM dendrimers (5-100µM), cadmium ions (5-100µM) and dendrimer-cadmium complexes (each component of complex was used in 5-100µM concentration in molar ratio 1:1) with human serum albumin (5µM). The measured parameter was quenching of HSA fluorescence descended from tryptophan amino acid. Fluorescence quenching give information about conformational changes in structure of albumin. The effect of these compounds was determined on Perkin-Elmer LS-50B spectrofluorimeter in 37^oC. The results of this experiment shows that cadmium ions possess the most ability to quenching the HSA fluorescence among all used compounds. Half-generation PAMAM dendrimer G3.5 also evoked decrease of albumin fluorescence but degree of this changes is lower in comparison with cadmium ions. The least changes in HSA fluorescence were observed for G3.5-Cd complex. Even the highest concentration of this compound (100µM) didn’t change the fluorescence radically. In conclusion our investigation show that G3.5 PAMAM dendrimer could be use as a chelator for cadmium ions and protections factor for human serum albumin from destructive effects of cadmium ions.

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