In this thesis, bimetallic complex [ Pd 2 {(C,N)-C 6 H 4 CH (CH 3 )NH} 2 (?-OAc)] 2 Has been synthesized and characterized from the combination of palladium acetate and ?-methyl benzylamine ligand by reflux in toluene as solvent. This complex was used as a basis for further reactions and then two target complexes were prepared and characterized structurally. 1) [Pd 2 {(C,N)-C 6 H 4 CH (CH 3 )NH 2 } 2 (µ-OAc)] 2 ] 2) [Pd 2 {(C,N)-C 6 H 4 CH (CH 3 )NH 2 } 2 (µ-N 3 )] 2 ] 3) [Pd{(C,N)-C 6 H 4 CH (CH 3 )NH 2 }(CUR)] 4) [Pd 2 {(C,N)-C 6 H 4 CH (CH 3 )NH 2 } 2 (µ-N 3 CS 2 )] Complex 3 has been prepared by the reaction of the preliminary complex with curcumin ligand [1,7 bis-(4-hydroxyl-3-methoxyphenyl)1,6-hepta diene-3,5-di one] which is the effective material of turmeric and complex (4), was prepared by replacing the previous dimer bridge with sodium azide (NaN 3 ) in complex (2) and then with CS 2 . Both complexes were characterized using FT-IR and NMR spectrums and elemental analysis. In the second part of the project, biological activity of the complexes was evaluated by examining their ability to bind to DNA(CT-DNA) using uv-Vis and thermal denaturation, and according to the experiments performed, intercalation interaction was suggested. In this section, the interaction between two complexes (3) and (4) with BSA was studied. As a result of absorption uv-spectrums of protein in the presence and absence of different concentrations of complexes (3) and (4) , it was observed that reduction and shifting to higher wavelengths indicates the interaction of the complexes with BSA and the alterations in the intensity of the absorption band of BSA revealed that the interactions between BSA and complexes (3) and (4) causes changes in BSA microenvironments around the amino-acids. While investigating the interaction between complexes (3) and (4) with protein using fluorescent spectroscopy, the value of quenching rate constant (Kq), suggested statistical mechanism and the value of quenching constant of stern-velmer (Ksv) for both complexes, indicated the proper binding of BSA with complexes (3) and (4). But complex (3) is more strongly bound to BSA than complex (4). Competitive studies of sitemarkers of ibuprofen and warfarine were also performed to identify the binding site of the complex to BSA, and as a result of the experiments, complex (3) and complex (4) have been placed in binding sites II and I respectively. And in the last section of the thesis, the anti-tumor effects on the cell-domains of three types of cancer cells, including JURKAT, MCF7 and PBMC. was carried out and reported.