Interaction Mechanism Investigation Between Ruthenium Arene Complexs With Antitumor Activity And Human Serum Albumin

Cisplatin and carboplatin are the most classical chemotherapy drugs in clinic.However,these drugs are of low bioavailability,high toxicity and can only be injected.It has been shown that ruthenium complexes have many advantages.They are easy to be absorbed,to metabolize,to be functionalized and can treat a broad spectrum of cancers.Curcumin derivatives and thiosemicarbazones are two kinds of ligand that can be used to adjust the complexes for better bioactivities and pharmacological activities.They also hold up fairly well in anticancer activity.In this paper,we study the interaction between a class of ruthenium complexs containing thiosemicarbazones and curcumin derivatives and biological macromolecules,which has significant guidance in designing and developing novel ruthenium anticancer drugs.The spectroscopic techniques and Mass spectra were used to systematically investigatethe interaction between ruthenium complexes of curcumin analogs and thiosemicarbazones and human serum albumin(HSA).The steady-state fluorescence spectral results showed that seven complexes quenched the intrinsic fluorescence of HSA through static quenching mode.Hydrogen bond interactions and the van der Waals interactions are of the most importance of the formation and stabilization of the ground complex.The structure variation and the changes of micro-environments of HSA are apparent while the seven complexs are added.The variation of the substituent group on the thiophene ring of curcumin analogs and benzene ring of thiosemicarbazones,the number of Ru groups which resulted in the space steric hindrance were the possible reason why the the differences in the interactions between different Ru complexes and HSA exist.Our results shed light upon the interaction between ruthenium complexes of curcumin analogs and thiosemicarbazones and HSA which will do good to the develop of ruthenium derivatives in therapeutic fields.