Systematic Investigation On The Interactions Between Steroids,Ruthenium(Ⅱ),Rhodium(Ⅲ),Iridium(Ⅲ) Arene Complexes With Curcuminoid Ligands And Human Serum Albumin

Human serum albumin(HSA)has many physiological functions,such as special spatial structure,material transport and p H regulation.The molecular weight of HSA is small it is easy to be prepared and purified and it has high stability and good solubility.It is a model protein to study the interaction between proteins and different ligands.Steroids compounds,curuminoid compounds,ruthenium complexs,rhodium complexs,iridium complexs are the focus of current research.They not only have good antitumor activity,but also have excellent performance in toxicity,side effects and drug resistance.The study of the interaction mechanism between steroidal compounds and ruthenium(Ⅱ),rhodium(Ⅲ),and iridium(Ⅲ)arene complexes with curuminoid and HSA at the molecular level helps us to know its metabolism and the medicinal mechanism in the human body,it has important value for the study of the synthesis and biological activity of new drugs.It has important reference value for the synthesis and bioactivity of new drugs.This thesis consists of five chapters:The first chapter,the research progress of steroids,curuminoid,ruthenium(Ⅱ),rhodium(Ⅲ)and iridium(Ⅲ)arene complexes,the structure and function of human serum albumin,and the research methods of small molecular ligands and human serum albumin were introduced.The second chapter,in this chapter,through a variety of spectral methods,ultra-high performance liquid chromatography-mass spectra,and molecular modeling techniques,a comparative study of the interaction mechanism of the three steroid compounds and HSA was conducted at the molecular level.The results show that these three steroid compounds were the ground state complexes were formed by HSA.The quenching mechanism was a static quenching mechanism.The main forces were hydrogen bonding and van der Waals forces.The binding sites of compounds in HSA were Site Ⅰ,and the binding ratio was 1:1.Steroid compounds affect the microenvironment and conformation of HSA,and the influence of different structures of the three steroid compounds was also different,the effect of compound 3 is the largest.The third chapter,in this chapter,the interaction mechanism between two ruthenium(Ⅱ)arene 1,3,5-triaza-7-phosphaadamantane(PTA)type complexes with curuminoid and HSA was compare studied by various spectral methods,ultra-high performance liquid chromatography-mass spectra and electrochemical analysis.The experimental results showed that these two complexes formed a ground state complex with HSA.The quenching mechanism was static quenching mechanism,and the main interaction forces were hydrogen bonding and van der Waals force,the binding sites of these two complexes in HSA were Site Ⅰ,the binding ratio was 1:1,the complexes affect the microenvironment and conformation of HSA,and the structure of the two complexes was different.The size of the influence was also different,complex 1 produces more influence than complex 2.The fourth chapter,in this chapter,various spectral methods and electrochemical analysis were used to compare the interactions between three kinds of rhodium(Ⅲ)arene complexes with curuminoid and HSA.The experimental results show that these three complexes form a ground state complex with HSA.The quenching mechanism was static quenching mechanism.The main force was hydrogen bonding and van der Waals force.The binding sites were both Site Ⅰ of HSA,and some metal ions will have different degrees of combination of the complex and HSA.Inhibitory effects of these three complexes on the microenvironment and conformation of HSA were different,and the influence of the three complexes on the structure was different,and the effect of complex 3 was greater than that of the other two complexes.The fifth chapter,in this chapter,various spectral methods and electrochemical analysis were used to compare the interactions between three kinds of iridium(Ⅲ)arene complexes with curuminoid and HSA.The experimental results show that these three complexes form a ground state complex with HSA.The quenching mechanism was static quenching mechanism.The main force was hydrogen bonding and van der Waals force.The binding sites were both Site Ⅰ of HSA,and some metal ions will have different degrees of combination of the complex and HSA.Inhibitory effects of these three complexes on the microenvironment and conformation of HSA were different,and the influence of the three complexes on the structure was different,and the effect of complex 3 was greater than that of the other two complexes.