Studies On The Non-covalent Complexes Formed By Phosphorylated Flavone-Ca～(2+)-binding Protein Interaction

Cellular functions are often triggered by weak non-covalent enzyme-substrate, protein-ligand, protein-protein or antibody-antigen interactions. In organisms, proteins are vital substances, being very important during the course of movement and development of life. The mechanisms about proteins' structure and constitutes and the interaction with small molecules are topics interested by life scientists and chemists and clinic doctors. Recently, duing to the development of life scinence and medicine scinence, studies on the interaction between small molecules, especially medicative small ones and proteins have good meanings to the empolder of new drugs. Since its introduction, ESI-MS has served a powerful tool in providing evidence in support of the existence of non-covalently associated marcromolecular complexes in the gas phase.It is an established fact that esters of phosphoric acid have wide bio-activities and play a vital role in many biological processes.In the study described in this thesis, aminophenols and dihydroxybenzenes were first phosphorylated by modification of the classical Atheron-Todd procedure in our primary stage; Then the mechanism of the reaction between salicylic acid and dialkyl phosphite was studied by electrospray ionozation mass spectrometry and ³¹P NMR; 4-aminoantipine was further phosphorylated by modification of the classical Atheron-Todd procedure; finally, we have been able to enlarge the scope of the Atheron-Todd reaction to flavone.Electrospray ionization results showed that the phosphorylated flavonoids could form non-covalent complexes with many proteins such as lysozyme, myoglobin, bovine insulin and cytochrome c, while non-covalent complexes were not detected with the mixed solution of the chrysin and proteins. The phosphorylated flavonoids possess relatively stronger affinities and form non-covalent complexes with the proteins more easily than the unphosphorylated compounds.α-Lactalbumin is a protein deserved attention according to its composing of amino acids. The interaction between α-lactalbumin and dithyl flavon-7-yl phosphate...