Synthesis Of Electron-rich Amino Acid Molecules And Study On Their Self-assembly Behaviors And Recognition

Amino acids are the basic construction unit of protein.It is very important to study the self-assembly behaviors of amino acid molecules in order to understand the stereoscopic structure and properties of protein.A series of electron-rich amino acid molecular containing amide functional groups were designed and synthesized.The effects of solvent on the self-assembly behaviors of electron-rich amino acid molecular were observed by SEM.The effects of electron-rich amino acids side groups on the self-assembly behaviors of amino acid molecular were investigated.The recognition of electron-rich amino acid molecular were carried out by fluorescence spectroscopy.The main contents are as follows:（1）Synthesize and characterize of electron-rich amino acid molecules.The electron-rich amino acid molecules have been synthesized based on terephthaloyl chloride,trimesoyl chloride and L-type amino acid methyl ester hydrochloride as raw materials,which have been characterized by infrared spectroscopy,nuclear magnetic resonance spectrum and mass spectrum.The effects of various reaction conditions on the yield were investigated.（2）Modulation of self-assembly behaviors of electron-rich amino acid molecules.（a）The behaviors of electron-rich amino acid molecules was studied by SEM in the presence of five kinds of solvent ratio（CH₃OH:H₂O,10:0,8:2,6:4,5:5,4:6）.The results showed that the assembly morphologies are different from each other for the different residues of electron-rich amino acids（b）The changes of spectral properties of electron-rich amino acid molecules in different solvent ratios were observed by UV and CD spectroscopy.（3）The recognition of electron-rich amino acid molecules.（a）A new novel of biological molecular sensoren material tetraphenyletthene-pyridinium salt(Tpp⁴⁺)was synthesized,which has been characterized by infrared spectroscopy,nuclear magnetic resonance spectrum and mass spectrum.The interaction between L-Phenylalanine,L-Tryptophan,L-Isoleucine,L-Histidine and Tpp⁴⁺molecular were investigated by fluorescence spectroscopy.In order to determine the mechanism of interaction between L-tryptophan and Tpp⁴⁺molecule,the Stern-Volmer curves at different temperatures were measured by temperature variation experiments.