Application Of ESI-MS In The Reaction Of Amino Acids And THF With Phosphoryl Chloride

In nature, there are various species of proteins and active polypeptides possessing different biological functions. All kinds of proteins and polypeptides are built by amino acids residues through peptide bond. The synthesis of polypeptide started by Fisher from the beginning of 20th century and had reached its peak at fifties as many classical methods developed. For decades, a number of physiological active polypeptides were discovered in pituitary, hypothalamic, enteron, all kinds of glands and neural and circulation system. However, these natural proteins were only present in low quantity in nature. Therefore, developing new methods for peptides synthesis is very important.There are two general methods for the formation of peptide bond, i.e. amino activation or carboxylic group activation. So far, the latter one was used more often. Among them, the mixed anhydride, activated ester and DCC coupling reagent were the most familiar methods. At presence, liquid phase synthesis, solid phase synthesis and enzymatic synthesis are used to synthesize peptides.Organophosphorus compounds have been used as coupling regents to synthesize bioactive peptides and some of them were excellent. In our previous work, it was discovered that polypeptides were formed by self-assembly of N,O-bis(trimethylsilyl) amino acids with the assistance of O,O-phenylene phosphoryl chloride.Up to now, a lot of methods have been developed for the cleavage of the C-O bond of ethers. Among them, acylation cleavage of ethers is an attractive one, since it affords useful esters and can be catalyzed by Lewis acids such as TiCl4 and ZnCl2 as well as low-valent metal complexes such as Mo(CO)6. During the course of the investigation, it was found that POCl3 not only...