Hydrolysis Reaction of N-Phosphoryl-α-, β- and γ-amino Acids Studied by HPLC

✍ Scribed by Li-Ming QIANG; Shu-Xia CAO; Xiao-Yang ZHAO; Ruo-Yu LIU; Ji-Hong LIU; Jian-Sha LU; Yu-Fen ZHAO

• Publisher: John Wiley and Sons
• Year: 2007
• Tongue: English
• Weight: 85 KB
• Volume: 25
• Category: Article
• ISSN: 0256-7660
• DOI: 10.1002/cjoc.200790287

✦ Synopsis

Abstract

The hydrolysis reactions of N‐(O,O′‐diisopropyl)phosphoryl‐L‐α‐alanine (DIPP‐L‐α‐Ala), N‐(O,O′‐diisopropyl)‐ phosphoryl‐D‐α‐alanine (DIPP‐D‐α‐Ala), N‐(O,O′‐diisopropyl)phosphoryl‐β‐alanine (DIPP‐β‐Ala) and N‐(O,O′‐ diisopropyl)phosphoryl‐γ‐amino butyric acid (DIPP‐γ‐Aba), were studied by HPLC and their hydrolysis reaction kinetic equations were obtained. Under acid conditions, the reaction rate of DIPP‐L‐α‐Ala was close to that of DIPP‐D‐α‐Ala and the same rule was true between DIPP‐β‐Ala and DIPP‐γ‐Aba. Meantime, the reaction rate of DIPP‐L/D‐α‐Ala was as 10 times as that of DIPP‐β‐Ala or DIPP‐γ‐Aba. Under basic conditions, the hydrolysis reactions of DIPP‐β‐Ala and DIPP‐γ‐Aba almost did not take place and the reaction rate of DIPP‐L/D‐α‐Ala was about 1/10 of that under acid conditions. Moreover, theoretical calculation further illuminated the differences of the hydrolysis rate from the view of energy. The results would provide some helpful clues to why nature chose α‐amino acids but not other kinds of analogs as protein backbones.