Formation of Artificial Serine Protease by Polymerization of Acrylated Amino Acids

• Main Authors: Chieh-Chih Chen, 陳玠志
• Other Authors: Dar-Fu Tai
• Format: Others
• Language: zh-TW
• Published: 2003
• Online Access: http://ndltd.ncl.edu.tw/handle/75485377207533098978

碩士 === 國立東華大學 === 化學系 === 91 === Abstract This thesis is to describe the production of polymers with catalytic activity toward hydrolysis by copolymerization of monomers containing amino acid residues. It has been known that serine, histidine and aspartate residues are involved in the active-site of serine protease, we synthesized N-acryl-L-serine-NHBn, N-acryl-L-aspartic acid-NHBn and N-acryl-L-histidine-NHBn from N-Boc protected amino acids by chemo- enzymatic synthesis. These synthetic functional monomers, crosslinker - ethylene glycol dimethacrylate and 2, 2’-azobisisobutyronitrile were mixed into a solution. After the polymerization was initiated photochemically, a serine protease-mimicking polymer was obtained. In addition, several transition state analogues were added as template during polymerization to form molecularly imprinted polymers ( MIPs ). Finally, we took the advantage of speedy ELISA readers to produce polymers on the wells of ELISA plates under different conditions, then measured and compared the catalytic activity of these polymers upon hydrolysis of esters and amides.