Enzymatic Synthesis of Poly(α-ethyl β-aspartate) by Poly(ethylene glycol) Modified Poly(aspartate) Hydrolase-1
作者： Tomohiro Hiraishi , Eriko Masuda , Daisuke Miyamoto , Naoki Kanayama , Hideki Abe
关键词: End-group 、 Polymerization 、 Polymer chemistry 、 Ethylene glycol 、 Hydrolase 、 Peptide bond 、 Chemistry 、 PEG ratio 、 Monomer 、 Substrate (chemistry) 、 Biotechnology 、 Materials Chemistry 、 Bioengineering 、 Polymers and Plastics 、 Biomaterials
摘要: We recently discovered that poly(aspartate) (PAA) hydrolase-1 from Pedobacter sp. KP-2 has a unique property of specifically cleaving the amide bond between β-aspartate units in thermally synthesized PAA (tPAA). In present study, enzymatic synthesis poly(α-ethyl β-aspartate) (β-PAA) was performed by taking advantage substrate specificity hydrolase-1. No polymerization diethyl L-aspartate native occurred because low dispersibility enzyme organic solvent. Poly(ethylene glycol) (PEG) modification improved its and enabled it to polymerize monomer substrate. MALDI-TOF MS analysis showed polymer observed range m/z = 750-2 500. This also revealed composed ethyl aspartate units, containing either an ester or free carboxyl end group at terminus. (1) H NMR demonstrated consisted only β-amide linkages. Thus, results indicate modified with PEG is useful for β-PAA due good
sci-hub.se 参考文章(19)
Hiroshi Uyama, Tokuma Fukuoka, Izuru Komatsu, Takashi Watanabe, Shiro Kobayashi, Protease-Catalyzed Regioselective Polymerization and Copolymerization of Glutamic Acid Diethyl Ester Biomacromolecules. ,vol. 3, pp. 318- 323 ,(2002) , 10.1021/BM010135C
Cristina Monfardini, Oddone Schiavon, Paolo Caliceti, Margherita Morpurgo, J. Milton Harris, Francesco M. Veronese, A BRANCHED MONOMETHOXYPOLY(ETHYLENE GLYCOL) FOR PROTEIN MODIFICATION Bioconjugate Chemistry. ,vol. 6, pp. 62- 69 ,(1995) , 10.1021/BC00031A006
Takashi UEMURA, Manami FUJIMORI, Ho-Hi LEE, Sakio IKEDA, Keiichi ASO, Polyethylene Glycol–Modified Papain Catalyzed Oligopeptide Synthesis from the Esters of l-Aspartic and l-Glutamic Acids in Benzene Agricultural and biological chemistry. ,vol. 54, pp. 2277- 2281 ,(1990) , 10.1271/BBB1961.54.2277
Tomohiro Hiraishi, Eriko Masuda, Naoki Kanayama, Madoka Nagata, Yoshiharu Doi, Hideki Abe, Mizuo Maeda, Cloning of Poly(aspartic acid) (PAA) Hydrolase‐1 Gene from Pedobacter sp. KP‐2 and Hydrolysis of Thermally Synthesized PAA by its Gene Product Macromolecular Bioscience. ,vol. 9, pp. 10- 19 ,(2009) , 10.1002/MABI.200800106
Shuichi Matsumura, Yasuhiro Tsushima, Nobuyuki Otozawa, Saeko Murakami, Kazunobu Toshima, Graham Swift, Enzyme-catalyzed polymerization of L-aspartate Macromolecular Rapid Communications. ,vol. 20, pp. 7- 11 ,(1999) , 10.1002/(SICI)1521-3927(19990101)20:1<7::AID-MARC7>3.0.CO;2-M
Yasuyuki Soeda, Kazunobu Toshima, Shuichi Matsumura, Sustainable enzymatic preparation of polyaspartate using a bacterial protease. Biomacromolecules. ,vol. 4, pp. 196- 203 ,(2003) , 10.1021/BM0200534
Hans R. Kricheldorf, Polypeptides and 100 years of chemistry of α-amino acid N-carboxyanhydrides Angewandte Chemie. ,vol. 45, pp. 5752- 5784 ,(2006) , 10.1002/ANIE.200600693
Frank Bordusa, Proteases in organic synthesis. Chemical Reviews. ,vol. 102, pp. 4817- 4867 ,(2002) , 10.1021/CR010164D
Tomohiro Hiraishi, Mariko Kajiyama, Kenji Tabata, Ichiro Yamato, Yoshiharu Doi, Genetic analysis and characterization of poly(aspartic acid) hydrolase-1 from Sphingomonas sp. KT-1. Biomacromolecules. ,vol. 4, pp. 80- 86 ,(2003) , 10.1021/BM025658E
Tomohiro Hiraishi, Mariko Kajiyama, Kenji Tabata, Hideki Abe, Ichiro Yamato, Yoshiharu Doi, Biochemical and Molecular Characterization of Poly(aspartic acid) Hydrolase-2 from Sphingomonas sp. KT-1 Biomacromolecules. ,vol. 4, pp. 1285- 1292 ,(2003) , 10.1021/BM034085I