Expression of a model peptide of a marine mussel adhesive protein in Escherichia coli and characterization of its structural and functional properties

大肠杆菌 化学 贻贝 表征(材料科学) 生物化学 胶粘剂 微生物学 生物物理学 生物 材料科学 纳米技术 基因 生态学 有机化学 图层(电子)
作者
Masaya Kitamura,Kiminori Kawakami,Naotoshi Nakamura,Kouhei Tsumoto,Hidefumi Uchiyama,Yoshitaka Ueda,Izumi Kumagai,Tadao Nakaya
出处
期刊:Journal of Polymer Science Part A [Wiley]
卷期号:37 (6): 729-736 被引量:47
标识
DOI:10.1002/(sici)1099-0518(19990315)37:6<729::aid-pola8>3.0.co;2-3
摘要

Journal of Polymer Science Part A: Polymer ChemistryVolume 37, Issue 6 p. 729-736 Article Expression of a model peptide of a marine mussel adhesive protein in Escherichia coli and characterization of its structural and functional properties Masaya Kitamura, Masaya Kitamura Department of Bioapplied Chemistry, Faculty of Engineering, Osaka City University, Sumiyoshi-ku, Osaka 558-8585, JapanSearch for more papers by this authorKiminori Kawakami, Kiminori Kawakami Department of Bioapplied Chemistry, Faculty of Engineering, Osaka City University, Sumiyoshi-ku, Osaka 558-8585, JapanSearch for more papers by this authorNaotoshi Nakamura, Naotoshi Nakamura Department of Bioapplied Chemistry, Faculty of Engineering, Osaka City University, Sumiyoshi-ku, Osaka 558-8585, JapanSearch for more papers by this authorKouhei Tsumoto, Kouhei Tsumoto Department of Chemistry and Biotechnology, Faculty of Engineering, The University of Tokyo, Bunkyo-ku, Tokyo 113-8656, Japan Department of Biomolecular Engineering, Graduate School of Engineering, Tohoku University, Aoba-yama, Sendai 980-8579, JapanSearch for more papers by this authorHidefumi Uchiyama, Hidefumi Uchiyama Department of Chemistry and Biotechnology, Faculty of Engineering, The University of Tokyo, Bunkyo-ku, Tokyo 113-8656, Japan Department of Biological Science and Technology, Science University of Tokyo, Noda, Chiba 278-8510, JapanSearch for more papers by this authorYoshitaka Ueda, Yoshitaka Ueda Department of Chemistry and Biotechnology, Faculty of Engineering, The University of Tokyo, Bunkyo-ku, Tokyo 113-8656, Japan Institute for Drug Discovery Research, Yamanouchi Pharmaceutical Co., Ltd., Tsukuba, Ibaraki 305-8585, JapanSearch for more papers by this authorIzumi Kumagai, Izumi Kumagai Department of Chemistry and Biotechnology, Faculty of Engineering, The University of Tokyo, Bunkyo-ku, Tokyo 113-8656, Japan Department of Biomolecular Engineering, Graduate School of Engineering, Tohoku University, Aoba-yama, Sendai 980-8579, JapanSearch for more papers by this authorTadao Nakaya, Corresponding Author Tadao Nakaya [email protected] Department of Bioapplied Chemistry, Faculty of Engineering, Osaka City University, Sumiyoshi-ku, Osaka 558-8585, JapanDepartment of Bioapplied Chemistry, Faculty of Engineering, Osaka City University, Sumiyoshi-ku, Osaka 558-8585, JapanSearch for more papers by this author Masaya Kitamura, Masaya Kitamura Department of Bioapplied Chemistry, Faculty of Engineering, Osaka City University, Sumiyoshi-ku, Osaka 558-8585, JapanSearch for more papers by this authorKiminori Kawakami, Kiminori Kawakami Department of Bioapplied Chemistry, Faculty of Engineering, Osaka City University, Sumiyoshi-ku, Osaka 558-8585, JapanSearch for more papers by this authorNaotoshi Nakamura, Naotoshi Nakamura Department of Bioapplied Chemistry, Faculty of Engineering, Osaka City University, Sumiyoshi-ku, Osaka 558-8585, JapanSearch for more papers by this authorKouhei Tsumoto, Kouhei Tsumoto Department of Chemistry and Biotechnology, Faculty of Engineering, The University of Tokyo, Bunkyo-ku, Tokyo 113-8656, Japan Department of Biomolecular Engineering, Graduate School of Engineering, Tohoku University, Aoba-yama, Sendai 980-8579, JapanSearch for more papers by this authorHidefumi Uchiyama, Hidefumi Uchiyama Department of Chemistry and Biotechnology, Faculty of Engineering, The University of Tokyo, Bunkyo-ku, Tokyo 113-8656, Japan Department of Biological Science and Technology, Science University of Tokyo, Noda, Chiba 278-8510, JapanSearch for more papers by this authorYoshitaka Ueda, Yoshitaka Ueda Department of Chemistry and Biotechnology, Faculty of Engineering, The University of Tokyo, Bunkyo-ku, Tokyo 113-8656, Japan Institute for Drug Discovery Research, Yamanouchi Pharmaceutical Co., Ltd., Tsukuba, Ibaraki 305-8585, JapanSearch for more papers by this authorIzumi Kumagai, Izumi Kumagai Department of Chemistry and Biotechnology, Faculty of Engineering, The University of Tokyo, Bunkyo-ku, Tokyo 113-8656, Japan Department of Biomolecular Engineering, Graduate School of Engineering, Tohoku University, Aoba-yama, Sendai 980-8579, JapanSearch for more papers by this authorTadao Nakaya, Corresponding Author Tadao Nakaya [email protected] Department of Bioapplied Chemistry, Faculty of Engineering, Osaka City University, Sumiyoshi-ku, Osaka 558-8585, JapanDepartment of Bioapplied Chemistry, Faculty of Engineering, Osaka City University, Sumiyoshi-ku, Osaka 558-8585, JapanSearch for more papers by this author First published: 21 January 2000 https://doi.org/10.1002/(SICI)1099-0518(19990315)37:6<729::AID-POLA8>3.0.CO;2-3Citations: 41AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onEmailFacebookTwitterLinkedInRedditWechat Abstract An expression system for a chemically synthesized gene, encoding a model peptide of marine mussel adhesive protein, was constructed in Escherichia coli under regulation of the T7-promoter. The model peptide consisted of six repeats of the decapeptide AKPSYPPTYK. Although the product was expressed as an inclusion body, we were able to solubilize it successfully, using acetic acid. The higher-order structure of this model peptide was investigated using CD spectroscopy and NMR spectroscopy. Using the modified enzyme, mushroom tyrosinase, the tyrosine residue was hydroxylated to 3,4-dihydoxyphenylalanine (Dopa), and the resulting modified peptide was polymerized, solidified, and insolubilized spontaneously. © 1999 John Wiley & Sons, Inc. J Polym Sci A: Polym Chem 37: 729–736, 1999 REFERENCES AND NOTES 1 Hecht, M. H.; Richardson, J. S.; Richardson, D. C.; Ogden, R. C. 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