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. Science, 1990, 249, 884. 10.1126/science.2392678 CASPubMedWeb of Science®Google Scholar 2 Walker, G. J Adhesion 1981, 12, 51. 10.1080/00218468108071188 CASWeb of Science®Google Scholar 3 Young, G. A.; Crisp, D. J. Adhesion 1982, 6, 18. Web of Science®Google Scholar 4 Lindner, E. Marine Biodeterioration: An Interdisciplinary Study, Naval Institute Press, 1984; p 183. 10.1007/978-1-4615-9720-9_24 Google Scholar 5 Waite, J. H. J Biol Chem 1983, 258, 2911. 10.1016/S0021-9258(18)32805-9 CASPubMedWeb of Science®Google Scholar 6 Waite, J. H.; Tanzer, M. L. Science 1981, 212, 1038. 10.1126/science.212.4498.1038 CASPubMedWeb of Science®Google Scholar 7 Filpula, D. R.; Lee, S.; Link, R. P.; Strausberg, S. L.; Strausberg, R. L. Biotechnol Prog 1990, 6, 171. 10.1021/bp00003a001 CASPubMedWeb of Science®Google Scholar 8 Marumo, K. Nippon Seikeigeka Gakkai Zasshi Japan 1989, 63, 852. CASPubMedGoogle Scholar 9 Nagy, P. I.; Patel, H. C.; Dreyer, W.; Hopfinger, A. J. Int J Peptide Protein Res 1991, 38, 84. 10.1111/j.1399-3011.1991.tb01414.x CASPubMedWeb of Science®Google Scholar 10 Ikemura, T. J Mol Biol 1981, 146, 1. 10.1016/0022-2836(81)90363-6 CASPubMedWeb of Science®Google Scholar 11 Albertini, A. M.; Hofer, M.; Calos, M. P.; Miller, J. H. Cell 1982, 29, 319. 10.1016/0092-8674(82)90148-9 CASPubMedWeb of Science®Google Scholar 12 Sanger, F.; Nicklen, S.; Coulson, A. R. Proc Natl Acad Sci USA 1977, 74, 5463. 10.1073/pnas.74.12.5463 CASPubMedWeb of Science®Google Scholar 13 Kumagai, I.; Takeda, S.; Hibino, T.; Miura, K. Protein Eng 1990, 3, 449. 10.1093/protein/3.5.449 CASPubMedWeb of Science®Google Scholar 14 Gross, E.; Witkop, B. J Biol Chem 1962, 237, 1856. 10.1016/S0021-9258(19)73948-9 CASPubMedWeb of Science®Google Scholar 15 Kitamura, M.; et al. Biochim Biophys Acta 1997, 1351, 239. 10.1016/S0167-4781(96)00203-5 CASPubMedWeb of Science®Google Scholar 16 Laemmli, U. K. Nature 1970, 227, 680. 10.1038/227680a0 CASPubMedWeb of Science®Google Scholar 17 Imoto, M. Nippon Setchaku Kyoukaishi Osaka 1989, 25, 405. CASGoogle Scholar 18 Dupré, A. Théorie Méchanique de la Chaleur; Paris, 1869. Google Scholar 19 Greenfield, N.; Fasman, G. Biochemistry 1969, 8, 4108. 10.1021/bi00838a031 CASPubMedWeb of Science®Google Scholar 20 Greenfield, N. J. Anal Biochem 1996, 235, 1. 10.1006/abio.1996.0084 CASPubMedWeb of Science®Google Scholar 21 Wright, P. E.; Dyson, H. J.; Lerner, R. A. Biochemistry 1988, 27, 7167. 10.1021/bi00419a001 CASPubMedWeb of Science®Google Scholar 22 Graham, D. G.; Jeffs, P. W. J Biol Chem 1977, 252, 5729. 10.1016/S0021-9258(17)40083-4 CASPubMedWeb of Science®Google Scholar 23 Williams, T.; Marumo, K.; Waite, J. H.; Henkens, R. W. Arch Biochem Biophys 1989, 269, 415. 10.1016/0003-9861(89)90125-2 CASPubMedWeb of Science®Google Scholar 24 Yamamoto, H.; Nagai, A. Marine Chem 1992, 37, 131. 10.1016/0304-4203(92)90061-E CASWeb of Science®Google Scholar 25 Crips, D. J. Proc. 3rd Inter. Congress on Marine Corrosion and Fouling; Northwestern University Press: Evanston, 1973; p 691. Google Scholar 26 Olivieri, M. P.; Baier, R. E.; Loomis, R. E. Biomaterials 1992, 13, 1000. 10.1016/0142-9612(92)90150-M CASPubMedWeb of Science®Google Scholar 27 Yamamoto, H. J Adhesion Sci Tech 1987, 1, 177. 10.1163/156856187X00175 CASGoogle Scholar 28 Yamamoto, H. Nihonkagakukaishi Japan 1986, 90. Google Scholar 29 Papov, V. V.; Diamond, T. V.; Biemann, K.; Waite, J. H. J Biol Chem 1995, 270, 20183. 10.1074/jbc.270.34.20183 CASPubMedWeb of Science®Google Scholar 30 Inoue, K.; et al. Eur J Biochem 1996, 239, 172. 10.1111/j.1432-1033.1996.0172u.x CASPubMedWeb of Science®Google Scholar 31 Rawson, P. D.; Joyner, K. L.; Meetze, K.; Hilbish, T. J. Heredity 1996, 77, 599. 10.1038/hdy.1996.187 CASPubMedWeb of Science®Google Scholar 32 Inoue, K.; et al. J Mol Evol 1996, 43, 348. 10.1007/BF02339009 CASPubMedWeb of Science®Google Scholar 33 Inoue, K.; Takeuchi, Y.; Miki, D.; Odo, S. J Biol Chem 1995, 270, 6698. 10.1074/jbc.270.12.6698 CASPubMedWeb of Science®Google Scholar 34 Miki, D.; Takeuchi, Y.; Inoue, K.; Odo, S. Biol Bull 1996, 190, 213. 10.2307/1542541 CASPubMedWeb of Science®Google Scholar Citing Literature Volume37, Issue615 March 1999Pages 729-736 ReferencesRelatedInformation
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