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Volume 18 (2003)
- Issue 6 Pages 497-
- Issue 5 Pages 421-
- Issue 4 Pages 331-
- Issue 3 Pages 150-
- Issue 2 Pages 81-
- Issue 1 Pages 3-
Volume 18, Issue 6
Displaying 1-7 of 7 articles from this issue
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[in Japanese]2003 Volume 18 Issue 6 Pages 497
Published: November 10, 2003
Released on J-STAGE: December 26, 2008
JOURNAL FREE ACCESSDownload PDF (220K) -
[in Japanese]2003 Volume 18 Issue 6 Pages 499
Published: November 10, 2003
Released on J-STAGE: December 26, 2008
JOURNAL FREE ACCESSDownload PDF (196K) -
Expansion of the genetic code for the biosynthesis of useful alloproteinsKensaku Sakamoto, Shigeyuki Yokoyama2003 Volume 18 Issue 6 Pages 502-510
Published: November 10, 2003
Released on J-STAGE: December 26, 2008
JOURNAL FREE ACCESSThe biosynthesis of proteins containing unnatural amino acids, alloproteins, is a promising way of expanding the structural and chemical diversity in proteins. Thus, chemical probes, photo-crosslinkers, heavy atoms, and the unique groups for chemical conjugate have been incorporated into proteins. Unnatural amino acids can be attached to the adaptor tRNAs by the method of chemical aminoacylation, or by the use of the wild-type and engineered aminoacyl-tRNA synthetases. These tRNAs recognize the amber codon, four-base codons, the artificial codons with unnatural bases, and sense codons. The first three types of these codons can be used for the site-specific incorporation of unnatural amino acids into proteins. Such “site-specific alloproteins” have been synthesized in cell-free protein synthesis systems, Xenopus oocytes, the E. coil cells, yeasts, and cultured mammalian cells. The availability of the various aminoacylation methods, the various codons for unnatural amino acids, and the various translation systems adds to the usefulness of unnatural amino acids in proteins.View full abstractDownload PDF (2142K) -
Biopharmaceuticals based on in vitro protein evolutionKiyotaka Shiba2003 Volume 18 Issue 6 Pages 511-518
Published: November 10, 2003
Released on J-STAGE: December 26, 2008
JOURNAL FREE ACCESSIn this review, I overview “evolutionary molecular engineering” in these 10 years, and discuss how it will change in the age of “Genome and Proteome”. “Evolutionary molecular engineering” or “in vitro evolution” has emerged at beginning in the 1990's as a basic science asking origin of genes. From the stream, powerful new technologies, such as aptamer selection, peptide-phage selection, shuffling PCR etc. have been invented and, with these technologies, we are now able (i) to evolve existing proteins to desired direction in vitro, and (ii) to create functional peptides de novo. The stream, of course, affected and continues to affect the area of biopharmaceutical. The first artificial biopharmaceutical was a genetically modified insulin that has been approved in 1996. Since then, several artificial proteinous drugs have been approved including Enbrel, Ongak and Infergen. Most of these artificial proteins have been rationally engineered but not evolved in vitro. However, many novel “evolved” are under clinical trials and they should be approved in the near future. I have developed a novel type of protein evolution system, MolCraft. With MolCraft, we can synthesize novel proteins by remixing existing peptide motifs. I will introduce of potentials of MolCraft in biopharmaceuticals and bionanothnology.View full abstractDownload PDF (1810K) -
Comprehensive protein-protein interaction analysis (proteorne analysis) using “in vitro virus” and its application for drug target explorationHideaki Takashima, Hiroshi Yanagawa2003 Volume 18 Issue 6 Pages 519-527
Published: November 10, 2003
Released on J-STAGE: December 26, 2008
JOURNAL FREE ACCESSIn vitro virus(IVV) is an assignment molecule in which the genotype molecule (mRNA) binds to the phenotype molecule (protein). We have demonstrated that an IVV selection system is useful for the comprehensive analysis of protein-protein interactions (proteome analysis). We are studying to apply the IVV selection system to the analysis of drug-protein interactions to explore the drug target proteins or to understand the mode of action of drugs. In this review, we describe about the structure and the property of IVV. The application of the IVV selection system for proteome analysis and the analysis of drug-protein interactions is also explained.View full abstractDownload PDF (1914K) -
Strategies for development of medicine using antibodies as toots and of therapeutic antibodiesYoshikazu Kurosawa2003 Volume 18 Issue 6 Pages 528-535
Published: November 10, 2003
Released on J-STAGE: December 26, 2008
JOURNAL FREE ACCESSAntibodies can specifically bind to various antigens and form a large repertoire. If we well understand the characteristics of antibodies and utilize them as tools, we can obtain various informations which will be useful for development of medicine. Furthermore, since antibodies themselves are powerful self-defense molecules, we can directly develop human therapeutic antibodies against various diseases. In this review, I describe what should be considered and what kinds of problems should be solved to reach the above goals, based on the experiences of our “antibody project”.View full abstractDownload PDF (1964K) -
Creation of functional bioactive muteins using phage display technique results in a novel drug delivery systemYasuo Tsutsumi, Tadanori Mayumi2003 Volume 18 Issue 6 Pages 536-544
Published: November 10, 2003
Released on J-STAGE: December 26, 2008
JOURNAL FREE ACCESSWith the success of human genome projects, the focus of life science research has shifted to the functional and structural analyses of proteins, such as proteomics and structural genomics. These analyses of proteins including newly identified proteins are expected to contribute to the identification of therapeutically applicable proteins for various diseases. Thus, pharmaco-proteomic based drug discovery and development for protein therapies is most noticed currently. However, there is a clinical difficulty to use almost bioactive proteins, because of their very low stability and pleiotropic actions in vivo. To promote pharmaco-proteornic based drug discovery and development, we have attempted to establish a system for creating functional mutant proteins (muteins) with desired properties, and to develop a site-specific bioconjugation system for further improving their therapeutic potency. In this review, we are introducing these protein-drug innovation systems.View full abstractDownload PDF (2342K)
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