- About this Journal ·
- Abstracting and Indexing ·
- Aims and Scope ·
- Article Processing Charges ·
- Articles in Press ·
- Author Guidelines ·
- Bibliographic Information ·
- Citations to this Journal ·
- Contact Information ·
- Editorial Board ·
- Editorial Workflow ·
- Free eTOC Alerts ·
- Publication Ethics ·
- Reviewers Acknowledgment ·
- Submit a Manuscript ·
- Subscription Information ·
- Table of Contents
International Journal of Peptides
Volume 2011 (2011), Article ID 834525, 10 pages
In Vitro Selection of Cathepsin E-Activity-Enhancing Peptide Aptamers at Neutral pH
1Department of Functional Materials Science, Graduate School of Science and Engineering, Saitama University, 255 Shimo-Okubo, Saitama 338-8570, Japan
2City Area Program Saitama Metropolitan Area, Saitama Small and Medium Enterprises Development Corporation, 2-3-2 Kamiochiai, Chuo-Ku, Saitama 338-0001, Japan
3Rational Evolutionary Design of Advanced Biomolecules, Saitama (REDS) Group, Saitama Small Enterprise Promotion Corporation, no. 552 Saitama Industrial Technology Center, 3-12-18 Kami-Aoki, Kawaguchi, Saitama 333-0844, Japan
4Janusys Corporation, no. 508 Saitama Industrial Technology Center, 3-12-18 Kami-Aoki, Kawaguchi, Saitama 333-0844, Japan
5Proteolysis Research Laboratory, Graduate School of Pharmaceutical Sciences, Kyushu University, Higashi-Ku, Fukuoka 812-8582, Japan
Received 3 December 2010; Accepted 17 January 2011
Academic Editor: Brian Walker
Copyright © 2011 Madhu Biyani et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
- C. Southan, “A genomic perspective on human proteases as drug targets,” Drug Discovery Today, vol. 6, no. 13, pp. 681–688, 2001.
- B. Turk, “Targeting proteases: successes, failures and future prospects,” Nature Reviews Drug Discovery, vol. 5, no. 9, pp. 785–799, 2006.
- K. S. Putt, G. W. Chen, J. M. Pearson et al., “Small-molecule activation of procaspase-3 to caspase-3 as a personalized anticancer strategy,” Nature Chemical Biology, vol. 2, no. 10, pp. 543–550, 2006.
- J. A. Zorn and J. A. Wells, “Turning enzymes on with small molecules,” Nature Chemical Biology, vol. 6, no. 3, pp. 179–188, 2010.
- C. Ottmann, P. Hauske, and M. Kaiser, “Activation instead of inhibition: targeting proenzymes for small-molecule intervention,” ChemBioChem, vol. 11, no. 5, pp. 637–639, 2010.
- P. Hauske, C. Ottmann, M. Meltzer, M. Ehrmann, and M. Kaiser, “Allosteric regulation of proteases,” Chembiochem, vol. 9, no. 18, pp. 2920–2928, 2008.
- A. Wlodawer, M. Li, A. Gustchina et al., “Inhibitor complexes of the Pseudomonas serine-carboxyl proteinase,” Biochemistry, vol. 40, no. 51, pp. 15602–15611, 2001.
- I. Redzynia, A. Ljunggren, A. Bujacz, M. Abrahamson, M. Jaskolski, and G. Bujacz, “Crystal structure of the parasite inhibitor chagasin in complex with papain allows identification of structural requirements for broad reactivity and specificity determinants for target proteases,” FEBS Journal, vol. 276, no. 3, pp. 793–806, 2009.
- K. Kitamura, C. Yoshida, Y. Kinoshita et al., “Development of systemic in vitro evolution and its application to generation of peptide-aptamer-based inhibitors of cathepsin E,” Journal of Molecular Biology, vol. 387, no. 5, pp. 1186–1198, 2009.
- N. Nemoto, E. Miyamoto-Sato, Y. Husimi, and H. Yanagawa, “In vitro virus: bonding of mRNA bearing puromycin at the 3'-terminal end to the C-terminal end of its encoded protein on the ribosome in vitro,” FEBS Letters, vol. 414, no. 2, pp. 405–408, 1997.
- R. W. Roberts and J. W. Szostak, “RNA-peptide fusion for the in vitro selection of peptides and proteins,” Proceedings of the National Academy of Sciences of the United States of America, vol. 98, no. 9, pp. 4825–4826, 1997.
- J. Yamaguchi, M. Naimuddin, M. Biyani et al., “cDNA display: a novel screening method for functional disulfide-rich peptides by solid-phase synthesis and stabilization of mRNA-protein fusions,” Nucleic Acids Research, vol. 37, no. 16, article e108, 2009.
- M. Naimuddin, K. Kitamura, Y. Kinoshita et al., “Selection-by-function: efficient enrichment of cathepsin E inhibitors from a DNA library,” Journal of Molecular Recognition, vol. 20, no. 1, pp. 58–68, 2007.
- T. Kawakubo, K. Okamoto, J. I. Iwata et al., “Cathepsin E prevents tumor growth and metastasis by catalyzing the proteolytic release of soluble TRAIL from tumor cell surface,” Cancer Research, vol. 67, no. 22, pp. 10869–10878, 2007.
- R. S. DiPaola, J. Rinehart, J. Nemunaitis et al., “Characterization of a novel prostate-specific antigen-activated peptide-doxorubicin conjugate in patients with prostate cancer,” Journal of Clinical Oncology, vol. 20, no. 7, pp. 1874–1879, 2002.
- S. B. P. Athauda and K. Takahashi, “Distinct cleavage specificity of human cathepsin E at neutral pH with special preference for Arg-Arg bonds,” Protein and Peptide Letters, vol. 9, no. 1, pp. 15–22, 2002.
- D. Bromme and K. Okamoto, “Human cathepsin O2, a novel cysteine protease highly expressed in osteoclastomas and ovary molecular cloning, sequencing and tissue distribution,” Biological Chemistry Hoppe-Seyler, vol. 376, no. 6, pp. 379–384, 1995.
- K. Kitamura, C. Yoshida, MD. Salimullah et al., “Rapid in vitro synthesis of pico-mole quantities of peptides,” Chemistry Letters, vol. 37, no. 12, pp. 1250–1251, 2008.
- K. Kitamura, Y. Kinoshita, S. Narasaki, N. Nemoto, Y. Husimi, and K. Nishigaki, “Construction of block-shuffled libraries of DNA for evolutionary protein engineering: Y-ligation-based block shuffling,” Protein Engineering, vol. 15, no. 10, pp. 843–853, 2003.
- P. J. Alaimo, M. A. Shogren-Knaak, and K. M. Shokat, “Chemical genetic approaches for the elucidation of signaling pathways,” Current Opinion in Chemical Biology, vol. 5, no. 4, pp. 360–367, 2001.
- R. Huang, I. Martinez-Ferrando, and P. A. Cole, “Enhanced interrogation: emerging strategies for cell signaling inhibition,” Nature Structural and Molecular Biology, vol. 17, no. 6, pp. 646–649, 2010.
- D. R. Goode, R. K. Totten, J. T. Heeres, and P. J. Hergenrother, “Identification of promiscuous small molecule activators in high-throughput enzyme activation screens,” Journal of Medicinal Chemistry, vol. 51, no. 8, pp. 2346–2349, 2008.
- C. Chothia, J. Gough, C. Vogel, and S. A. Teichmann, “Evolution of the protein repertoire,” Science, vol. 300, no. 5626, pp. 1701–1703, 2003.
- C. Chothia and J. Gough, “Genomic and structural aspects of protein evolution,” Biochemical Journal, vol. 419, no. 1, pp. 15–28, 2009.
- C. A. Orengo and J. M. Thornton, “Protein families and their evolution—a structural perspective,” Annual Review of Biochemistry, vol. 74, pp. 867–900, 2005.