Bulletin of the Korean Chemical Society

Korean Chemical Society (대한화학회)
권호 표지
DOI QR코드

DOI QR Code

Cell Selectivity of Arenicin-1 and Its Derivative with Two Disulfide Bonds

  • Lee, Ju-Un (Department of Bioscience and Biotechnology, and Bio/Molecular Informatics Center, Konkuk University) ;
  • Park, Ka-Hyon (Department of Bio-Materials, Graduate School and Research Center for Proteineous Materials, Chosun University) ;
  • Lee, Jee-Young (Department of Bioscience and Biotechnology, and Bio/Molecular Informatics Center, Konkuk University) ;
  • Kim, Jin-Kyoung (Department of Bioscience and Biotechnology, and Bio/Molecular Informatics Center, Konkuk University) ;
  • Shin, Song-Yub (Department of Bio-Materials, Graduate School and Research Center for Proteineous Materials, Chosun University) ;
  • Park, Yoon-Kyung (Department of Bio-Materials, Graduate School and Research Center for Proteineous Materials, Chosun University) ;
  • Hahm, Kyung-Soo (Department of Bio-Materials, Graduate School and Research Center for Proteineous Materials, Chosun University) ;
  • Kim, Yang-Mee (Department of Bioscience and Biotechnology, and Bio/Molecular Informatics Center, Konkuk University)
  • Published : 2008.06.20
Download PDF
⟨ Previous Next ⟩

Abstract

Keywords

References

  1. Lee, K. H.; Lee, D. G.; Park, Y.; Kang, D. I.; Shin, S. Y.; Hahm, K. S.; Kim, Y. Biochem. J. 2006, 394, 105 https://doi.org/10.1042/BJ20051574
  2. Anthony, C.; Yanmin, H.; Richard, B.; Clive, P. Nature Reviews 2002, 1, 895 https://doi.org/10.1038/nrd940
  3. Michael, Z. Nature 2002, 415, 389 https://doi.org/10.1038/415389a
  4. Zasloff, M. Curr. Opin. Immunol. 1992, 4, 3 https://doi.org/10.1016/0952-7915(92)90115-U
  5. Yount, N. Y.; Bayer, A. S.; Xiong, Y. Q.; Yeaman, M. R. Biopolymers (Peptide Science) 2006, 84, 435 https://doi.org/10.1002/bip.20543
  6. Hancock, R. E. W.; Diamond, G. Trends in Microbiology 1999, 8, 402
  7. Boman, H. G. J. Intern. Med. 2003, 254, 197 https://doi.org/10.1046/j.1365-2796.2003.01228.x
  8. Ovchinnikova, T. V.; Aleshina, G. M.; Balandin, S. V.; Krasnosdembskaya, A. D.; Markelov, M. L.; Frolova, E. I.; Leonova, Y. F.; Tagaev, A. A.; Krasnodembsky, E. G.; Kokryakov, V. N. FEBS Lett. 2004, 577, 209 https://doi.org/10.1016/j.febslet.2004.10.012
  9. Lee, J. U.; Kang, D. I.; Zhu, W. L.; Shin, S. Y.; Hahm, K. S.; Kim, Y. Biopolymers (Peptide Science) 2007, 88, 208 https://doi.org/10.1002/bip.20700
  10. Fields, G. B.; Noble, R. L. Int. J. Pept. Protein Res. 1990, 35, 161 https://doi.org/10.1111/j.1399-3011.1990.tb00939.x
  11. Vila-Perello, M.; Sanchez-Vallet, A.; Garcia-Olmedo, F.; Molina, A.; Andreu, D. FEBS Lett. 2003, 536, 215 https://doi.org/10.1016/S0014-5793(03)00053-X
  12. Kang, D. I.; Back, D.; Shin, S. Y.; Kim, Y. Bull. Korean Chem. Soc. 2005, 26, 1225 https://doi.org/10.5012/bkcs.2005.26.8.1225
  13. Lee, J. Y.; Baek, S.; Kim, Y. Bull. Korean Chem. Soc. 2007, 28, 379 https://doi.org/10.5012/bkcs.2007.28.3.379
  14. Lee, J. Y.; Lee, S. A.; Kim, Y. Bull. Korean Chem. Soc. 2007, 28, 941 https://doi.org/10.5012/bkcs.2007.28.6.941
  15. Shin, S. Y.; Kang, J. H.; Jang, S. Y.; Kim, Y.; Kim, K. L.; Hahm, K. S. Biochem Biophy Acta 2000, 1463, 209 https://doi.org/10.1016/S0005-2736(99)00210-2
  16. Zhu, W. L.; Lan, H.; Park, Y.; Yang, S. T.; Kim, J. I.; Park, I. S.; You, H. J.; Lee, J. S.; Park, Y. S.; Kim, Y.; Hahm, K. S.; Shin, S. Y. Biochemistry 2006, 45, 13007 https://doi.org/10.1021/bi060487+
  17. Zhu, W. L.; Nan, Y. H.; Hahm, K. S.; Shin, S. Y. Journal of Biochemistry and Molecular Biology 2007, 40, 1090 https://doi.org/10.5483/BMBRep.2007.40.6.1090
  18. Ahn, H. S.; Cho, W.; Kang, S. H.; Ko, S. S.; Park, M. S.; Cho, H.; Lee, K. H. PEPTIDES 2006, 27, 640 https://doi.org/10.1016/j.peptides.2005.08.016
  19. Lee, S. H. Bull. Korean Chem. Soc. 2006, 27, 1154 https://doi.org/10.5012/bkcs.2006.27.8.1154
  20. Bulet, P.; Stocklin, R.; Menin, L. Immunol. Rev. 2004, 198, 169 https://doi.org/10.1111/j.0105-2896.2004.0124.x
  21. Laederach, A.; Andreotti, A. H.; Fulton, D. B. Biochemistry 2002, 41, 12359 https://doi.org/10.1021/bi026185z
  22. Powers, J. S.; Rozek, A.; Hancock, R. E. Biochem. Biophys. Acta 2004, 1698, 239 https://doi.org/10.1016/j.bbapap.2003.12.009

Cited by

  1. Formation of arenicin-1 microdomains in bilayers and their specific lipid interaction revealed by Z-scan FCS vol.399, pp.10, 2011, https://doi.org/10.1007/s00216-011-4694-z
  2. Influence of Arenicin on Phase Transitions and Ordering of Lipids in 2D Model Membranes vol.29, pp.39, 2013, https://doi.org/10.1021/la402340d
  3. Multifaceted Roles of Disulfide Bonds. Peptides as Therapeutics vol.114, pp.2, 2014, https://doi.org/10.1021/cr400031z
  4. Ion Mobility-Mass Spectrometry as a Tool for the Structural Characterization of Peptides Bearing Intramolecular Disulfide Bond(s) vol.27, pp.10, 2016, https://doi.org/10.1007/s13361-016-1443-8
  5. Antibacterials from the Sea vol.16, pp.42, 2008, https://doi.org/10.1002/chem.201001279
  6. Redesigning Arenicin-1, an Antimicrobial Peptide from the Marine Polychaeta Arenicola marina, by Strand Rearrangement or Branching, Substitution of Specific Residues, and Backbone Linearization or Cyc vol.17, pp.6, 2008, https://doi.org/10.3390/md17060376
  7. Worms’ Antimicrobial Peptides vol.17, pp.9, 2019, https://doi.org/10.3390/md17090512
  8. Effects of C-Terminal Residues of 12-Mer Peptides on Antibacterial Efficacy and Mechanism vol.29, pp.11, 2008, https://doi.org/10.4014/jmb.1907.07061
  9. Venom peptides - A comprehensive translational perspective in pain management vol.2, pp.None, 2021, https://doi.org/10.1016/j.crtox.2021.09.001