DOI QR코드

DOI QR Code

Solution State Structure of pA1, the Mimotopic Peptide of Apolipoprotein A-I, by NMR Spectroscopy

  • Kim, Hyo-Joon (Department of Biochemistry and Molecular Biology, Hanyang University) ;
  • Won, Ho-Shik (Department of Applied Chemistry, Hanyang University)
  • 투고 : 2011.06.09
  • 심사 : 2011.07.31
  • 발행 : 2011.09.20

초록

Apolipoprotein A-I (Apo A-I) is a major component for high density lipoproteins (HDL). A number of mimetic peptides of Apo A-I were screened from the phase-displayed random peptide library by utilizing monoclonal antibodies (A12). Mimetic peptide for A12 epitope against Apo A-I was selected as CPFARLPVEHHDVVGL (pA1). From the BLAST search, the mimetic peptide pA1 had 40% homology with Apo A-I. As a result of the structural determination of this mimotope using homo/hetero nuclear 2D-NMR techniques and NMR-based distance geometry (DG)/molecular dynamic (MD) computations, DG structure had low penalty value of 0.3-0.7 ${\AA}^2$ and the total RMSD was 0.6-1.6 ${\AA}$. The mimotope pA1 exhibited characteristic conformation including a ${\beta}$-turn from Pro[7] to His[11].

키워드

참고문헌

  1. Cruzado, I. D.; Cockrill, S. L.; McNeal, C. J.; Macfarlane, R. D. J. Lipid Res. 1998, 39, 205.
  2. Mahley, R. W.; Innerarity, T. L.; Rall, S. C., Jr.; Wesgraber, K. H. J. Lipid Res. 1984, 25, 1277.
  3. Davis, R. A. Biochemistry of Lipids, Lipoproteins and Membranes; Elsevier Science Publishers: Canada, 1991.
  4. Browman, B. H. Hepatic Plasma Proteins Mechanisms of Function and Regulation; Academic Press, Inc.: London, 1993.
  5. Schumaker, V. N.; Phillips, M. L.; Chatterton, J. E. Adv. Protein Chem. 1994, 45, 205. https://doi.org/10.1016/S0065-3233(08)60641-5
  6. Chen, S. H.; Yang, C. Y.; Chen, P. F.; Setzer, D.; Tamimura, M.; Li, W. H.; Gotto, A. M.; Chan, L. J. Biol. Chem. 1986, 261, 12918.
  7. Segrest, J. P.; Jackson, R. L.; Morrisett, J. D.; Gotto, A. M. FEBS Lett. 1974, 38, 347.
  8. Kaiser, E. T.; Kezdy, F. J. Science 1984, 223, 249. https://doi.org/10.1126/science.6322295
  9. Knott, T. J.; Pease, R. J.; Powell, L. M.; Wallis, S. C.; Rall, S. C., Jr.; Innerarity, R. L.; Blackhart, B.; Taylor, W. H.; Marcel, Y.; Milne, Y.; Johnson, D.; Fuller, M.; Lusis, A. J.; McCarthy, B. J.; Mahley, R. W.; Levy-Wilson, B.; Scott, J. Nature 1986, 323, 734. https://doi.org/10.1038/323734a0
  10. Borhani, D. W.; Rogers, D. P.; Engler, J. A.; Brouillette, C. G. Proc. Natl. Acad. Sci. U. S. A. 1997, 94, 12291. https://doi.org/10.1073/pnas.94.23.12291
  11. Castelli, W. P.; Garrison, R. J.; Wilson, P. W. F.; Abbott, R. D.; Kalousdian, S.; Kannel, W. B. J. Am. Med. Assoc. 1986, 256, 2835. https://doi.org/10.1001/jama.256.20.2835
  12. Atkinson, D.; Davis, M. A. F.; Leslie, R. B. Proc. R. Soc. London 1974, 186, 165. https://doi.org/10.1098/rspb.1974.0044
  13. Segrest, J. P.; Jones, M. K.; De Loof, H.; Brouillette, C. G.; Venkatachalapathi, Y. V.; Anantharamaiah, G. M. J. Lipid Res. 1992, 33, 141.
  14. Johnson, B. A.; Blevins, R. A. J. Biomol. NMR 1994, 4, 603. https://doi.org/10.1007/BF00404272
  15. Wuthrich, K. NMR of Proteins and Nucleic Acids; Wiley: New York, 1986.
  16. Evans, J. N. S. Biomolecular NMR Spectroscopy, Oxford Univ. Press, 1995.
  17. South, T. L.; Blake, P. R.; Hare, D. R.; Summers, M. F. Biochemistry 1991, 30, 6342. https://doi.org/10.1021/bi00239a036
  18. Kim, D.; Rho, J.; Won, H. J. Korean Mag. Reson. Soc. 1999, 3, 44.