Bulletin of the Korean Chemical Society

Korean Chemical Society (대한화학회)
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Solution Structure of pA2, the Mimotopic Peptide of Apolipoprotein A-I, by NMR Spectroscopy

  • Won, Ho-Shik (Department of Applied Chemistry, Hanyang University)
  • Received : 2011.07.31
  • Accepted : 2011.09.20
  • Published : 2011.11.20
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Abstract

A number of mimetic peptides of apolipoprotein A-I, a major component for high density lipoproteins (HDL), were screened from the phase-displayed random peptide library by utilizing monoclonal antibodies (A12). A mimetic peptide for A12 epitope against apolipoprotein A-I was selected as FVLVRDTFPSSVCCP(pA2) exhibiting 45% homology with Apo A-I in the BLAST search. Solution structure determination of this mimotope was made by using 2D-NMR data and NMR-based distance geometry (DG)/molecular dynamic calculations. The resulting DG structures had low penalty value of 0.4-0.6 ${\AA}^2$ and the total RMSD of 0.7-1.7 ${\AA}$. The mimotope pA2 exhibited a characteristic ${\beta}$-turn conformation from Val[2] to Phe[8] near Pro[9] residue.

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References

  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. Segrest, J. P.; Jackson, R. L.; Morrisett, J. D.; Gotto, A. M. FEBS Lett. 1974, 38, 347.
  5. Kaiser, E. T.; Kezdy, F. J. Science 1984, 223, 249. https://doi.org/10.1126/science.6322295
  6. 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
  7. 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
  8. 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.1986.03380200073024
  9. Atkinson, D.; Davis, M. A. F.; Leslie, R. B. Proc. R. Soc. London 1974, 186, 165. https://doi.org/10.1098/rspb.1974.0044
  10. Segrest, J. P.; Jones, M. K.; De Loof, H.; Brouillette, C. G.; Venkatachalapathi, Y. V.; Anantharamaiah, G. M. J. Lipid Res. 1992, 33, 141.
  11. Johnson, B. A.; Blevins, R. A. J. Biomol. NMR 1994, 4, 603. https://doi.org/10.1007/BF00404272
  12. Wuthrich, K. NMR of Proteins and Nucleic Acids; Wiley: New York, 1986.
  13. Evans, J. N. S. Biomolecular NMR Spectroscopy; Oxford Univ. Press: 1995.
  14. South, T. L.; Blake, P. R.; Hare, D. R.; Summers, M. F. Biochemistry 1991, 30, 6342. https://doi.org/10.1021/bi00239a036
  15. Kim, D.; Rho, J.; Won, H. J. Korean. Mag. Reson. Soc. 1999, 3, 44.
  16. Kim, H.; Won, H. Bull. Korean Chem. Soc. 2011, 9, 3425.