한국자기공명학회논문지 (Journal of the Korean Magnetic Resonance Society)

한국자기공명학회 (Korean Magnetic Resonance Society)
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The Structural Studies of Peptide P143 Derived from Apo B-100 by NMR

  • Lee, Ji-Eun (Department of Chemistry and Molecular Engineering, Hanyang University) ;
  • Kim, Gil-Hoon (Department of Chemistry and Molecular Engineering, Hanyang University) ;
  • Won, Ho-Shik (Department of Chemistry and Molecular Engineering, Hanyang University)
  • 투고 : 2021.12.13
  • 심사 : 2021.12.20
  • 발행 : 2021.12.20
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초록

Apolipoprotein B-100 (apo B-100), the main protein component that makes up LDL (Low density lipoprotein), consists of 4,536 amino acids and serves to combine with the LDL receptor. The oxidized LDL peptides by malondialdehyde (MDA) or acetylation in vivo act as immunoglobulin (Ig) antigens and peptide groups were classified into 7 peptide groups with subsequent 20 amino acids (P1-P302). The biomimetic peptide P143 (IALDD AKINF NEKLS QLQTY) out of C-group peptides carrying the highest value of IgG antigens were selected for structural studies that may provide antigen specificity. Experimental results show that P143 has β-sheet in Ile[1]-Asn[9] and α-helice in Gln[16]-Tyr[20] structure. Homonuclear 2D-NMR (COSY, TOCSY, NOESY) experiments were carried out for NMR signal assignments and structure determination for P143. On the basis of these completely assigned NMR spectra and proton distance information, distance geometry (DG) and molecular dynamic (MD) were carried out to determine the structures of P143. The proposed structure was selected by comparisons between experimental NOE spectra and back-calculated 2D NOE results from determined structure showing acceptable agreement. The total Root-Mean-Square-Deviation (RMSD) value of P143 obtained upon superposition of all atoms were in the set range. The solution state P143 has a mixed structure of pseudo α-helix and β-turn(Phe[10] to Glu[12]). These results are well consistent with calculated structure from experimental data of NOE spectra. Structural studies based on NMR may contribute to the prevent oxidation studies of atherosclerosis and observed conformational characteristics of apo B-100 in LDL using monoclonal antibodies.

키워드

과제정보

This work was supported by the research fund of Hanyang University (HY-2021-G).

참고문헌

  1. R. W. Mahley, T. L. Innerarity, S. C. Jr. Rall, and K. H. Wesgraber, J. Lipid Res. 25, 1277 (1984) https://doi.org/10.1016/S0022-2275(20)34443-6
  2. R. A. Davis, Biochem. Lipid (1991)
  3. B. H. Browman, Hepatic Plasma Proteins Mechanisms of Function and Regulations, Academic Press, Inc., London (1993)
  4. V. N. Schumaker, M. L. Phillips, and J. E. Chatterton, Adv. Protein 45, 205 (1994) https://doi.org/10.1016/S0065-3233(08)60641-5
  5. S. H. Chen, C. Y. Yang, P. F. Chen, D. Setzer, M. Tamimura, W. H. Li, A. M. Gotto, and L. J. Chan, Biol. Chem. 261, 12918 (1986) https://doi.org/10.1016/S0021-9258(18)69248-8
  6. T. J.Knott, R. J.Pease, L. M.Powell, S. C.Wallis, S. C.Rall Jr, T. L. Innerarity, B. Blackhart, W. H. Taylor, Y. Marcel, R. Milne, D. Johnson, M. Fuller, A. J. Lusis, B. J. McCarthy, R. W. Mahley, B. L. Wilson, J. Scott, Nature 323, 734 (1986) https://doi.org/10.1038/323734a0
  7. M. L. Phillips, and V. N. Schumaker, J. Lipid Res. 30, 415 (1989) https://doi.org/10.1016/S0022-2275(20)38356-5
  8. A. D. Cardin, and R. L. Jackson, Biochem. Biophys. Acta. 877, 366 (1986) https://doi.org/10.1016/0005-2760(86)90201-8
  9. G. C. Chen, S. Zhu, D. A. Hardman, J. W. Schilling, K. Lau, and J. P. Kane, J. Biol. Chem. 264, 14369 (1989) https://doi.org/10.1016/S0021-9258(18)71687-6
  10. R. A. Davis, R. N. Thrift, C. C. Wu, and K. E. Howell, J. Biol. Chem. 265, 10005 (1990) https://doi.org/10.1016/S0021-9258(19)38770-8
  11. C. Ettelaie, P. I. Haris, N. J. James, B. Wilbourn, J. M. Adam, and K. R. Bruckdorfer, Biochem. Biophy. Acta. 1345, 237 (1997) https://doi.org/10.1016/S0005-2760(96)00185-3
  12. C. Y. Yang, S. H. Chen, S. H. Gianturco, W. A. Bradley, J. T. Sparrow, M. Tanimura, W. H. Li, D. A. Sparrow, S. Deloof, M. Rosseneu, F. S. Lee, Z. W. Gu, A. M. Gotto, L. Chan, Nature 323, 738 (1986) https://doi.org/10.1038/323738a0
  13. H. Jamila, C. H. Chua, J. K. Dickson, Y. Chenb, M. Yana, S. A. Billerb, R. C. Gregga, J. R. Wetteraua, and D. A. Gordana, J. Lipid Res. 39, 1448 (1998) https://doi.org/10.1016/S0022-2275(20)32526-8
  14. S. W. Law, S. M. Grant, and K. Hlguchi et al, Proc. Nati. Acad. Sci. U. S. A. 83, 8142 (1988)
  15. U. Stelnbrecher, J. Biol. Chem. 262, 3603 (1987) https://doi.org/10.1016/S0021-9258(18)61395-X
  16. S. Lee, D. Kim, H. Kim, Y. Lee, H. Won, Bull. Korean Chem. Soc. 25, 12 (2004)
  17. D. Kim, J. Rho, and H. Won, J. Kor. Magn. Reson. Soc. 3, 44 (1999)
  18. N. J. Greenfield, Trac-Trends Anal. Chem. 18, 236 (1999) https://doi.org/10.1016/S0165-9936(98)00112-5
  19. G. Kim, H. Won, J. Kor. Magn. Reson. Soc. 20, 96 (2016)
  20. G. Kim, H. Won, J. Kor. Magn. Reson. Soc. 24, 136 (2020) https://doi.org/10.6564/JKMRS.2020.24.4.136