Bulletin of the Korean Chemical Society

  • 제17권11호
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  • Pages.1036-1039
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  • 1996
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  • 0253-2964(pISSN)
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  • 1229-5949(eISSN)
대한화학회 (Korean Chemical Society)
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Characterization of Extremely Hydrophobic Immunostimulatory Lipoidal Peptides by Matrix Assisted Laser Desorption Ionization Mass Spectrometry

  • 발행 : 1996.11.20
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초록

Synthetic lipoidal peptides based on viral protein sequences have been prepared. These peptides contain an N-palmitoyl group at the N-terminal residue, which is a modified cysteine, containing a S-[2,3-bis(acyloxy)-(2-R,S)-propyl] moiety. When this residue (Pam3Cys) is at the N-terminus of a synthetic peptide, it acts as potent immunoadjuvant to enhance both IgM and IgG antibody responses to the attached peptide. Conventional analytical procedures (e.g., Edman degradation and amino acid analysis) are either not applicable due to the N-terminal modification, or do not provide confirmation of the intact structure. Chromatographic analysis is also hindered by the tendency of these lipoidal Pam3Cys peptides to form large aggregates, and in some cases to be permanently adsorbed on reversed phase columns. We have applied several mass spectrometric techniques, including fast atom bombardment (FAB), electrospray ionization (ESI) and matrix assisted laser desorption ionization (MALDI) to characterize the intact structures of a number of different Pam3Cys synthetic peptides. The MALDI-MS has been found to be the most sensitive for the analysis of the structure of Pam3Cys peptides.

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참고문헌

  1. J. Immunol. v.135 Bessler, W. G.;Cox, M.;Lex, A.;Suhr, B.;Wiesmuller, K.;Jung, G.
  2. Biochem. Biophys. Res. Commun. v.121 Bessler, W. G.;Cox, M.;Wiesmuller, K. H.;Jung, G.
  3. Hoppe Syeler's Z. Physiol. Chem. v.363 Bessler, W. G.;Johnson, R. B.;Wiesmuller, K. H.;Jung, G.
  4. Vaccine v.7 Wiesmuller, K.;Jung, G.;Hess, G.
  5. Nature v.342 Deres, K.;Schild, H.;Wiesmuller, K-H.;Jung, G.;Rammensee, H-G.
  6. Chem. Phys. Lipids v.28 Eibl, H.
  7. Anal. Chem. v.65 Caprioli, R.;Wu, A. H. B.
  8. Peptide Res. v.5 Ioannis, A. P.;Biemann, K.
  9. Proceedings 41st ASMS Conf. Mass Spectrom. Allied Topics Chang, Y-S.;Kanda, P.;Gage, D. A.
  10. Int. J. Peptide Protein Res. v.38 Metzger, J. W.;Wiesmuller, K-H.;Jung, G.
  11. Science v.237 Biemann, K.;Scoble, H. A.
  12. Int. J. Mass Spectrom. Ion Processes v.111 Hill, J. A.;Biller, J. E.;Biemann, K.
  13. Anal. Chem. v.67 Nelson, R. W.;Krone, J. R.;Bieber, A. L.;Williams, P.
  14. Anal. Chem. v.67 Alexander, A. J.;Hughes, D. E.
  15. Mass Spectrom. Reviews v.9 Fenn, J. B.;Mann, M.;Meng, C. K.;Wong, S. F.;Whitehouse, C. M.
  16. J. Am. Soc. Mass Spectrom. v.4 Fenn, J. B.
  17. Scientific American The Science of AIDS