Solid-Phase Syntheses of Peptoids using Fmoc-Protected N-Substituted Glycines: The Synthesis of (Retro)Peptoids of Leu-Enkephalin and Substance P
✍ Scribed by John A. W. Kruijtzer; Lovina J. F. Hofmeyer; Wigger Heerma; Cornelis Versluis; Rob M. J. Liskamp
- Publisher
- John Wiley and Sons
- Year
- 1998
- Tongue
- English
- Weight
- 331 KB
- Volume
- 4
- Category
- Article
- ISSN
- 0947-6539
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✦ Synopsis
A particularly interesting class of oligomeric peptidomimetics is formed by the peptoids, which consist of N-substituted glycine residues. A solidphase synthesis method for peptoids is presented in which these residues are introduced using their Fmoc derivatives. This ªmonomerº method allowed the monitored synthesis of relatively large quantities of pure peptoids as well as the translation of, in principle, any peptide into the corresponding peptoid. The required Fmoc-substituted glycines were accessible by convenient synthesis, and a number of monomers including those containing side chains with functional groups have been synthesized. The use of Fmoc monomers also allowed implementation of a solid-phase synthesis protocol on a commercial peptide synthesizer. The method was exempli-fied by the solid-phase syntheses of the (retro)peptoids of Leu-enkephalin and substance P. Mass spectrometric studies of (retro)peptoids were essential for their characterization, and the presence of the B-and Y''-type ions allows sequence analysis. Substance P (retro)peptoids were biologically active. HPLC analysis showed an increased hydrophobicity, and pepsin treatment resulted in greatly reduced degradation compared with the corresponding peptide.