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Modifications of the Tic Residue in TIPP-Peptides

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Peptides: The Wave of the Future

Part of the book series: American Peptide Symposia ((APSY,volume 7))

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Abstract

H-Tyr-Tic-Phe-Phe-OH (TIPP) is a potent and selective δ-opioid antagonist developed by P. Schiller. Its δ-antagonist properties are related to the cyclic nature of the Tic residue. In the proposed bioactive conformation, the aromatic ring of Tic overlaps with the indole ring of the non-peptide δ-antagonist naltrindole (NTI) [1]. We have prepared several Tic analogs having modifications in the saturated ring 1, 2 or in the aromatic part 3, 4 (Figure 1).

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References

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© 2001 Springer Science+Business Media Dordrecht

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Tourwé, D. et al. (2001). Modifications of the Tic Residue in TIPP-Peptides. In: Lebl, M., Houghten, R.A. (eds) Peptides: The Wave of the Future. American Peptide Symposia, vol 7. Springer, Dordrecht. https://doi.org/10.1007/978-94-010-0464-0_318

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  • DOI: https://doi.org/10.1007/978-94-010-0464-0_318

  • Publisher Name: Springer, Dordrecht

  • Print ISBN: 978-94-010-3905-5

  • Online ISBN: 978-94-010-0464-0

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