Peptide backbone modifications on the C-terminal hexapeptide of neurotensin

Einsiedel J, Hübner H, Hervet M, Härterich S, Koschatzky S, Gmeiner P (2008)


Publication Type: Journal article

Publication year: 2008

Journal

Publisher: Elsevier

Book Volume: 18

Pages Range: 2013-2018

DOI: 10.1016/j.bmcl.2008.01.110

Abstract

To compare backbone-induced susceptibilities with affinity changes that are caused by side-chain modifications in the respective positions, structure activity relationship studies on a series of NT(8-13) analogues were performed providing valuable insights into the major requirement for neurotensin receptor recognition and activation. The data led us to highly potent NTR1 ligands and the generation of a pharmacophore model that will be helpful for the discovery of therapeutically relevant non-peptidic NTR1 agonists. © 2008 Elsevier Ltd. All rights reserved.

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APA:

Einsiedel, J., Hübner, H., Hervet, M., Härterich, S., Koschatzky, S., & Gmeiner, P. (2008). Peptide backbone modifications on the C-terminal hexapeptide of neurotensin. Bioorganic & Medicinal Chemistry Letters, 18, 2013-2018. https://doi.org/10.1016/j.bmcl.2008.01.110

MLA:

Einsiedel, Jürgen, et al. "Peptide backbone modifications on the C-terminal hexapeptide of neurotensin." Bioorganic & Medicinal Chemistry Letters 18 (2008): 2013-2018.

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