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Bioorg Med Chem Lett. 2008 Mar 15;18(6):2013-8. doi: 10.1016/j.bmcl.2008.01.110. Epub 2008 Feb 2.

Peptide backbone modifications on the C-terminal hexapeptide of neurotensin.

Author information

1
Department of Chemistry and Pharmacy, Emil Fischer Center, Friedrich Alexander University, D-91052 Erlangen, Germany.

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.

PMID:
18276136
DOI:
10.1016/j.bmcl.2008.01.110
[Indexed for MEDLINE]

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