High-Affinity and Proteolytically Stable Peptidic Fluorescent NTS₁R Ligands.

ABSTRACT: Labeled ligands for the neurotensin receptor 1 (NTS₁R), which is expressed in the CNS, the gastrointestinal tract, and in malignant tumors, are needed to investigate NTS₁R-ligand binding and NTS₁R expression. Aiming for fluorescence-labeled neurotensin(8-13)-derived NTS₁R ligands with high affinity and proteolytic stability, several previous approaches were combined: (1) replacement of Arg⁸ by an amino-functionalized carbamoylated arginine, allowing conjugation to a fluorophore, (2) N^α-methylation of Arg⁸ and replacement of Tyr by β,β-dimethyl-l-Tyr¹¹, conferring proteolytic stability, and (3) replacement of Leu¹³ by trimethylsilyl-Ala, boosting binding affinity. This strategy gave flu

SUBMITTER: Ertl FJ 

PROVIDER: S-EPMC12481580 | biostudies-literature | 2025 Sep

REPOSITORIES: biostudies-literature