Introduction of a fatty acid chain modification to prolong circulatory half-life of a radioligand towards glucose-dependent insulinotropic polypeptide receptor.

Glucose-dependent insulinotropic polypeptide receptor Incretins PET imaging Peptide radioligands

Journal

Nuclear medicine and biology
ISSN: 1872-9614
Titre abrégé: Nucl Med Biol
Pays: United States
ID NLM: 9304420

Informations de publication

Date de publication:
10 Jan 2024
Historique:
received: 04 10 2023
revised: 11 12 2023
accepted: 03 01 2024
medline: 20 1 2024
pubmed: 20 1 2024
entrez: 19 1 2024
Statut: aheadofprint

Résumé

The beneficial role of glucose-dependent insulinotropic polypeptide receptor (GIPR) in weight control and maintaining glucose levels has led to the development of several multi-agonistic peptide drug candidates, targeting GIPR and glucagon like peptide 1 receptor (GLP1R) and/or the glucagon receptor (GCGR). The in vivo quantification of target occupancy by these drugs would accelerate the development of new drug candidates. The aim of this study was to evaluate a novel peptide (GIP1234), based on previously reported ligand DOTA-GIP-C803, modified with a fatty acid moiety to prolong its blood circulation. It would allow higher target tissue exposure and consequently improved peptide uptake as well as in vivo PET imaging and quantification of GIPR occupancy by novel drugs of interest. A 40 amino acid residue peptide (GIP1234) was synthesized based on DOTA-GIP-C803, in turn based on the sequences of endogenous GIP and Exendin-4 with specific amino acid modifications to obtain GIPR selectivity. A palmitoyl fatty acid chain was furthermore added at Lys14 via a glutamic acid linker to prolong its blood circulation time by the interaction with albumin. GIP1234 was conjugated with a DOTA chelator at the C-terminal cysteine residue to achieve [ [

Sections du résumé

BACKGROUND BACKGROUND
The beneficial role of glucose-dependent insulinotropic polypeptide receptor (GIPR) in weight control and maintaining glucose levels has led to the development of several multi-agonistic peptide drug candidates, targeting GIPR and glucagon like peptide 1 receptor (GLP1R) and/or the glucagon receptor (GCGR). The in vivo quantification of target occupancy by these drugs would accelerate the development of new drug candidates. The aim of this study was to evaluate a novel peptide (GIP1234), based on previously reported ligand DOTA-GIP-C803, modified with a fatty acid moiety to prolong its blood circulation. It would allow higher target tissue exposure and consequently improved peptide uptake as well as in vivo PET imaging and quantification of GIPR occupancy by novel drugs of interest.
METHOD METHODS
A 40 amino acid residue peptide (GIP1234) was synthesized based on DOTA-GIP-C803, in turn based on the sequences of endogenous GIP and Exendin-4 with specific amino acid modifications to obtain GIPR selectivity. A palmitoyl fatty acid chain was furthermore added at Lys14 via a glutamic acid linker to prolong its blood circulation time by the interaction with albumin. GIP1234 was conjugated with a DOTA chelator at the C-terminal cysteine residue to achieve
RESULTS RESULTS
[
CONCLUSION CONCLUSIONS
[

Identifiants

pubmed: 38241936
pii: S0969-8051(24)00002-7
doi: 10.1016/j.nucmedbio.2024.108876
pii:
doi:

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

108876

Informations de copyright

Copyright © 2024 The Authors. Published by Elsevier Inc. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper. Martin Bossart is an employee of Sanofi Germany. Michael Wagner is an employee of Dewpoint Therapeutics. Olof Eriksson is an employee of Antaros Medical AB and a shareholder of Antaros Tracer AB. No other potential conflicts of interest relevant to this article exist.

Auteurs

Amina Khalil (A)

Science for Life Laboratory, Department of Medicinal Chemistry, Uppsala University, 751 83 Uppsala, Sweden.

Sona Hakhverdyan (S)

Science for Life Laboratory, Department of Medicinal Chemistry, Uppsala University, 751 83 Uppsala, Sweden.

Pierre Cheung (P)

Science for Life Laboratory, Department of Medicinal Chemistry, Uppsala University, 751 83 Uppsala, Sweden.

Martin Bossart (M)

R&D Research Platform, Integrated Drug Discovery, Sanofi, Frankfurt, Germany.

Michael Wagner (M)

R&D Research Platform, Integrated Drug Discovery, Sanofi, Frankfurt, Germany; Current address: Dewpoint Therapeutics, Frankfurt, Germany.

Olof Eriksson (O)

Science for Life Laboratory, Department of Medicinal Chemistry, Uppsala University, 751 83 Uppsala, Sweden; Antaros Medical AB, Mölndal, Sweden; Antaros Tracer AB, Mölndal, Sweden. Electronic address: olof.eriksson@ilk.uu.se.

Irina Velikyan (I)

Science for Life Laboratory, Department of Medicinal Chemistry, Uppsala University, 751 83 Uppsala, Sweden; Department of Surgical Sciences, Radiology, Uppsala University Uppsala, Sweden. Electronic address: irina.velikyan@akademiska.se.

Classifications MeSH