Development of disulfide-functionalized peptides covalently binding G protein-coupled receptors

Einsiedel J, Schmidt M, Hübner H, Gmeiner P (2022)

Publication Type: Journal article

Publication year: 2022

Journal

Book Volume: 61

Article Number: 116720

DOI: 10.1016/j.bmc.2022.116720

Abstract

A broadly applicable synthesis of peptides incorporating mixed disulfides between cysteine and homocysteine and cysteamine was developed. The method was established using pharmacologically relevant G protein-coupled receptor (GPCR) ligands including the μ-receptor agonist Dmt-DALDA and extended to the orexin derivative Oxa(17–33) and NT(8–13), the C-terminal hexapeptide of neurotensin. The newly developed NT(8–13) analog 6b incorporating an S-functionalized homocysteine revealed covalent binding of the neurotensin receptor 1 (NTSR1) in a radioligand depletion study.

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How to cite

APA:

Einsiedel, J., Schmidt, M., Hübner, H., & Gmeiner, P. (2022). Development of disulfide-functionalized peptides covalently binding G protein-coupled receptors. Bioorganic & Medicinal Chemistry, 61. https://doi.org/10.1016/j.bmc.2022.116720

MLA:

Einsiedel, Jürgen, et al. "Development of disulfide-functionalized peptides covalently binding G protein-coupled receptors." Bioorganic & Medicinal Chemistry 61 (2022).

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