A proopiomelanocortin-derived peptide sequence enhances plasma stability of peptide drugs.

Détails

ID Serval
serval:BIB_DF5744688599
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
A proopiomelanocortin-derived peptide sequence enhances plasma stability of peptide drugs.
Périodique
FEBS letters
Auteur(s)
Löw K., Roulin A., Kunz S.
ISSN
1873-3468 (Electronic)
ISSN-L
0014-5793
Statut éditorial
Publié
Date de publication
09/2020
Peer-reviewed
Oui
Volume
594
Numéro
17
Pages
2840-2866
Langue
anglais
Notes
Publication types: Journal Article
Publication Status: ppublish
Résumé
Bioactive peptide drugs hold promise for therapeutic application due to their high potency and selectivity but display short plasma half-life. Examination of selected naturally occurring peptide hormones derived from proteolytic cleavage of the proopiomelanocortin (POMC) precursor lead to the identification of significant plasma-stabilizing properties of a 12-amino acid serine-rich orphan sequence NSSSSGSSGAGQ in human γ3-melanocyte-stimulating hormone (MSH) that is homologous to previously discovered NS <sub>n</sub> GGH (n = 4-24) sequences in owls. Notably, transfer of this sequence to des-acetyl-α-MSH and the therapeutically relevant peptide hormones neurotensin and glucagon-like peptide-1 likewise enhance their plasma stability without affecting receptor signaling. The stabilizing effect of the sequence module is independent of plasma components, suggesting a direct effect in cis. This natural sequence module may provide a possible strategy to enhance plasma stability, complementing existing methods of chemical modification.
Mots-clé
blood-plasma, cerebrospinal fluid, peptide-drug stabilization, γ3-MSH-derived tag, blood plasma
Pubmed
Web of science
Création de la notice
10/06/2020 19:14
Dernière modification de la notice
20/01/2021 6:24
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