Minimal Increments of Hydrophobic Collapse within the N-Terminus of the Neuropeptide Galanin.
Journal
Biochemistry
ISSN: 1520-4995
Titre abrégé: Biochemistry
Pays: United States
ID NLM: 0370623
Informations de publication
Date de publication:
21 06 2022
21 06 2022
Historique:
pubmed:
28
5
2022
medline:
23
6
2022
entrez:
27
5
2022
Statut:
ppublish
Résumé
The neuropeptide galanin has a 35-year history as an intriguing target in drug design owing to its implication as a potential anticonvulsant and neuronal trophic factor among many other therapeutically interesting functions including analgesia and mood alteration. In this study, we report the structural characterization of three synthetic fragments of the galanin N-terminus in buffered aqueous solution: hGal(2-12)KK, hGal(1-12)KK, and hGal(1-17)KK. High-field two-dimensional
Identifiants
pubmed: 35622960
doi: 10.1021/acs.biochem.2c00141
doi:
Substances chimiques
Neuropeptides
0
Peptides
0
Galanin
88813-36-9
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
1151-1166Subventions
Organisme : NIGMS NIH HHS
ID : P20 GM103499
Pays : United States
Organisme : Howard Hughes Medical Institute
Pays : United States