Transition-Linker Containing Detergents for Membrane Protein Studies.
NMR spectroscopy
detergents
membrane proteins
micelles
transition linkers
Journal
Chemistry (Weinheim an der Bergstrasse, Germany)
ISSN: 1521-3765
Titre abrégé: Chemistry
Pays: Germany
ID NLM: 9513783
Informations de publication
Date de publication:
09 Dec 2022
09 Dec 2022
Historique:
received:
18
07
2022
pubmed:
3
9
2022
medline:
15
12
2022
entrez:
2
9
2022
Statut:
ppublish
Résumé
It is a pressing need, but still challenging to explore the structure and function of membrane proteins (MPs). One of the main obstacles is the limited availability of matched detergents for the handling of specific MPs. We describe herein the design of new detergents by incorporation of a transition linker between the hydrophilic head and the hydrophobic tail. This design allows a gradual change of hydrophobicity between the outside and inside of micelles, in contrast to the abrupt switch in conventional detergents. Notably, many of these detergents assembled into micelles in while retaining low critical micelle concentrations. Meanwhile, thermal stabilizing evaluation identified superior detergents for representative MPs, including G protein-coupled receptors and a transporter protein. Among them, further improved the NMR study of MPs. We anticipate these that results will encourage future detergent expansion through new remodeling on the traditional detergent scaffold.
Identifiants
pubmed: 36053145
doi: 10.1002/chem.202202242
doi:
Substances chimiques
Detergents
0
Membrane Proteins
0
Micelles
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
e202202242Subventions
Organisme : National Natural Science Foundation of China
ID : 21672147
Informations de copyright
© 2022 Wiley-VCH GmbH.
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