Cell-free synthesis of amyloid fibrils with infectious properties and amenable to sub-milligram magic-angle spinning NMR analysis.
Journal
Communications biology
ISSN: 2399-3642
Titre abrégé: Commun Biol
Pays: England
ID NLM: 101719179
Informations de publication
Date de publication:
09 11 2022
09 11 2022
Historique:
received:
25
07
2022
accepted:
26
10
2022
entrez:
9
11
2022
pubmed:
10
11
2022
medline:
15
11
2022
Statut:
epublish
Résumé
Structural investigations of amyloid fibrils often rely on heterologous bacterial overexpression of the protein of interest. Due to their inherent hydrophobicity and tendency to aggregate as inclusion bodies, many amyloid proteins are challenging to express in bacterial systems. Cell-free protein expression is a promising alternative to classical bacterial expression to produce hydrophobic proteins and introduce NMR-active isotopes that can improve and speed up the NMR analysis. Here we implement the cell-free synthesis of the functional amyloid prion HET-s(218-289). We present an interesting case where HET-s(218-289) directly assembles into infectious fibril in the cell-free expression mixture without the requirement of denaturation procedures and purification. By introducing tailored
Identifiants
pubmed: 36352173
doi: 10.1038/s42003-022-04175-1
pii: 10.1038/s42003-022-04175-1
pmc: PMC9646696
doi:
Substances chimiques
Amyloid
0
Prions
0
Amyloidogenic Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1202Informations de copyright
© 2022. The Author(s).
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