Improved method for preparation and purification of recombinant α-synuclein: high-mannose-type free N-glycan prepared from an edible bean (Vigna angulari, Azuki bean) inhibits α-synuclein aggregation

Parkinson's disease is characterized by the accumulation of amyloid, which consists of α-synuclein (α-Syn). To screen compounds with amyloid aggregation inhibitory activity, an effective method for the preparation of α-Syn is a prerequisite. We established a simpler method for α-Syn preparation...

Full description

Saved in:
Bibliographic Details
Published inBioscience, biotechnology, and biochemistry Vol. 86; no. 6; pp. 770 - 774
Main Authors Kosaka, Shota, Katsube, Makoto, Maeda, Megumi, Kimura, Yoshinobu
Format Journal Article
LanguageEnglish
Published England 24.05.2022
Subjects
inhibition of amyloid aggregation
rapid purification
free N-glycans
α-synuclein
Online AccessGet full text

Cover

More Information
Summary:Parkinson's disease is characterized by the accumulation of amyloid, which consists of α-synuclein (α-Syn). To screen compounds with amyloid aggregation inhibitory activity, an effective method for the preparation of α-Syn is a prerequisite. We established a simpler method for α-Syn preparation using freeze-thaw treatment of transformed Escherichia coli. Furthermore, we found that the high-mannose type free N-glycans could prevent α-Syn aggregation.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:1347-6947
1347-6947
DOI:10.1093/bbb/zbac040