Infrared nanospectroscopy reveals the molecular interaction fingerprint of an aggregation inhibitor with single Aβ42 oligomers
Our understanding of the molecular mechanisms underlying pathological protein aggregation remains incomplete. Here, single molecule infrared nanospectroscopy (AFM-IR) offers insight into the structure of Aβ42 oligomeric and fibrillar species and their interaction with an aggregation inhibitor, pavin...
Enregistré dans:
Auteurs principaux: | Francesco Simone Ruggeri, Johnny Habchi, Sean Chia, Robert I. Horne, Michele Vendruscolo, Tuomas P. J. Knowles |
---|---|
Format: | article |
Langue: | EN |
Publié: |
Nature Portfolio
2021
|
Sujets: | |
Accès en ligne: | https://doaj.org/article/7f8ac1eb0b6149b48b24e7005907776f |
Tags: |
Ajouter un tag
Pas de tags, Soyez le premier à ajouter un tag!
|
Documents similaires
-
Single molecule secondary structure determination of proteins through infrared absorption nanospectroscopy
par: Francesco Simone Ruggeri, et autres
Publié: (2020) -
Screening of small molecules using the inhibition of oligomer formation in α-synuclein aggregation as a selection parameter
par: Roxine Staats, et autres
Publié: (2020) -
Trodusquemine enhances Aβ42 aggregation but suppresses its toxicity by displacing oligomers from cell membranes
par: Ryan Limbocker, et autres
Publié: (2019) -
A dopamine metabolite stabilizes neurotoxic amyloid-β oligomers
par: Rodrigo Cataldi, et autres
Publié: (2021) -
Publisher Correction: A dopamine metabolite stabilizes neurotoxic amyloid-β oligomers
par: Rodrigo Cataldi, et autres
Publié: (2021)