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...
Guardado en:
Autores principales: | Francesco Simone Ruggeri, Johnny Habchi, Sean Chia, Robert I. Horne, Michele Vendruscolo, Tuomas P. J. Knowles |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2021
|
Materias: | |
Acceso en línea: | https://doaj.org/article/7f8ac1eb0b6149b48b24e7005907776f |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
Single molecule secondary structure determination of proteins through infrared absorption nanospectroscopy
por: Francesco Simone Ruggeri, et al.
Publicado: (2020) -
Screening of small molecules using the inhibition of oligomer formation in α-synuclein aggregation as a selection parameter
por: Roxine Staats, et al.
Publicado: (2020) -
Trodusquemine enhances Aβ42 aggregation but suppresses its toxicity by displacing oligomers from cell membranes
por: Ryan Limbocker, et al.
Publicado: (2019) -
A dopamine metabolite stabilizes neurotoxic amyloid-β oligomers
por: Rodrigo Cataldi, et al.
Publicado: (2021) -
Publisher Correction: A dopamine metabolite stabilizes neurotoxic amyloid-β oligomers
por: Rodrigo Cataldi, et al.
Publicado: (2021)