New Paradigm for Nano-Bio Interactions: Multimolecular Assembly of a Prototypical Disordered Protein with Ultrasmall Nanoparticles.
NMR spectroscopy
intrinsically disordered proteins
protein aggregation
protein−nanoparticle interaction
ultrasmall nanoparticles
Journal
Nano letters
ISSN: 1530-6992
Titre abrégé: Nano Lett
Pays: United States
ID NLM: 101088070
Informations de publication
Date de publication:
23 11 2022
23 11 2022
Historique:
pubmed:
9
11
2022
medline:
25
11
2022
entrez:
8
11
2022
Statut:
ppublish
Résumé
Understanding the interactions between nanoparticles (NPs) and proteins is crucial for the successful application of NPs in biological contexts. Protein adsorption is dependent on particle size, and protein binding to ultrasmall (1-3 nm) NPs is considered to be generally weak. However, most studies have involved structured biomacromolecules, while the interactions of ultrasmall NPs with intrinsically disordered proteins (IDPs) have remained elusive. IDPs are abundant in eukaryotes and found to associate with NPs intracellularly. As a model system, we focused on ultrasmall gold nanoparticles (usGNPs) and tau, a cytosolic IDP associated with Alzheimer's disease. Using site-resolved NMR, steady-state fluorescence, calorimetry, and circular dichroism, we reveal that tau and usGNPs form stable multimolecular assemblies, representing a new type of nano-bio interaction. Specifically, the observed interaction hot spots explain the influence of usGNPs on tau conformational transitions, with implications for the intracellular targeting of aberrant IDP aggregation.
Identifiants
pubmed: 36346924
doi: 10.1021/acs.nanolett.2c02902
pmc: PMC9706667
doi:
Substances chimiques
Gold
7440-57-5
Intrinsically Disordered Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
8875-8882Références
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