Inhibiting mTTR Aggregation/Fibrillation by a Chaperone-like Hydrophobic Amino Acid-Conjugated SPION

Transthyretin (TTR) aggregation via misfolding of a mutant or wild-type protein leads to systemic or partial amyloidosis (ATTR). Here, we utilized variable biophysical assays to characterize two distinct aggregation pathways for mTTR (a synthesized monomer TTR incapable of association into a tetrame...

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Veröffentlicht in:	The journal of physical chemistry. B 2022-03, Vol.126 (8), p.1640-1654
Hauptverfasser:	Arghavani, Payam, Badiei, Alireza, Ghadami, Seyyed Abolghasem, Habibi-Rezaei, Mehran, Moosavi-Movahedi, Faezeh, Delphi, Ladan, Moosavi-Movahedi, Ali Akbar
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acids Amyloid - chemistry B: Biophysical and Biochemical Systems and Processes Magnetic Iron Oxide Nanoparticles Molecular Chaperones - metabolism Protein Conformation, beta-Strand Protein Structure, Secondary
Online-Zugang:	Volltext
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