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Title: Tannic Acid Inhibits α-Synuclein Amyloid Fibril Formation via Binding to the Monomer N-terminal Domain
Authors: Stoeber, Jonathan
Keywords: alpha synuclein; axit tannic; protein; rối loạn nội tại; polyphenol; phối tử
Issue Date: 2021
Publisher: bioRxiv
Abstract: α-Synuclein (αS) is an intrinsically disordered protein (IDP) that aggregates into amyloid fibrils during the progression of Parkinson’s Disease and other synucleinopathies. The N-terminal domain (residues 1-60) is now understood to play a critical role in the initial nucleation of aggregation, as well as a pivotal role in the monomer-fibril interaction underlying amyloid seeding. Here we report on the interaction between αS and the polyphenol tannic acid (TA), where a combination of solution NMR, atomic force microscopy (AFM), and ThT assays have identified that TA targets the aS N-terminal domain to inhibit amyloid fibril formation in a pH dependent manner. This work highlights the importance of targeting the N-terminus of aS to arrest fibril formation, and suggests the importance of including polyphenolic moieties in future amyloid inhibitors.
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