Abstract
Protein misfolding as well as the subsequent self-association and deposition of amyloid aggregates is implicated in the progression of several neurodegenerative disorders including Alzheimer’s and Parkinson’s diseases. Modulators of amyloidogenic aggregation serve as essential tools to dissect the underlying molecular mechanisms and may offer insight on potential therapeutic solutions. These modulators include green tea catechins, which are potent inhibitors of amyloid aggregation. Although catechins often exhibit poor pharmacokinetic properties and bioavailability, they are still essential tools for identifying the drivers of amyloid aggregation and for developing other aggregation modulators through structural mimicry. As an illustration of such strategies, here we review how catechins have been used to map the toxic surfaces of oligomeric amyloid-like species and develop catechin-based phenolic compounds with enhanced anti-amyloid activity.
Highlights
Neurodegenerative diseases, including Alzheimer’s disease (AD) and Parkinson’s disease (PD), have been associated with the accumulation of amyloid-like aggregates formed by intrinsically disordered proteins (IDPs) [1]
These results are in agreement with the previously discussed data reported for epigallocatechin gallate (EGCG) by Ahmed et al [21]
Structural comparison with untreated, toxic assemblies mainly at the central hydrophobic core of Aβ. These results are in agreement with the previously unveiled the molecular determinants underlying membrane binding and damage as well as cellular discussed data reported for EGCG by Ahmed et al [21]
Summary
Neurodegenerative diseases, including Alzheimer’s disease (AD) and Parkinson’s disease (PD), have been associated with the accumulation of amyloid-like aggregates formed by intrinsically disordered proteins (IDPs) [1]. Antioxidant, and anti-inflammatory properties make catechins a potential therapeutic lead for the treatment of neurodegenerative diseases, their typically poor pharmacokinetics, including variable bioavailability and instability, limit their effectiveness as drug leads [33]. [21,27,34,35,36].InInaddition, addition, alsopresent present other studies where previous knowledge of catechin-based amyloid inhibition was useful forsynthesis the synthesis new previous knowledge of catechin-based amyloid inhibition was useful for the of newofphenolic phenolic compounds [12,37,38]. Field [32,39,40,41,42,43,44]
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