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Published on: May 22, 2018
Inhibition of Amyloid Protein Aggregation Using Selected Peptidomimetics
1Department of Organic Synthesis and Process Chemistry, CSIR-Indian Institute of Chemical Technology (CSIR-IICT), Hyderabad, 500007, India.
Abstract:
Aberrant protein aggregation leads to the formation of amyloid fibrils. This phenomenon is linked to the development of more than 40 irremediable diseases such as Alzheimer's disease, Parkinson's disease, type 2 diabetes, and cancer. Plenty of research efforts have been given to understanding the underlying mechanism of protein aggregation, associated toxicity, and the development of amyloid inhibitors. Recently, the peptidomimetic approach has emerged as a potential tool to modulate several protein-protein interactions (PPIs). In this review, we discussed selected peptidomimetic-based approaches for the modulation of important amyloid proteins (Islet Amyloid Polypeptide, Amyloid Beta, α-synuclein, mutant p53, and insulin) aggregation. This approach holds a powerful platform for creating an essential stepping stone for the vital development of anti-amyloid therapeutic agents.
Insights
Peptidomimetics can inhibit amyloid protein aggregation, offering a new therapeutic strategy for diseases like Alzheimer's and Parkinson's. This approach targets protein-protein interactions to develop novel anti-amyloid agents.
Area of Science:
- Biochemistry and Molecular Biology
- Drug Discovery and Development
- Neuroscience and Neurodegenerative Diseases
Background:
- Aberrant protein aggregation into amyloid fibrils is implicated in over 40 incurable diseases, including Alzheimer's, Parkinson's, type 2 diabetes, and cancer.
- Understanding the mechanisms of protein aggregation and toxicity is crucial for developing effective therapeutic interventions.
- Amyloid inhibitors are actively researched to combat these debilitating conditions.
Purpose of the Study:
- To review peptidomimetic-based strategies for modulating the aggregation of key amyloidogenic proteins.
- To highlight the potential of peptidomimetics as a therapeutic tool against amyloid-related diseases.
- To explore the application of peptidomimetics in targeting specific amyloid proteins like Islet Amyloid Polypeptide, Amyloid Beta, α-synuclein, mutant p53, and insulin.
Main Methods:
- Literature review of peptidomimetic approaches targeting protein-protein interactions (PPIs).
- Focus on studies modulating the aggregation of specific amyloid proteins: Islet Amyloid Polypeptide (IAPP), Amyloid Beta (Aβ), α-synuclein, mutant p53, and insulin.
- Analysis of how peptidomimetics interfere with the formation of amyloid fibrils.
Main Results:
- Peptidomimetics show promise in modulating the aggregation pathways of critical amyloidogenic proteins.
- These agents can interfere with protein-protein interactions essential for fibril formation.
- The reviewed approaches demonstrate the versatility of peptidomimetics in targeting diverse amyloid proteins.
Conclusions:
- Peptidomimetic-based strategies offer a powerful platform for developing novel anti-amyloid therapeutic agents.
- This approach represents a significant step towards creating treatments for a range of irremediable amyloid diseases.
- Further research into peptidomimetics could lead to breakthrough therapies for neurodegenerative and other amyloid-associated conditions.
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