Litcius/Paper detail

Inhibition of Amyloid Protein Aggregation Using Selected Peptidomimetics

Debabrata Maity

2022ChemMedChem16 citationsDOI

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.

Topics & Concepts

PeptidomimeticAmyloid (mycology)Protein aggregationAmyloid fibrilAmyloid diseaseProtein–protein interactionProtein foldingMechanism (biology)ChemistryBiochemistryAmyloid βDiseaseComputational biologyBiologyMedicinePeptidePathologyPhilosophyEpistemologyInorganic chemistryChemical Synthesis and AnalysisAlzheimer's disease research and treatmentsProtein Structure and Dynamics