biostudies-literatureLow KJYMinistry of Education - Singapore113-132https://www.ebi.ac.uk/biostudies/studies/S-EPMC8799873biostudies-literatureUnknown36<h4>Introduction</h4>Protein aggregation and deposition of uniformly arranged amyloid fibrils in the form of plaques or amorphous aggregates is characteristic of amyloid diseases. The accumulation and deposition of proteins result in toxicity and cause deleterious effects on affected individuals known as amyloidosis. There are about fifty different proteins and peptides involved in amyloidosis including neurodegenerative diseases and diseases affecting vital organs. Despite the strenuous effort to find a suitable treatment option for these amyloid disorders, very few compounds had made it to unsuccessful clinical trials. It has become a compelling challenge to understand and manage amyloidosis with the increased life expectancy and ageing population.<h4>Objective</h4>While most of the currJournal of advanced researchMolecular mechanisms of amyloid disaggregation.PMC8799873MOE2019-T3-1-012RG28/19Pervushin KMehta JSLow KJYVenkatraman AfalseMolecular mechanisms of amyloid disaggregation.<h4>Introduction</h4>Protein aggregation and deposition of uniformly arranged amyloid fibrils in the form of plaques or amorphous aggregates is characteristic of amyloid diseases. The accumulation and deposition of proteins result in toxicity and cause deleterious effects on affected individuals known as amyloidosis. There are about fifty different proteins and peptides involved in amyloidosis including neurodegenerative diseases and diseases affecting vital organs. Despite the strenuous effort to find a suitable treatment option for these amyloid disorders, very few compounds had made it to unsuccessful clinical trials. It has become a compelling challenge to understand and manage amyloidosis with the increased life expectancy and ageing population.<h4>Objective</h4>While most of the curr2022-01-01T00:00:00Z2022 Feb2025-04-04T07:51:11.151Z2025-04-04T07:51:11.151ZS-EPMC87998733512716910.1016/j.jare.2021.05.007