Journal
BIOCHIMIE
Volume 202, Issue -, Pages 123-135Publisher
ELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER
DOI: 10.1016/j.biochi.2022.08.003
Keywords
Amyloid proteins; Protein aggregation; Amyloid therapeutics; Fluorinated compounds; Fluorinated nanoparticles
Categories
Funding
- Laboratory for Process Engineering, Environment, Biotechnology and Energy-LEPABE - national funds through the FCT/MCTES (PIDDAC)
- 2SMART-engineered Smart materials for Smart citizens [NORTE-01-0145-FEDER-000054]
- Norte Portugal Regional Operational Programme (NORTE 2020), under the PORTUGAL 2020 Partnership Agreement, through the European Regional Development Fund (ERDF)
- J.A.L. under the Scientific Employment Stimulus-Institutional Call [SFRH/BD/2020.04 932.BD, CEECINST/00049/2018]
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Amyloidosis is a disease caused by improperly folded proteins accumulating in tissues and damaging organs. It has a significant impact on global health, but there are currently no effective treatments available. However, recent research has shown the potential of fluorine-modified therapeutic molecules and nanoparticles in regulating amyloidogenic proteins.
Amyloidosis, commonly known as amyloid-associated diseases, is characterized by improperly folded proteins accumulating in tissues and eventually causing organ damage, which is linked to several dis-orders ranging from neurodegenerative to peripheral diseases. It has an enormous societal and financial impact on the global health sector. Due to the complexity of protein misfolding and intertwined ag-gregation, there are no effective disease-modifying medications at present, and the condition is likely mis/non-diagnosed half of the time. Nonetheless, over the last two decades, substantial research into aggregation processes has revealed the possibilities of new intervention approaches. On the other hand, fluorine has been a rising star in therapeutic development for numerous neurodegenerative illnesses and other peripheral diseases. In this study, we revised and emphasized the possible significance of fluorine -modified therapeutic molecules and fluorine-modified nanoparticles (NPs) in the modulation of amy-loidogenic proteins, including insulin, amyloid beta peptide (A0), prion protein (PrP), transthyretin (TTR) and Huntingtin (htt). (c) 2022 The Authors. Published by Elsevier B.V. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
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