Pathological implications of nucleic acid interactions with proteins associated with neurodegenerative diseases

Biophysics Reviews
Yraima CordeiroMariana P B Gomes

Abstract

Protein misfolding disorders (PMDs) refer to a group of diseases related to the misfolding of particular proteins that aggregate and deposit in the cells and tissues of humans and other mammals. The mechanisms that trigger protein misfolding and aggregation are still not fully understood. Increasing experimental evidence indicates that abnormal interactions between PMD-related proteins and nucleic acids (NAs) can induce conformational changes. Here, we discuss these protein-NA interactions and address the role of deoxyribonucleic (DNA) and ribonucleic (RNA) acid molecules in the conformational conversion of different proteins that aggregate in PMDs, such as Alzheimer's, Parkinson's, and prion diseases. Studies on the affinity, stability, and specificity of proteins involved in neurodegenerative diseases and NAs are specifically addressed. A landscape of reciprocal effects resulting from the binding of prion proteins, amyloid-β peptides, tau proteins, huntingtin, and α-synuclein are presented here to clarify the possible role of NAs, not only as encoders of genetic information but also in triggering PMDs.

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Citations

Apr 20, 2017·The Journal of Biological Chemistry·Petar Stefanov KovachevSuparna Sanyal
Jan 29, 2020·Translational Neurodegeneration·Niccolo CandeliseInga Zerr
May 18, 2017·International Journal of Molecular Sciences·Bruno Macedo, Yraima Cordeiro
Jun 12, 2016·The Journal of Biological Chemistry·Jerson L Silva, Yraima Cordeiro
Feb 13, 2020·Scientific Reports·George TetzVictor Tetz
Jan 22, 2021·International Journal of Biological Macromolecules·Yulli M PassosYraima Cordeiro
Feb 27, 2020·Chemical Reviews·Moran Frenkel-PinterLuke J Leman
Oct 5, 2021·Nucleic Acids Research·Kannan HariniM Michael Gromiha

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