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Lipid-Chaperone Hypothesis: A Common Molecular Mechanism of Membrane Disruption by Intrinsically Disordered Proteins

MF. Sciacca, F. Lolicato, C. Tempra, F. Scollo, BR. Sahoo, MD. Watson, S. García-Viñuales, D. Milardi, A. Raudino, JC. Lee, A. Ramamoorthy, C. La Rosa

. 2020 ; 11 (24) : 4336-4350. [pub] 20201203

Language English Country United States

Document type Journal Article, Research Support, N.I.H., Extramural, Research Support, Non-U.S. Gov't

Persistent link   https://www.medvik.cz/link/bmc21019632

Grant support
ZIA HL001055 Intramural NIH HHS - United States

An increasing number of human diseases has been shown to be linked to aggregation and amyloid formation by intrinsically disordered proteins (IDPs). Amylin, amyloid-β, and α-synuclein are, indeed, involved in type-II diabetes, Alzheimer's, and Parkinson's, respectively. Despite the correlation of the toxicity of these proteins at early aggregation stages with membrane damage, the molecular events underlying the process is quite complex to understand. In this study, we demonstrate the crucial role of free lipids in the formation of lipid-protein complex, which enables an easy membrane insertion for amylin, amyloid-β, and α-synuclein. Experimental results from a variety of biophysical methods and molecular dynamics results reveal that this common molecular pathway in membrane poration is shared by amyloidogenic (amylin, amyloid-β, and α-synuclein) and nonamyloidogenic (rat IAPP, β-synuclein) proteins. Based on these results, we propose a "lipid-chaperone" hypothesis as a unifying framework for protein-membrane poration.

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$a An increasing number of human diseases has been shown to be linked to aggregation and amyloid formation by intrinsically disordered proteins (IDPs). Amylin, amyloid-β, and α-synuclein are, indeed, involved in type-II diabetes, Alzheimer's, and Parkinson's, respectively. Despite the correlation of the toxicity of these proteins at early aggregation stages with membrane damage, the molecular events underlying the process is quite complex to understand. In this study, we demonstrate the crucial role of free lipids in the formation of lipid-protein complex, which enables an easy membrane insertion for amylin, amyloid-β, and α-synuclein. Experimental results from a variety of biophysical methods and molecular dynamics results reveal that this common molecular pathway in membrane poration is shared by amyloidogenic (amylin, amyloid-β, and α-synuclein) and nonamyloidogenic (rat IAPP, β-synuclein) proteins. Based on these results, we propose a "lipid-chaperone" hypothesis as a unifying framework for protein-membrane poration.
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$a Scollo, Federica $u Department of Chemical Sciences, University of Catania, Catania 95124, Italy $u J. Heyrovský Institute of Physical Chemistry, Academy of Sciences of the Czech Republic, Prague 117 20, Czech Republic
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$a Sahoo, Bikash R $u Biophysics and Department of Chemistry, University of Michigan, Ann Arbor, Michigan 48109-1055, United States
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$a Watson, Matthew D $u National Institutes of Health, Bethesda, Maryland 20892-0001, United States
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$a Lee, Jennifer C $u National Institutes of Health, Bethesda, Maryland 20892-0001, United States
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$a Ramamoorthy, Ayyalusamy $u Biophysics and Department of Chemistry, University of Michigan, Ann Arbor, Michigan 48109-1055, United States
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