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DC Field | Value | Language |
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dc.contributor.author | Agarwal, Aishwarya | - |
dc.contributor.author | Das, Debapriya | - |
dc.contributor.author | Banerjee, Tisya | - |
dc.contributor.author | Mukhopadhyay, S. | - |
dc.date.accessioned | 2020-12-28T06:19:11Z | - |
dc.date.available | 2020-12-28T06:19:11Z | - |
dc.date.issued | 2020 | - |
dc.identifier.citation | Biochimica et Biophysica Acta - Proteins and Proteomics 1868(2), | en_US |
dc.identifier.other | https://doi.org/10.1016/j.bbapap.2019.140324 | - |
dc.identifier.uri | https://www.sciencedirect.com/science/article/pii/S1570963919302092?via%3Dihub | - |
dc.identifier.uri | http://hdl.handle.net/123456789/3408 | - |
dc.description.abstract | Excitation energy migration via homo-Förster resonance energy transfer (homo-FRET) can serve as an intermolecular proximity ruler within complex biomolecular assemblies. Here we present a unique case to demonstrate that energy migration can be a novel and sensitive readout to capture the membrane-mediated misfolding and oligomerization of the human prion protein (PrP), which is known to undergo an aberrant conformational conversion from an α-helical form into a self-propagating aggregated β-rich state causing deadly transmissible neurodegenerative diseases. Using site-specific energy migration studies by monitoring steady-state and time-resolved fluorescence anisotropy of fluorescently-tagged PrP, we elucidate the molecular details of lipid membrane-induced oligomers. We show that the intrinsically disordered N-terminal segment is critical for lipid-induced conformational sequestration of PrP into higher-order, β-rich oligomeric species that exhibit membrane permeabilization. Our results revealed that the N-terminal regions constitute the central core of the oligomeric architecture, whereas the distal C-terminal ends participate in peripheral association with the lipid membrane. Our study will find applications in the sensitive detection and in the structural characterization of membrane-induced protein misfolding and aggregation in a variety of deadly amyloid diseases. | en_US |
dc.language.iso | en | en_US |
dc.publisher | Elsevier | en_US |
dc.subject | Depolarization kinetics | en_US |
dc.subject | Förster resonance energy transfer | en_US |
dc.subject | Fluorescence anisotropy | en_US |
dc.subject | Intrinsically disordered regions | en_US |
dc.title | Energy migration captures membrane-induced oligomerization of the prion protein | en_US |
dc.type | Article | en_US |
Appears in Collections: | Research Articles |
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