Single-molecule approaches to prion protein misfolding

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Journal titlePrion
Pages140146; # of pages: 7
Subjectoligomer; prion protein; atomic force microscopy; energy; fluorescence correlation spectroscopy; fluorescence resonance energy transfer; human; molecular dynamics; molecular probe; molecule; nonhuman; optical tweezers; prion disease; protein aggregation; protein analysis; protein conformation; protein folding; protein misfolding; protein structure; review; single molecule probe
AbstractThe structural conversion of the prion protein PrP into a transmissible, misfolded form is the central element of prion disease, yet there is little consensus as to how it occurs. Key aspects of conversion into the diseased state remain unsettled, from details about the earliest stages of misfolding such as the involvement of partially- or fully-unfolded intermediates to the structure of the infectious state. Part of the difficulty in understanding the structural conversion arises from the complexity of the underlying energy landscapes. Single-molecule methods provide a powerful tool for probing complex folding pathways as in prion misfolding, because they allow rare and transient events to be observed directly. We discuss recent work applying single-molecule probes to study misfolding in prion proteins, and what it has revealed about the folding dynamics of PrP that may underlie its unique behavior. We also discuss single-molecule studies probing the interactions that stabilize non-native structures within aggregates, pointing the way to future work that may help identify the microscopic events triggering pathogenic conversion. Although single-molecule approaches to misfolding are relatively young, they have a promising future in prion science. © 2013 Landes Bioscience. © 2013 Landes Bioscience.
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AffiliationNational Research Council Canada (NRC-CNRC); National Institute for Nanotechnology (NINT-INNT)
Peer reviewedYes
NPARC number21269722
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Record identifier6e292684-08ac-4ba8-b2c9-580d385c7db6
Record created2013-12-13
Record modified2016-05-09
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