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Are Amyloid Fibrils RNA-Traps? A Molecular Dynamics Perspective.


ABSTRACT: The self-assembly of proteins and peptides into amyloids is a key feature of an increasing number of diseases. Amyloid fibrils display a unique surface reactivity endowing the sequestration of molecules such as MicroRNAs, which can be the active moiety of the toxic action. To test this hypothesis we studied the recognition between a model RNA and two different steric zipper spines using molecular dynamics simulations. We found that the interaction occurs and displays peptide-sequence dependence. Interestingly, interactions with polar zipper surfaces such as the formed by SNQNNF are more stable and favor the formation of ?-barrel like complexes resembling the structures of toxic oligomers. These sequence-structure-recognition relationships of the two different assemblies may be exploited for the design of compounds targeting the fibers or competing with RNA-amyloid attachment.

SUBMITTER: Meli M 

PROVIDER: S-EPMC6004406 | biostudies-literature | 2018

REPOSITORIES: biostudies-literature

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Are Amyloid Fibrils RNA-Traps? A Molecular Dynamics Perspective.

Meli Massimiliano M   Gasset Maria M   Colombo Giorgio G  

Frontiers in molecular biosciences 20180611


The self-assembly of proteins and peptides into amyloids is a key feature of an increasing number of diseases. Amyloid fibrils display a unique surface reactivity endowing the sequestration of molecules such as MicroRNAs, which can be the active moiety of the toxic action. To test this hypothesis we studied the recognition between a model RNA and two different steric zipper spines using molecular dynamics simulations. We found that the interaction occurs and displays peptide-sequence dependence.  ...[more]

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