Biophysical Society Thematic Meeting - October 25-30, 2015

Polymers and Self Assembly: From Biology to Nanomaterials Poster Session II

21-POS Board 21 Prion-DNA Interaction Probed by Solution and Solid-State NMR Yohan Kevorkian 1 , Carolina C. Da Silva 1 , Cristina S. Resende 1 , Yraima Cordeiro 2 , Jerson L. Da Silva 1 , Mônica S. De Freitas 1 . 1 Universidade Federal do Rio de Janeiro, Rio de Janeiro, Brazil, 2 Universidade Federal do Rio de Janeiro, Rio de Janeiro, Brazil. Amyloidosis is a clinical disorder caused by extracellular deposition of proteins that suffered conformational modifications resulting in insoluble, abnormal fibrils that impair organ function. Prion is an uncommon amyloid disease, since pathogenic form of prion protein can transmit the disease between animals, coming to epizootic events that often spread to different species through various routes, such as inoculation or ingestion of contaminated meat. In the 1980’s, prion disease was implicated to a major epizootic event, in which more than 2 million UK cattle were infected. In humans, the number of cases to date has been relative modest, around 200. However, the genetic factors allied with widespread population exposure and the lower incubation time for prion diseases, suggest the need for caution. The main goal of this work is to apply solid-state NMR in order to obtain more information about prion fibrils formation and stabilization. Amyloid proteins are usually organized in ordered fibers, which are characterized by a cross beta-sheet quaternary structure. However the prion protein forms amorphous aggregates that are founded in the brain of infected animal, instead of fibrillar ones. The lack in the prion structural studies in the solid-state NMR field has opened opportunity to begin this work in one of the best laboratories that develop this technology and apply it to study formation of prion protein aggregates and the mechanisms underlying prion conversion. This study has good perspectives since it can help us to obtain atomic information about protein-protein and protein-nucleic acid interactions and the dynamics of monomer-fibers incorporation. Altogether, these information may contribute to the development of new strategies to control prion diseases.

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