Previous Page  79 / 92 Next Page
Information
Show Menu
Previous Page 79 / 92 Next Page
Page Background

- 78 -

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.