Servicio de Información Comunitario sobre Investigación y Desarrollo - CORDIS

A new process to form filaments of expanded PABPN1 in vitro

An in vitro assay was developed to induce formation of fibrillar aggregates with the mutant protein. The filaments had the anticipated characteristics of amyloid structures and could be induced by seeding.

Although conditions to induce filament formation could not be established for the full length PABPN1 protein, an N-terminal PABPN1 fragment was produced with the wild-type sequence, the +7 ala sequence and with the ala sequence. Upon incubation at high concentrations and for prolonged time periods, the formation of fibrillar aggregates was observed with the +7 ala mutant and, with a longer lag time and a more stringent concentration-dependence, also for the wild-type protein, but never for the ala mutant.

This result was made public through a publication in a scientific journal.

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MARTIN LUTHER UNIVERSITAET HALLE - WITTENBERG
Kurt-Mothes-Str.3
06120 HALLE/SAALE
Germany
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