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Estabilidad conformacional de la proteína priónica del hámster sirio PrP ((90-231))

Megan Grabenauer¹, Thomas Wyttenbach, Narinder Sanghera

¹Department of Chemistry and Biochemistry, University of California, Santa Barbara, California 93106, USA.

Journal of the American Chemical Society

|June 12, 2010

Resumen

Los investigadores descubrieron una forma altamente estable de la proteína priónica (PrP(C)) utilizando técnicas avanzadas de IMS-MS. Este hallazgo desafía la comprensión previa de la estabilidad de PrP ((C) en la investigación de las encefalopatías espongiformes transmisibles.

Área de la Ciencia:

La bioquímica es la bioquímica.
Biología Estructural Biología Estructural
La neurociencia es la neurociencia.

Sus antecedentes:

Las encefalopatías espongiformes transmisibles (ETS) están vinculadas a las proteínas priónicas mal plegadas (PrP(Sc)).
La proteína priónica celular normal (PrP(C)) generalmente se considera menos estable que su contraparte mal plegada.
Comprender la estabilidad de PrP (C) es crucial para la investigación de la patogénesis de las EET.

Objetivo del estudio:

Para investigar la estabilidad conformacional de la proteína priónica recombinante PrP ((90-231).
Explorar la existencia de conformaciones estables de PrP(C) bajo condiciones específicas.
Para medir las secciones transversales de colisión absoluta para el hámster sirio PrP ((90-231).

Principales métodos:

Espectrometría de masa de movilidad iónica utilizada (IMS-MS).
Aplicó altas energías de inyección y temperaturas superiores a 600 K.
Se analizó la proteína priónica recombinante del hámster sirio PrP ((90-231).1).

Principales resultados:

Se encontraron pruebas de una conformación altamente estable de PrP recombinante (residuos 90-231).
Esta conformación estable resistió el despliegue en ausencia de disolvente.
Informó las primeras secciones transversales de colisión absoluta para PrP ((90-231).1).

Conclusiones:

El PrP recombinante puede adoptar conformaciones excepcionalmente estables, contrariamente a las suposiciones anteriores.
Los hallazgos proporcionan nuevos conocimientos sobre la dinámica estructural de las proteínas priónicas.
Este trabajo avanza en la comprensión del comportamiento de las proteínas priónicas relevantes para las EET.

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