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05:48
Rapid Generation of Amyloid from Native Proteins In vitro
Published on: December 5, 2013
Comportamiento parecido al amiloide en los foldameres abióticos y anfifílicos
Valerie J Bradford1, Brent L Iverson
1Department of Chemistry and Biochemistry, The University of Texas at Austin, Texas 78712, USA.
Journal of the American Chemical Society
|January 5, 2008
Resumen
Los foldameros anfifílicos, que no son proteínas, pueden formar hidrogeles similares a los amiloides cuando se calientan. Los cambios estructurales sutiles tienen un impacto significativo en las propiedades del hidrogel, revelando el comportamiento general de plegamiento de las moléculas.
Área de la Ciencia:
- Química supramolecular de las moléculas.
- Ciencia de los materiales Ciencia de los materiales.
- Los biomateriales son biomateriales.
Sus antecedentes:
- Los foldameros anfifílicos abióticos reportados anteriormente sufren cambios conformacionales irreversibles al calentarse.
- Este estudio investiga una serie de foldameres estructuralmente relacionados para refinar la comprensión de su conmutación conformacional.
Objetivo del estudio:
- Explorar el comportamiento de conmutación y agregación conformacional de los nuevos foldameres anfifílicos.
- Para caracterizar la formación de hidrogel y las propiedades de estos foldamers.
- Investigar el potencial para el ensamblaje tipo amiloide en moléculas no proteicas.
Principales métodos:
- Síntesis y caracterización de una serie de foldameres anfifílicos.
- Tratamiento térmico para inducir cambios conformacionales y agregación.
- Mediciones reológicas para evaluar las propiedades del hidrogel.
- Espectroscopia de dicroísmo circular para analizar el ensamblaje molecular.
Principales resultados:
- Todos los foldamers exhibieron conformaciones dobladas antes del calentamiento.
- El calentamiento a 80°C indujo la agregación irreversible y la formación de hidrogel en tres de los cuatro foldamers.
- La formación de hidrogel dependía del ensamblaje intermolecular altamente ordenado, análogo a la formación de proteínas amiloides.
- Las sutiles diferencias estructurales entre los isómeros de foldamer llevaron a variaciones significativas en las propiedades del hidrogel.
Conclusiones:
- El comportamiento parecido al amiloide no es exclusivo de las proteínas y se puede observar en moléculas plegables anfifílicas.
- Los foldamers anfifílicos pueden autoensamblarse en hidrogeles ordenados con propiedades sintonizables.
- Este trabajo proporciona un modelo refinado para la conmutación y agregación conformacional de pliegues.
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