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Análisis y control de la movilidad de la cadena en hidrogeles de proteínas
Peter B Rapp1, Ahmad K Omar1, Jeff J Shen1
1Division of Chemistry and Chemical Engineering, California Institute of Technology , 1200 East California Boulevard, MC 210-41, Pasadena, California 91125, United States.
Journal of the American Chemical Society
|February 23, 2017
Resumen
Los investigadores utilizaron la recuperación de la fluorescencia después del foto blanqueamiento para estudiar la movilidad de la cadena de hidrogel de proteínas. Descubrieron que la modificación de dominios de bobina enrollada altera significativamente el movimiento de la cadena, lo que permite propiedades de material sintonizables.
Área de la Ciencia:
- Ciencia de los biomateriales
- Química de los polímeros
- Ingeniería de proteínas
Sus antecedentes:
- Los copolímeros de bloque de proteínas con dominios en espiral forman hidrogeles viscoelásticos físicamente entrelazados.
- La comprensión de la dinámica de la cadena es crucial para el diseño de materiales de hidrogel avanzados.
Objetivo del estudio:
- Investigar la movilidad de la cadena en hidrogeles basados en proteínas reversibles.
- Para correlacionar la dinámica de la red de hidrogel con el comportamiento del dominio de la bobina.
- Para demostrar el control de la movilidad de la cadena a través de la ingeniería de proteínas.
Principales métodos:
- Se utilizó la recuperación de fluorescencia después del fotoblanqueamiento (FRAP) para cuantificar la movilidad de la cadena de la sonda.
- Aplicó un modelo de salto de tres estados para analizar la dinámica de la migración en cadena.
- Empleó programación genética para modificar sistemáticamente las secuencias de proteínas.
- Realizó mutagenesis dirigida al sitio e introdujo residuos hidrofóbicos para alterar la estabilidad y las interacciones entre bobinas.
Principales resultados:
- La movilidad de la cadena en los hidrogeles está directamente relacionada con la dinámica de los dominios terminales enrollados-enrollados.
- La movilidad efectiva de la cadena fue variada en un rango de 500 veces a través de modificaciones en la secuencia de proteínas.
- La desestabilización de los dominios en espiral a través de la mutagenesis aumentó la difusividad de la cadena de la sonda.
- El aumento de la superficie hidrofóbica de los dominios en espiral redujo la movilidad de la sonda.
Conclusiones:
- La movilidad de la cadena en hidrogeles reversibles se puede ajustar con precisión mediante la ingeniería de secuencias de proteínas y dominios de bobina en espiral.
- El modelo de salto de tres estados describe con precisión la migración en cadena, lo que sugiere una unión secuencial asimétrica de dominios terminales.
- La asimetría de enlace es una característica inherente de los geles reversibles, impulsada por cambios entrópicos durante el puente de cadena.
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