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Estabilización de prolina y agua de un mecanismo universal de plegado en dos pasos para la formación de β-turnos en
Nicola Steinke1, Anna Genina2, Richard J Gillams1
1Department of Biochemistry , University of Oxford , Oxford OX1 3QU , U.K.
Journal of the American Chemical Society
|May 29, 2018
Resumen
El plegamiento de proteínas es impulsado por moléculas de agua que atraen sitios específicos de la columna vertebral del péptido en un proceso de dos pasos. Esta hidratación específica del sitio, especialmente con prolina, estabiliza los estados plegados y promueve los giros beta.
Área de la Ciencia:
- La biofísica
- Biología estructural
- Química computacional
Sus antecedentes:
- Los mecanismos de plegamiento de proteínas en soluciones acuosas aún no se comprenden por completo.
- Se debate el papel preciso de las moléculas de agua en la conducción del plegamiento de las proteínas.
- Comprender el plegamiento de proteínas es crucial para la biología molecular y el desarrollo de fármacos.
Objetivo del estudio:
- Para aclarar el mecanismo a escala atómica del plegamiento de proteínas, específicamente la formación de beta-giro.
- Investigar la influencia del residuo de la cadena lateral central en el plegamiento de los péptidos.
- Determinar el papel de las interacciones agua-proteína en la estabilización de los productos intermedios plegables.
Principales métodos:
- Utilizó una combinación de difracción de neutrones y rayos X para obtener información estructural a nivel atómico.
- Empleó avanzadas simulaciones por computadora para modelar el comportamiento de los péptidos.
- Se analizó una serie de péptidos KGXGK con residuos centrales variables (X = P, G, S, L).
Principales resultados:
- Se determinó que la formación de beta-giro en los péptidos KGXGK ocurre a través de una atracción en dos pasos, impulsada por el agua, entre los sitios de la columna vertebral.
- Se identificó la hidratación específica del sitio de la columna vertebral del péptido como un facilitador clave en las primeras etapas de plegamiento.
- Se observó que la prolina en la posición i + 1 mejora la estabilidad de los estados plegados e intermedios.
Conclusiones:
- Propuso un mecanismo donde la hidratación de la columna vertebral específica del sitio inicia el plegamiento de proteínas.
- Se concluyó que las interacciones agua-proteína, particularmente con la prolina, son críticas para estabilizar las estructuras de péptidos.
- Se sugiere que estos hallazgos explican la mayor prevalencia de secuencias que contienen prolina en los giros beta dentro de las proteínas.
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