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Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

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Los péptidos helicoidales de fase gaseosa imitan el comportamiento de la fase de solución.

Lindsay J Morrison¹, Vicki H Wysocki

¹Ohio State University , 484 West 12th Avenue, Columbus, Ohio 43210, United States.

Journal of the American Chemical Society

|September 10, 2014

Resumen

Este resumen es generado por máquina.

Los estudios de péptidos en fase gaseosa revelan la estabilización de la hélice alfa en los terminales. Se analizaron las conformaciones helicoidales y globulares de péptidos doblemente cargados, mostrando la estabilidad de la secuencia y la influencia de la longitud.

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Área de la Ciencia:

Química biofísica y bioquímica.
Espectrometría de masas por espectrometría de masas.
La conformación de las proteínas.

Sus antecedentes:

Las hélices alfa en solución son estabilizadas por las interacciones de cierre terminal.
Los estudios de la fase gaseosa ofrecen información sobre las propiedades estabilizadoras intrínsecas.
Estudios previos en la fase de solución examinaron los efectos de los aminoácidos N-terminales.

Objetivo del estudio:

Para investigar las conformaciones helicoidales y globulares de péptidos en fase gaseosa.
Para explorar la influencia de la secuencia y longitud del péptido en la estabilidad helicoidal.
Para analizar las preferencias conformacionales de los fragmentos de péptidos.

Principales métodos:

Análisis de péptidos de doble carga en fase gaseosa (XAnK).
Espectrometría de masas para estudiar las conformaciones y fragmentación de péptidos.
Variación de las energías de colisión para inducir cambios conformacionales.

Principales resultados:

Conformaciones helicoidales y globulares observadas en péptidos en fase gaseosa.
La abundancia de la conformación helicoidal depende de la longitud del péptido y el residuo N-terminal (X).
Los fragmentos helicoidales de iones b se forman preferentemente a energías de colisión más bajas, especialmente de precursores helicoidales.

Conclusiones:

Los estudios de péptidos en fase gaseosa confirman las observaciones en la fase de solución sobre la estabilización helicoidal.
La estabilidad del fragmento está influenciada por la longitud, el residuo N-terminal, la conformación del precursor y la energía de colisión.
Se requiere una longitud mínima de fragmento (b10) para las conformaciones helicoidales estables en b-iones.