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Cucurbit[8]uril se une a los sitios no terminales del dipeptido con alta afinidad e induce un tipo II β-Turn

Paolo Suating¹, Lauren B Kimberly¹, Marc B Ewe¹

¹Department of Chemistry, Trinity University, 1 Trinity Place, San Antonio, Texas 78212, United States.

Journal of the American Chemical Society

|February 13, 2024

Resumen

El receptor sintético cucurbit[8]uril (Q8) se une efectivamente a los sitios de péptido no terminales con alta afinidad. Este descubrimiento avanza las aplicaciones de plegado de péptidos mediante la comprensión del reconocimiento molecular y las interacciones de unión.

Área de la Ciencia:

Química supramolecular
Biología Química
Biología estructural

Sus antecedentes:

Apuntar a sitios no terminales en polipéptidos es un desafío.
Los receptores sintéticos ofrecen nuevos enfoques para el reconocimiento de péptidos.

Objetivo del estudio:

Para examinar y caracterizar el receptor sintético cucurbit[8]uril (Q8) que se une a los sitios no terminales del dipeptido.
Para dilucidar la base molecular de las interacciones del péptido Q8.

Principales métodos:

La selección de una biblioteca de tetrapeptidos.
Calorimetría por titulación isotérmica (ITC).
Espectroscopia de resonancia magnética nuclear (RMN).
Espectrometría de masas (EM).
La cristalografía de rayos X.

Principales resultados:

Q8 demostró una alta afinidad por los sitios dipeptídicos no terminales Lys-Phe (KF) y Phe-Lys (FK) con constantes de disociación de 60 y 86 nm, respectivamente.
La cristalografía de rayos X reveló un motivo de inclusión de pares que involucra a las cadenas laterales Leu y Tyr.
El reconocimiento implica enlaces de hidrógeno y giros β de tipo II inducidos por Q8.

Conclusiones:

Q8 exhibe una afinidad sin precedentes para los sitios no terminales no modificados del péptido.
Los conocimientos estructurales detallados facilitan el diseño de aplicaciones basadas en péptidos.
Este sistema permite estrategias de plegamiento de polipéptidos inducidos por ligandos.

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