Structure-based evolution of a promiscuous inhibitor to a selective stabilizer of protein–protein interactions

Small molecule stabilizers of protein–protein interactions hold great therapeutic potential. Based on virtual screening and molecular docking, the authors here develop a strategy to evolve weak, promiscuous inhibitors of 14-3-3 interactions into selective stabilizers of the 14-3-3/ChREBP complex.

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Detalles Bibliográficos
Autores principales: Eline Sijbesma, Emira Visser, Kathrin Plitzko, Philipp Thiel, Lech-Gustav Milroy, Markus Kaiser, Luc Brunsveld, Christian Ottmann
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2020
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Acceso en línea:https://doaj.org/article/8ff8fc48608f42e5b0be3c2e5c15b283
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Sumario:Small molecule stabilizers of protein–protein interactions hold great therapeutic potential. Based on virtual screening and molecular docking, the authors here develop a strategy to evolve weak, promiscuous inhibitors of 14-3-3 interactions into selective stabilizers of the 14-3-3/ChREBP complex.