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

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.

Bibliographic Details
Main Authors: Eline Sijbesma, Emira Visser, Kathrin Plitzko, Philipp Thiel, Lech-Gustav Milroy, Markus Kaiser, Luc Brunsveld, Christian Ottmann
Format: Article
Language:English
Published: Nature Publishing Group 2020-08-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-020-17741-0
Description
Summary: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.
ISSN:2041-1723

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