Article Dans Une Revue (Article De Synthèse) Drug Discovery Today Année : 2023

Targeting protein self-association in drug design.

Résumé

Protein self-association is a universal phenomenon essential for stability and molecular recognition. Disrupting constitutive homomers constitutes an original and emerging strategy in drug design. Inhibition of homomeric proteins can be achieved through direct complex disruption, subunit intercalation, or by promoting inactive oligomeric states. Targeting self-interaction grants several advantages over active site inhibition because of the stimulation of protein degradation, the enhancement of selectivity, substoichiometric inhibition, and by-pass of compensatory mechanisms. This new landscape in protein inhibition is driven by the development of biophysical and biochemical tools suited for the study of homomeric proteins, such as differential scanning fluorimetry (DSF), native mass spectrometry (MS), Förster resonance energy transfer (FRET) spectroscopy, 2D nuclear magnetic resonance (NMR), and X-ray crystallography. In this review, we discuss the different aspects of this new paradigm in drug design.
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Dates et versions

hal-04829320 , version 1 (10-12-2024)

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Léopold Thabault, Maxime Liberelle, Raphaël Frédérick. Targeting protein self-association in drug design.. Drug Discovery Today, 2023, Drug Discovery Today, 26, pp.1148-1163. ⟨10.1016/j.drudis.2021.01.028⟩. ⟨hal-04829320⟩

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