Targeting protein self-association in drug design.

Thabault, Léopold; Liberelle, Maxime; Frédérick, Raphaël

Document type :

Article dans une revue scientifique: Article de synthèse/Review paper

DOI :

10.1016/j.drudis.2021.01.028

PMID :

33548462

Permalink :

http://hdl.handle.net/20.500.12210/102102

Title :

Targeting protein self-association in drug design.

Author(s) :

Thabault, Léopold [Auteur]
Liberelle, Maxime [Auteur]

Lille Neurosciences & Cognition (LilNCog) - U 1172
Frédérick, Raphaël [Auteur]

Journal title :

Drug Discovery Today

Volume number :

Pages :

1148-1163

Publication date :

2023-05-30

ISSN :

1878-5832

HAL domain(s) :

Sciences du Vivant [q-bio]

English abstract : [en]

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 ...
Show more >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.Show less >

Language :

Anglais

Audience :

Internationale

Popular science :

Non

Administrative institution(s) :

Université de Lille
Inserm
CHU Lille

Collections :

Lille Neurosciences & Cognition (LilNCog) - U 1172

Submission date :

2024-01-16T02:19:45Z
2024-12-10T13:47:42Z

Version	Link	Modification date
2	20.500.12210/102102*	2024-12-10T13:44:59Z
1	20.500.12210/102102.1	2024-01-16T02:19:45Z

Targeting protein self-association in drug design.

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Targeting protein self-association in drug design.

BibTeX

CSV

Excel

RIS