Targeting protein self-association in drug design.

Thabault, Léopold; Liberelle, Maxime; Frédérick, Raphaël

Type de document :

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

DOI :

10.1016/j.drudis.2021.01.028

PMID :

33548462

URL permanente :

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

Titre :

Targeting protein self-association in drug design.

Auteur(s) :

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

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

Titre de la revue :

Drug Discovery Today

Numéro :

Pagination :

1148-1163

Date de publication :

2023-05-30

ISSN :

1878-5832

Discipline(s) HAL :

Sciences du Vivant [q-bio]

Résumé en anglais : [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 ...
Lire la suite >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.Lire moins >

Langue :

Anglais

Audience :

Internationale

Vulgarisation :

Non

Établissement(s) :

Université de Lille
Inserm
CHU Lille

Collections :

Lille Neurosciences & Cognition (LilNCog) - U 1172

Date de dépôt :

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

Numéro de version	Lien	Date de modification
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

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Targeting protein self-association in drug design.

BibTeX

CSV

Excel

RIS