Academic Journal
Targeting protein self-association in drug design.
| العنوان: | Targeting protein self-association in drug design. |
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| المؤلفون: | Thabault, Léopold, Liberelle, Maxime, Frédérick, Raphaël |
| المساهمون: | UCL - SSS/LDRI - Louvain Drug Research Institute |
| المصدر: | Drug Discovery Today, Vol. 26, no. 5, p. 1148-1163 (2021) |
| بيانات النشر: | Elsevier Ltd. * Trends Journals |
| سنة النشر: | 2021 |
| المجموعة: | DIAL@USL-B (Université Saint-Louis, Bruxelles) |
| مصطلحات موضوعية: | Self-association, Protein-protein association |
| الوصف: | 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, subunits intercalation or by promoting inactive oligomeric states. Targeting self-interaction grants several advantages over active site inhibition thanks to the stimulation of protein degradation, the enhancement of selectivity, a sub-stoichiometric inhibition and a 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 DSF, native MS, FRET spectroscopy, two-dimensional NMR and X-ray crystallography. The present review covers the different aspects of this new paradigm in drug design. |
| نوع الوثيقة: | article in journal/newspaper |
| اللغة: | English |
| تدمد: | 1359-6446 1878-5832 |
| Relation: | boreal:245989; http://hdl.handle.net/2078.1/245989; urn:ISSN:1359-6446; urn:EISSN:1878-5832 |
| DOI: | 10.1016/j.drudis.2021.01.028 |
| الاتاحة: | http://hdl.handle.net/2078.1/245989 https://doi.org/10.1016/j.drudis.2021.01.028 |
| Rights: | info:eu-repo/semantics/openAccess |
| رقم الانضمام: | edsbas.33B635CF |
| قاعدة البيانات: | BASE |
| تدمد: | 13596446 18785832 |
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| DOI: | 10.1016/j.drudis.2021.01.028 |