Document type
Doctoral thesisVersion
Published versionPublication date
All rights reserved
Please use this identifier to cite or link to this item: https://hdl.handle.net/2445/196480
Targeting the disordered N-terminal domain of androgen receptor. Novel inhibitors tackling biomolecular condensation to treat late stage prostate cancer
Journal Title
Authors
Director/Tutor
Journal ISSN
Volume Title
Related resource
Abstract
[eng] Drug discovery is the process by which new drugs are found and developed into the market. Given the scope of this thesis, the term “drug” will refer to small molecules and the term “target” to proteins, otherwise noted.
Currently, most drug discovery strategies rely on the resolved three-dimensional structure of the target. Structure-based drug discovery (SBDD) is advantageous as it accelerates and lowers the cost of the drug discovery process. However, the essential requisite for SBDD, the prior knowledge of the target protein structure, has narrowed the types of proteins in drug discovery programs to globular proteins.
It is estimated that 33-50% of our proteome is intrinsically disordered. Intrinsically disordered proteins (IDPs) and protein regions (IDRs) do not spontaneously fold into a stable secondary and tertiary structure in their native state yet are functionally active. IDPs have long been considered undruggable as their lack of a stable tertiary structure impedes the application of SBDD. Nevertheless, IDPs participate in many physiological processes, as well as in diseases. Hence finding new approaches to target IDPs is crucial to expand the druggable proteome and fill unmet needs across diseases in which disorder plays a role.
Subject (English)
Citation
Collections
Citation
FRIGOLÉ VIVAS, Marta. Targeting the disordered N-terminal domain of androgen receptor. Novel inhibitors tackling biomolecular condensation to treat late stage prostate cancer. [consulted: 8 of June of 2026]. Available at: https://hdl.handle.net/2445/196480