Why are there no clinically-approved drugs targeting disordered proteins?

Intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs) are critical regulators in health and disease but remain underexploited as drug targets. Unlike folded proteins, they populate dynamic ensembles where interactions can be transient or multivalent, and both enthalpic and entropic contributions shape binding, complicating ligand discovery. Here, we analyze three key barriers hindering progress: (1) nontraditional binding mechanisms that challenge classical drug design, (2) experimental and computational limitations for studying disorder, and (3) a lack of systematic datasets. Our analysis of the Biological Magnetic Resonance Data Bank (BMRB) and BindingDB highlights the extreme underrepresentation of IDPs and IDRs, underscoring the need for community-driven data resources. By integrating new binding paradigms, tailored methodologies, and standardized datasets, drug discovery can begin to harness IDPs as a new therapeutic frontier.

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Publication Details

Journal
Current Opinion in Structural Biology
Published
2026-03-02
DOI
https://doi.org/10.1016/j.sbi.2026.103236
Primary Topic
Monoclonal and Polyclonal Antibodies Research
Type
article
Field-Weighted Citation Impact
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article

Why are there no clinically-approved drugs targeting disordered proteins?

Gogulan Karunanithy, Gabriella T. Heller, Thomas Löhr
Current Opinion in Structural Biology
Monoclonal and Polyclonal Antibodies Research
article

Why are there no clinically-approved drugs targeting disordered proteins?

Gogulan Karunanithy, Gabriella T. Heller, Thomas Löhr
article en

Abstract

Intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs) are critical regulators in health and disease but remain underexploited as drug targets. Unlike folded proteins, they populate dynamic ensembles where interactions can be transient or multivalent, and both enthalpic and entropic contributions shape binding, complicating ligand discovery. Here, we analyze three key barriers hindering progress: (1) nontraditional binding mechanisms that challenge classical drug design, (2) experimental and computational limitations for studying disorder, and (3) a lack of systematic datasets. Our analysis of the Biological Magnetic Resonance Data Bank (BMRB) and BindingDB highlights the extreme underrepresentation of IDPs and IDRs, underscoring the need for community-driven data resources. By integrating new binding paradigms, tailored methodologies, and standardized datasets, drug discovery can begin to harness IDPs as a new therapeutic frontier.

Current Opinion in Structural BiologyVol. 97
Plextek (United Kingdom) (GB), Institute of Structural and Molecular Biology (GB), University College London (GB)
Openalex Percentile: Top 39%
Monoclonal and Polyclonal Antibodies Research
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Why are there no clinically-approved drugs targeting disordered proteins? — Gogulan Karunanithy, Gabriella T. Heller, et al. · Current Opinion in Structural Biology (2026) | TGRS Research Map | TGRS