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A Method for Remotely Silencing Neural Activity in Rodents During Discrete Phases of Learning

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Navigating the labyrinth of drugging the disordered.

Simran Tolani¹, Debarghya Mitra¹, Sarath Chandra Dantu²

¹Department of Bioscience and Bioengineering, IIT Bombay, Mumbai, India.

Biophysical Reviews

|June 19, 2026

Summary

Intrinsically disordered proteins (IDPs) and regions (IDRs) are crucial for cellular functions and diseases. Understanding their dynamic interactions is key to developing new therapeutic strategies targeting these flexible molecules.

Keywords:

Energy landscape Ensemble-based drug discovery Intrinsically disordered proteins Intrinsically disordered regions Molecular recognition

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Area of Science:

Biochemistry
Molecular Biology
Structural Biology

Background:

Intrinsically disordered proteins (IDPs) and regions (IDRs) lack stable 3D structures.
They are involved in numerous cellular processes and are implicated in various diseases.
IDPs/IDRs function through dynamic interactions with multiple partners.

Purpose of the Study:

To review the role of protein disorder in health and disease.
To highlight methods for investigating IDP/IDR dynamics and interactions.
To explore the potential of IDPs/IDRs as drug targets.

Main Methods:

Large-scale proteome studies.
Atomic-level investigations.
Analysis of structure-function relationships in disordered proteins.

Main Results:

Protein disorder influences cellular function, dysregulation, and disease.
Dynamic behavior and interactions of IDPs/IDRs are critical for their function.
Flexibility of IDPs/IDRs presents opportunities for drug discovery.

Conclusions:

Understanding IDP/IDR dynamics is essential for therapeutic development.
Targeting intrinsically disordered proteins offers promising avenues for novel treatments.
Further research into IDP/IDR interactions can unlock new therapeutic strategies.