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Related Concept Videos

Eukaryotic Transcription Inhibitors01:52

Eukaryotic Transcription Inhibitors

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Certain biochemical processes, such as embryonic development and cell growth regulation, depend on the repression of specific genes. DNA binding proteins known as eukaryotic transcription inhibitors regulate the repression of gene expression in eukaryotes. The presence of these inhibitors at the required location and time in the cell is triggered by the presence of hormones and additional signals from other cells.
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When T cells with CD4 markers are activated, they give rise to two types of effector cells: helper T cells and regulatory T cells. Meanwhile, T cells with CD8 markers differentiate into effector cytotoxic T cells. The differentiation of CD4 T cells into helper T cell subsets, such as Th1, Th2, and Th17 cells, is dependent on the antigen type, antigen-presenting cell, and regulatory cytokines.
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Related Experiment Video

Updated: Jan 11, 2026

Isolation and Th17 Differentiation of Naïve CD4 T Lymphocytes
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A Novel Small Molecule Allosteric Inhibitor of IL-17A from a DNA-Encoded Library.

Marcos E Milla1, Jonathan M Blevitt1, Steven D Goldberg1

  • 1Johnson & Johnson Innovative Medicine, 3210 Merryfield Row, La Jolla, California 92121, United States.

ACS Medicinal Chemistry Letters
|November 19, 2025
PubMed
Summary

Researchers discovered novel inhibitors of Interleukin-17A (IL-17A) signaling using DNA-encoded library technology. The lead compound allosterically disrupts IL-17A structure, blocking receptor binding and potent inhibition of inflammatory pathways.

Keywords:
DELDNA-encoded chemical libraryIL-17allosteric inhibitorprotein−protein interactions

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Area of Science:

  • Immunology
  • Medicinal Chemistry
  • Drug Discovery

Background:

  • Interleukin-17A (IL-17A) is a pro-inflammatory cytokine implicated in various autoimmune diseases.
  • Targeting the IL-17A pathway is a validated therapeutic strategy for inflammatory conditions.
  • Novel inhibitors are needed to effectively modulate IL-17A signaling.

Purpose of the Study:

  • To discover novel inhibitors of the IL-17A-receptor interaction.
  • To characterize the mechanism of action of these novel inhibitors.
  • To evaluate the potency of these inhibitors in relevant cellular models.

Main Methods:

  • DNA-encoded library (DEL) technology was employed for high-throughput screening.
  • Biochemical assays were used to assess the binding and inhibitory activity of compounds.
  • Structural analysis was performed to understand the mechanism of inhibition.
  • Inhibition of IL-17A signaling was evaluated in human primary cells.

Main Results:

  • A novel series of IL-17A inhibitors was identified using DEL technology.
  • The lead compound, JNJ627 (Compound 1), binds to the IL-17A homodimer interface.
  • Inhibition occurs via allosteric disruption of the IL-17A quaternary structure, preventing receptor binding.
  • Compounds exhibit slow on-rate kinetics and potent inhibition of IL-17A signaling in primary cells.

Conclusions:

  • Novel allosteric inhibitors of IL-17A have been discovered.
  • These inhibitors represent a new mechanism for targeting IL-17A signaling.
  • The identified compounds show potential for therapeutic development in IL-17A-mediated diseases.