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Heterotrimeric G proteins are guanine nucleotide-binding proteins. As the name suggests, heterotrimeric G proteins are composed of three subunits: alpha, beta, and gamma. They remain GDP-bound or GTP-bound inside the cells and switch between inactive/active states. The Gα subunit possesses the nucleotide-binding pocket that binds guanine nucleotides and switches between GDP or GTP-bound states. In contrast, the Gꞵ and Gγ subunits are always bound together with high...
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Engineered B7-H3 Binding in Modular Gp2 Miniproteins.

Abbigael Harthorn1, Hannah K Windsor2, Zachary Schmitz2

  • 1Department of Biomedical Engineering, University of Minnesota - Twin Cities, Minneapolis, MN, USA.

Biotechnology and Bioengineering
|April 30, 2026
PubMed
Summary
This summary is machine-generated.

Researchers engineered small protein ligands targeting B7-H3, a protein overexpressed in many cancers. These high-affinity binders are promising for developing new cancer diagnostics and therapeutics.

Keywords:
B7‐H3Gp2affinity maturationdirected evolutionligandminiproteinstability

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Area of Science:

  • Biochemistry
  • Immunology
  • Oncology

Background:

  • B7-H3 is an immune checkpoint modulator and tumor vasculature biomarker.
  • Overexpression of B7-H3 correlates with tumor growth, metastasis, and poor prognosis.
  • Targeting B7-H3 is crucial for developing novel cancer diagnostics and therapeutics.

Purpose of the Study:

  • To develop high-affinity, specific, and modular ligands for B7-H3.
  • To create tools for molecularly targeted cancer therapies and diagnostics.

Main Methods:

  • A combinatorial library of Gp2 scaffold was created and sorted for B7-H3 binders using yeast surface display.
  • Selected variants were characterized for binding affinity, specificity, and modularity.
  • Directed evolution was employed to enhance ligand potency and stability.

Main Results:

  • Engineered protein ligands achieved single-digit nanomolar affinities for B7-H3.
  • Ligands retained binding affinity after conjugation to an enzyme via a linker.
  • Directed evolution yielded a potent 0.7 nM binder with enhanced stability (67°C midpoint of denaturation).

Conclusions:

  • Small, modular, high-affinity B7-H3 binders were successfully engineered.
  • These ligands are suitable for molecularly targeted therapeutics and diagnostics.
  • The developed ligands offer a promising platform for advancing cancer treatment strategies.