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Chemically Engineered Affinity Protein Drugs for Covalent Targeted Cancer Therapy.

Xuelin Xia1, Wenhui Gao1, Xiaoyuan Yang1

  • 1School of Chemistry and Chemical Engineering, Frontiers Science Center for Transformative Molecules, Shanghai Jiao Tong University, Shanghai 200240, People's Republic of China.

Journal of the American Chemical Society
|May 30, 2025
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Summary
This summary is machine-generated.

This study introduces a new method to create covalent affinity protein drugs that bind irreversibly to tumors. This approach improves tumor targeting and drug efficacy, offering a promising solution for cancer therapy.

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Area of Science:

  • Biochemistry
  • Chemical Biology
  • Oncology

Background:

  • Affinity proteins show promise for tumor targeting but face challenges with rapid clearance and tumor accumulation due to their small size.
  • Covalent targeting offers a solution by creating irreversible binding, decoupling drug effects from pharmacokinetics.

Purpose of the Study:

  • To develop a chemical modification strategy for creating covalently targeted affinity protein drugs.
  • To demonstrate the efficacy of this strategy using affibody and monobody protein drugs.

Main Methods:

  • Engineered affinity proteins with a sulfur(VI) fluoride exchange (SuFEx) chemistry-based maleimide-substituted aryl fluorosulfate (MFS) linker.
  • Tested covalent binding, cell uptake, tumor retention, and tumor growth inhibition in vitro and in mouse models.

Main Results:

  • MFS-modified affibody achieved over 72% covalent binding to HER2 and 185% higher cell uptake in vitro.
  • Covalent affibody showed 2.01 times greater tumor retention and nearly complete tumor growth inhibition in mice.
  • Similar efficacy was observed for MFS-linker-armed monobody targeting EGFR.

Conclusions:

  • A facile chemical modification strategy enables the creation of covalently targeted affinity protein drugs.
  • This approach provides a general platform for protein therapeutics, potentially accelerating applications in diverse diseases.