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Engineering Single-Chain Antibody Fragment (scFv) Variants Targeting A Disintegrin and Metalloproteinase-17

Masoud Kalantar1, Elham Khorasani Buxton2, Korey M Reid3

  • 1Department of Chemical and Materials Engineering, University of Nevada, Reno, NV 89557, USA.

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Researchers engineered high-affinity single-chain antibodies targeting ADAM-17, a metalloproteinase involved in diseases. This work provides a framework for developing selective antibody therapeutics against metalloproteinases.

Keywords:
ADAM-17antibody engineeringdirected evolutionengineering protease inhibitorsmetalloproteinasesingle-chain variable fragment (scFv)yeast surface display

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Area of Science:

  • Biochemistry
  • Immunology
  • Molecular Biology

Background:

  • Metalloproteinases (MPs), including ADAM-17 (also known as TNF-α-converting enzyme or TACE), are zinc-dependent enzymes implicated in various diseases.
  • ADAM-17 dysregulation is linked to inflammatory diseases, cancer progression, and immune modulation.
  • Current small-molecule inhibitors for MPs face challenges with off-target effects and stability, while antibody approaches require enhanced selectivity.

Purpose of the Study:

  • To engineer single-chain variable fragment (scFv) antibodies with improved binding affinity and selectivity for ADAM-17.
  • To identify key structural determinants, particularly in the complementarity-determining region 3 of the heavy chain (CDR-H3), that enhance MP targeting.
  • To establish a framework for designing novel antibody-based scaffolds for therapeutic applications against ADAM-17 and other MPs.

Main Methods:

  • Yeast surface display (YSD) and fluorescence-activated cell sorting (FACS) were employed to select and engineer scFv antibodies.
  • Next-generation sequencing (NGS) was utilized to identify critical amino acid residues responsible for high-affinity binding to ADAM-17.
  • Structural analysis focused on optimizing CDR-H3 conformations for enhanced target engagement.

Main Results:

  • Engineered scFv antibodies demonstrated optimized CDR-H3 conformations, leading to enhanced binding affinity for ADAM-17.
  • NGS identified specific residues crucial for high-affinity interactions, providing insights into the molecular basis of MP targeting.
  • The study successfully developed a method for creating selective antibody fragments against metalloproteinases.

Conclusions:

  • The findings provide a robust framework for designing highly selective monoclonal antibodies against ADAM-17 and other MPs.
  • This approach enables the development of novel antibody-based designer scaffolds with potential therapeutic applications.
  • Optimizing antibody structure, particularly CDR-H3, is key to achieving high affinity and selectivity for targeted metalloproteinase inhibition.