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Continuous microfluidic assortment of interactive ligands (CMAIL).

Yi-Hsing Hsiao1,2, Chao-Yang Huang3, Chih-Yung Hu3

  • 1Institute of Nanoengineering and Microsystems, National Tsing Hua University, Hsinchu 30013, Taiwan.

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|September 1, 2016
PubMed
Summary

We developed a new method, continuous microfluidic assortment of interactive ligands (CMAIL), to rapidly screen for antibody fragments. CMAIL efficiently isolates antigen-binding phages from large libraries in minutes, improving antibody discovery.

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Area of Science:

  • Biotechnology
  • Molecular Biology
  • Biophysics

Background:

  • Identifying ligand-receptor interactions is vital for applications like monoclonal antibody development.
  • Traditional biopanning methods for affinity screening are time-consuming and labor-intensive due to extensive washing steps.

Purpose of the Study:

  • To introduce a novel microfluidic technique, continuous microfluidic assortment of interactive ligands (CMAIL), for efficient screening and sorting of antigen-binding antibody fragments.
  • To demonstrate CMAIL's capability in isolating specific phage-displayed antibody fragments with high affinity.

Main Methods:

  • Phages displaying single-chain variable antibody fragments (scFv) were subjected to electrophoresis through an antigen-functionalized hydrogel matrix.
  • Two alternating orthogonal electric fields were applied: a weak horizontal field for differential lateral sweeping based on antigen affinity and a strong vertical field for downward electrophoresis.
  • Spatial separation of phages based on affinity was achieved, enabling continuous sorting.

Main Results:

  • CMAIL successfully isolated over 10^5 colony-forming unit (CFU) antigen-interacting phages with approximately 100% specificity.
  • The method screened a phage library of 3x10^9 members within 40 minutes.
  • The process demonstrated high speed, sensitivity, and specificity without requiring washing, elution, or magnetic beads.

Conclusions:

  • Continuous microfluidic assortment of interactive ligands (CMAIL) offers an efficient, rapid, and cost-effective alternative to traditional biopanning.
  • This method significantly accelerates the isolation and sorting of affinity reagents, particularly those involving phage display.
  • CMAIL enhances the process of discovering and developing antibody-based therapeutics and diagnostics.