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Related Experiment Video

Updated: May 14, 2026

Construction of Synthetic Phage Displayed Fab Library with Tailored Diversity
12:31

Construction of Synthetic Phage Displayed Fab Library with Tailored Diversity

Published on: May 1, 2018

Anti-digoxin Fab variants generated by phage display.

Viviane Midori Murata1, Mariana Costa Braga Schmidt, Jorge Kalil

  • 1Laboratorio de Biofarmacos em Celulas Animais, Instituto Butantan, São Paulo, Brazil.

Molecular Biotechnology
|January 30, 2013
PubMed
Summary
This summary is machine-generated.

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Researchers developed a high-affinity monoclonal antibody for digoxin toxicity. This new antibody offers a more precise and potent option for digoxin detoxification compared to existing treatments.

Area of Science:

  • Biotechnology
  • Immunology
  • Pharmacology

Background:

  • Digoxin is crucial for cardiac dysfunction but has a narrow therapeutic window.
  • Existing polyclonal Fab fragments for digoxin toxicity have limitations.
  • Monoclonal antibodies offer potential for more precise digoxin detoxification.

Purpose of the Study:

  • To develop a high-affinity monoclonal anti-digoxin antibody using phage display technology.
  • To create a more specific and precisely dosed product for digoxin detoxification.
  • To improve upon existing treatments for digoxin toxicity.

Main Methods:

  • Phage display technology was employed to select high-affinity antibody variants.
  • cDNA synthesis from an anti-digoxin hybridoma followed by LC and Fd amplification.

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Last Updated: May 14, 2026

Construction of Synthetic Phage Displayed Fab Library with Tailored Diversity
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Construction of Synthetic Phage Displayed Fab Library with Tailored Diversity

Published on: May 1, 2018

Scalable High Throughput Selection From Phage-displayed Synthetic Antibody Libraries
12:55

Scalable High Throughput Selection From Phage-displayed Synthetic Antibody Libraries

Published on: January 17, 2015

Using Phage Display to Develop Ubiquitin Variant Modulators for E3 Ligases
06:30

Using Phage Display to Develop Ubiquitin Variant Modulators for E3 Ligases

Published on: August 27, 2021

  • Combinatorial Fab library construction in a phagemid vector (pComb3X).
  • Selection and characterization of clones using ELISA, Western blotting, and Biacore analysis.

    • Main Results:

    • Ten clones were screened, with six showing positive expression of anti-digoxin product.
    • Four clones with framework1 variations demonstrated specific binding to digoxin-BSA.
    • Biacore analysis confirmed specific binding and allowed for clone ranking.
    • Selected variants exhibited higher affinity than the original antibody.

    Conclusions:

    • High-affinity monoclonal anti-digoxin antibody variants were successfully developed.
    • These variants show promise for enhanced specificity and potency in digoxin detoxification.
    • The study provides a foundation for a superior therapeutic agent for digoxin toxicity.