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Related Concept Videos

Hybridoma Technology01:31

Hybridoma Technology

Hybridoma technology is used for the large-scale production of monoclonal antibodies. Monoclonal antibodies bind to only a single antigenic determinant or epitope. Such antibodies are used in research, diagnostics, and disease therapy. The hybridoma technology established in 1975 by Georges Köhler and Cesar Milstein was awarded the Nobel Prize in Medicine in 1984 for revolutionizing research and therapy.
Hybridoma Selection
Commonly used fusion techniques — electroporation, polyethylene glycol...

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Related Experiment Video

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Scalable High Throughput Selection From Phage-displayed Synthetic Antibody Libraries
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Scalable High Throughput Selection From Phage-displayed Synthetic Antibody Libraries

Published on: January 17, 2015

Synthetic single-framework antibody library integrated with rapid affinity maturation by VL shuffling.

E-C Brockmann1, S Akter, T Savukoski

  • 1Department of Biotechnology, University of Turku, Turku, Finland. eechbr@utu.fi

Protein Engineering, Design & Selection : PEDS
|June 18, 2011
PubMed
Summary

This study developed a rapid antibody affinity maturation method using a synthetic human antibody library. The new approach significantly improved antibody binding affinities against lysozyme, achieving low nanomolar ranges.

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Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library

Published on: January 14, 2020

Area of Science:

  • Immunotechnology
  • Molecular Biology
  • Biochemistry

Background:

  • Antibody affinity maturation is crucial for enhancing antibody properties from in vitro libraries.
  • Existing methods can be limited in diversity and efficiency.

Purpose of the Study:

  • To develop a rapid affinity maturation strategy for antibodies using a synthetic human scFv library.
  • To improve antibody binding affinities against lysozyme.

Main Methods:

  • Constructed a synthetic human scFv antibody library in a single framework for rapid affinity maturation.
  • Employed updated Kunkel's mutagenesis to generate diversity, focusing on V(H) domains.
  • Utilized phage display and panning techniques for library selection and enrichment.
  • Incorporated enriched V(H) genes into a mature library for further V(L) domain variant selection.

Main Results:

  • Generated a phage-displayed library with 3 × 10(10) unique members, emphasizing V(H) diversity.
  • Identified several unique anti-lysozyme antibodies with dissociation constants (K(d)) between 0.8-10 nM after affinity maturation.
  • Achieved significantly higher binding affinities compared to antibodies selected from the primary universal library (K(d) <20 nM).

Conclusions:

  • The single-framework strategy enables efficient transfer of V(H) domain diversity for antibody affinity maturation.
  • This method leads to a diverse set of antibodies with high binding affinities in the low nanomolar range.
  • The approach offers a streamlined process for generating potent antibodies without complex ligation steps.