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Related Experiment Video

Updated: Jul 3, 2026

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

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

Published on: January 14, 2020

Combinatorial surrobody libraries.

Li Xu¹, Helena Yee, Christina Chan

¹Sea Lane Biotechnologies, 1455 Adams Drive, Suite 2060, Menlo Park, CA 94025, USA.

Proceedings of the National Academy of Sciences of the United States of America

|July 31, 2008

Summary

This summary is machine-generated.

Researchers developed novel "surrobodies" using the pre-B cell receptor (pre-BCR) structure. These engineered proteins exhibit high antigen-binding affinity, offering a new class of antibody alternatives.

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Last Updated: Jul 3, 2026

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

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Published on: January 14, 2020

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Published on: January 17, 2015

Combinatorial Synthesis of and High-throughput Protein Release from Polymer Film and Nanoparticle Libraries

Combinatorial Synthesis of and High-throughput Protein Release from Polymer Film and Nanoparticle Libraries

Published on: September 6, 2012

Area of Science:

Biochemistry
Immunology
Protein Engineering

Background:

The pre-B cell receptor (pre-BCR) is crucial for antibody repertoire development.
Pre-BCR structure differs from canonical antibodies, featuring a trimer of a heavy chain and two surrogate light chains (SLC).

Purpose of the Study:

To construct novel combinatorial protein libraries based on the pre-BCR structure.
To explore the potential of pre-BCR-based proteins as antigen-binding molecules.

Main Methods:

Engineered combinatorial libraries by pairing diverse heavy chains with a fixed SLC.
Expressed these libraries in mammalian, Escherichia coli, and phagemid systems.

Main Results:

Identified members within the libraries exhibiting nanomolar affinity for specific antigens.
Demonstrated the feasibility of generating antigen-binding proteins from pre-BCR scaffolds.

Conclusions:

Introduced a new class of antigen-binding proteins termed "surrobodies".
Surrobodies represent a distinct alternative to canonical antibodies for therapeutic and diagnostic applications.