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Related Experiment Video

Updated: May 8, 2026

Procedures for Identifying Infectious Prions After Passage Through the Digestive System of an Avian Species
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Procedures for Identifying Infectious Prions After Passage Through the Digestive System of an Avian Species

Published on: November 6, 2013

New engineered antibodies against prions.

Nives Škrlj1, Marko Dolinar1

  • 1Chair of Biochemistry; Faculty of Chemistry and Chemical Technology; University of Ljubljana; Ljubljana, Slovenia.

Bioengineered
|August 15, 2013
PubMed
Summary

Researchers developed a novel antibody construct using a cell-penetrating peptide linker. This innovation enhances antibody transport across the blood-brain barrier for targeted brain therapies.

Keywords:
Creutzfeldt-Jakob disease (CJD)blood-brain barriercell-penetrating peptidesprion proteinsingle chain antibody fragment (scFv)

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Area of Science:

  • Biotechnology
  • Neuroscience
  • Immunology

Background:

  • Antibody therapy shows promise for treating diseases.
  • Developing therapeutics targeting the central nervous system is challenging due to the blood-brain barrier (BBB).
  • Efficient delivery of antibodies, including engineered single-chain variants, into brain tissue remains a significant hurdle.

Purpose of the Study:

  • To engineer antibody-based therapeutics for improved brain tissue penetration.
  • To overcome the limitations of the blood-brain barrier for antibody delivery.
  • To develop novel antibody constructs for targeting brain antigens, such as the pathogenic prion protein.

Main Methods:

  • Development of a novel antibody construct utilizing a cell-penetrating peptide (CPP) as a linker.
  • The CPP linker connects specificity-determining domains of the antibody peptide, replacing traditional flexible linkers (e.g., Gly4Ser repeats).
  • Intravenous injection of the prion-specific antibody construct into murine models to assess brain tissue transport.

Main Results:

  • Demonstrated efficient transport of the specific prion-specific antibody construct into brain tissue following intravenous administration.
  • The novel CPP linker facilitated antibody transport, bypassing the limitations typically imposed by the blood-brain barrier.
  • Eliminated the need for standard flexible linkers in the antibody construct.

Conclusions:

  • The developed antibody construct effectively crosses the blood-brain barrier.
  • The use of a cell-penetrating peptide linker represents a significant advancement in bioengineering antibody therapeutics for brain targeting.
  • This approach paves the way for improved antibody variants designed to target antigens within the brain.