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Small p53 derived peptide suitable for robust nanobodies dimerization.

Frank Dietsch1, Yves Nominé2, Audrey Stoessel1

  • 1Université de Strasbourg, UMR7242 Biotechnologie et Signalisation Cellulaire, Ecole Supérieure de Biotechnologie Strasbourg, F-67412 Illkirch, France.

Journal of Immunological Methods
|September 5, 2021
PubMed
Summary
This summary is machine-generated.

A novel E3 peptide enables nanobody dimerization, enhancing functional affinity. This dimeric format, particularly the nano-eGFP-E3 construct, shows superior cell-based specificity over tandem formats.

Keywords:
AvidityBivalencyDimerization domainPeptideV(H)Hsp53

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Area of Science:

  • Biotechnology
  • Molecular Biology
  • Protein Engineering

Background:

  • Bivalent variable heavy domains (VHHs) exhibit enhanced functional affinity over monovalent versions.
  • Dimerization strategies include hinge insertion or dimerization modules.
  • A p53-derived self-associating E3 peptide was explored for nanobody dimerization.

Purpose of the Study:

  • To develop and evaluate the E3 peptide as a tool for creating dimeric nanobodies.
  • To compare the performance of an E3-dimerized anti-eGFP nanobody (nano-eGFP-E3) against a tandem anti-eGFP nanobody.
  • To assess the benefits of bivalency in terms of avidity and specificity.

Main Methods:

  • Construction of nano-eGFP-E3 using the E3 peptide for dimerization.
  • Construction of a tandem anti-eGFP nanobody using a GS-rich linker.
  • Comparative analysis using ELISA, Surface Plasmon Resonance (SPR), and cell-based assays.

Main Results:

  • Both dimeric and tandem formats showed comparable avidity gains in vitro (ELISA, SPR) versus monovalent nanobodies.
  • The nano-eGFP-E3 construct demonstrated superior cell-based specificity, achieving a higher signal-to-noise ratio than the tandem format.
  • The E3 peptide proved effective for constructing dimeric antibody fragments.

Conclusions:

  • The E3 peptide is a versatile tool for creating dimeric biomolecules, including antibody fragments.
  • Dimerization via the E3 peptide enhances functional affinity and cell-based specificity.
  • This approach offers an improved strategy for developing high-affinity antibody fragments.