Engineering of affibody molecules for therapy and diagnostics

Joachim Feldwisch, Vladimir Tolmachev

Research output: Chapter in Book/Report/Conference proceedingChapter

56 Citations (Scopus)

Abstract

Affibody molecules are small and robust non-immunoglobulin affinity ligands capable of binding to a wide range of protein targets. They are selected from combinatorial libraries based on a 58 amino acid, three-alpha-helical Z-domain scaffold. They share no sequence or structural homologies to antibodies and in contrast to antibodies they can be functionally produced both by peptide synthesis and by recombinant expression in Escherichia coli. Protein engineering is used to adapt Affibody molecules binding to a target of interest to the specific demands imposed by the intended application. Obviously, the optimal molecule for molecular imaging will be different from the optimal molecule for therapy. Here, we describe general strategies to optimize Affibody molecules for diagnostic imaging and therapy applications.

Original languageEnglish
Title of host publicationTherapeutic Proteins
Subtitle of host publicationMethods and Protocols
EditorsVoynov Vladimir, Caravella Justin
Pages103-126
Number of pages24
DOIs
Publication statusPublished - 2012
Externally publishedYes

Publication series

NameMethods in Molecular Biology
Volume899
ISSN (Print)1064-3745

Keywords

  • ABD, Molecular Imaging
  • Affibody molecules
  • Affinity ligand
  • Albumin-binding domain
  • Biodistribution
  • Chelator
  • Radionuclides
  • Scaffold protein
  • Site-specific modification
  • Targeted therapy

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics

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