Cited by 656Monoclonal and Polyclonal Antibodies ResearchBiochemical and Structural CharacterizationChemical Synthesis and Analysis

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High-affinity binders selected from designed ankyrin repeat protein libraries

Binz, H Kaspar, Amstutz, Patrick, Kohl, Andreas, Stumpp, Michael T, Briand, Christophe, Forrer, Patrik, Grütter, Markus G, Plückthun, Andreas·2004·Nature Biotechnology

DOI 10.1038/nbt962

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Abstract

We report here the evolution of ankyrin repeat (AR) proteins in vitro for specific, high-affinity target binding. Using a consensus design strategy, we generated combinatorial libraries of AR proteins of varying repeat numbers with diversified binding surfaces. Libraries of two and three repeats, flanked by 'capping repeats,' were used in ribosome-display selections against maltose binding protein (MBP) and two eukaryotic kinases. We rapidly enriched target-specific binders with affinities in the low nanomolar range and determined the crystal structure of one of the selected AR proteins in complex with MBP at 2.3 A resolution. The interaction relies on the randomized positions of the designed AR protein and is comparable to natural, heterodimeric protein-protein interactions. Thus, our AR protein libraries are valuable sources for binding molecules and, because of the very favorable biophysical properties of the designed AR proteins, an attractive alternative to antibody libraries.

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Authors: Binz, H. K., Amstutz, P., Kohl, A., Stumpp, M. T., Briand, C., Forrer, P., Grütter, M. G., & Plückthun, A.
Affiliations: University of Zurich (CH)
Corresponding author: Grütter, Markus G
Plückthun, Andreas
ORCID: Stumpp, Michael T
Briand, Christophe
Forrer, Patrik
Plückthun, Andreas
Venue: Nature Biotechnology
Publisher: Springer Science and Business Media LLC
Published: 2004-04-18
Volume: 22
Issue: 5
Pages: 575-582
ISSN: 0733-222X (ISSN-L)
1087-0156
1546-1696
DOI: 10.1038/nbt962
OpenAlex: W2084938664
Cited by: 656
References: 51
Citations by year: 2026: 7 · 2025: 22 · 2024: 17 · 2023: 26 · 2022: 27 · 2021: 23 · 2020: 31 · 2019: 24 · 2018: 22 · 2017: 38 · 2016: 28 · 2015: 36 · 2014: 33 · 2013: 33 · 2012: 35
FWCI: 30.73
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature Biotechnology (publishedVersion)
PubMed (publishedVersion)
Funders: Bundesministerium für Bildung und Forschung
National Center of Competence in Research Chemical Biology
Topics: Life Sciences › Immunology and Microbiology › Immunology › Monoclonal and Polyclonal Antibodies Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
Physical Sciences › Chemistry › Organic Chemistry › Chemical Synthesis and Analysis
Keywords: ankyrin repeat proteins, combinatorial protein libraries, ribosome display, protein-protein interaction, maltose-binding protein, high-affinity binders, consensus design, protein crystal structure
MeSH terms: Amino Acid Sequence, Enzyme-Linked Immunosorbent Assay, Molecular Sequence Data, Protein Conformation, Ankyrin Repeat

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High-affinity binders selected from designed ankyrin repeat protein libraries

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