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High-affinity binders selected from designed ankyrin repeat protein libraries
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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“These POI-targeting polypeptides can either be single chain antibodies (e.g. variable domains from camelid or shark-derived heavy chain only antibodies, nanobodies), or a variety of synthetic polypeptide scaffolds that bind POIs such as fibronectin type III domain-based monobodies [110, 111], designed ankyrin repeats (DARPINs) [112, 113], cystatin-derived affimers [114] or Affibodies derived from”
From Advances in targeted degradation of endogenous proteins (2019) · cites this paper as [113]
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1 retracted
Fluorobodies combine GFP fluorescence with the binding characteristics of antibodies
Zeytun, A., Jeromin, A., Scalettar, B. A., Waldo, G. S., & Bradbury, A. M. (2003) · Nature Biotechnology · doi:10.1038/nbt911 · Cited by 31
RetractedMolecular Cloning: A Laboratory Manual
Sambrook, J., Fritsch, E., & Maniatis, T. (1989) · UCLA - Biblioteca de Ciencias de la Salud · Cited by 133,589
Molecular cloning: A laboratory manual
Deininger, P. L. (1990) · Analytical Biochemistry · doi:10.1016/0003-2697(90)90595-z · Cited by 84,684
The CCP4 suite: programs for protein crystallography
Number Collaborative Computational Project (1994) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444994003112 · Cited by 17,317
Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination
Brünger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse‐Kunstleve, R. W., Jiang, J., Kuszewski, J. J., Nilges, M., Pannu, N., et al. (1998) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444998003254 · Cited by 15,723
Jones, T. A., Zou, J.-Y., Cowan, S. W., & Kjeldgaard, M. (1991) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767390010224 · Cited by 12,616
MOLMOL: A program for display and analysis of macromolecular structures
Koradi, R., Billeter, M., & Wüthrich, K. (1996) · Journal of Molecular Graphics · doi:10.1016/0263-7855(96)00009-4 · Cited by 7,156
LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions
Wallace, A. C., Laskowski, R. A., & Thornton, J. M. (1995) · Protein Engineering Design and Selection · doi:10.1093/protein/8.2.127 · Cited by 5,731
Nicholls, A. O., Sharp, K. A., & Honig, B. H. (1991) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340110407 · Cited by 5,230
AMoRe: an automated package for molecular replacement
Navaza, J. (1994) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767393007597 · Cited by 4,941
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ek, D. A. L., Baynes, B. M., Basu, S., Mena, M. A., & Lippow, S. M. (2009) · CRC Press eBooks · doi:10.1201/9781420076592.ch4 · Cited by 4
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Jokilaakso, N. (2013) · KTH Publication Database DiVA (KTH Royal Institute of Technology) · Cited by 1
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Jestin, J., & Pecorari, F. (2007) · doi:10.1002/9783527611478.ch9 · Cited by 1
Strecker, M. (2022) · Publication Server of Goethe University Frankfurt am Main (Goethe University Frankfurt) · doi:10.21248/gups.68021
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Huxford, T., & Ghosh, G. (2007) · Springer eBooks · doi:10.1007/0-387-33573-0_1
Dunn, I. S. (2009) · doi:10.1002/9780470551455.refs
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Wichmann, C. W., Becker, Y., & Grez, M. (2009) · doi:10.1002/9783527626830.ch6
Protein Engineering by Phage Display
Urvoas, A., Minard, P., & Soumillion, P. (2008) · doi:10.1002/9783527634026.ch24
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Kramer, K., Mahlknecht, G., & Hock, B. (2007) · doi:10.1002/9780470061565.hbb007
Rajagopal, S. (2007) · UA Campus Repository (The University of Arizona)
Design and recombinant production of combinatorial peptide libraries for gene delivery
de Raad, M. (2013) · Utrecht University Repository (Utrecht University)
Isolation and characterization of DARPins against human EphB4
Trun, W. (2011) · Universitätsbibliothek der FU Berlin Hochschulschriftenstelle u. Dokumentenserver · doi:10.17169/refubium-15770
de Navaraez, A. A. (2008) · University Library - University of Saskatchewan (University of Saskatchewan)
Analysis and redesign of protein-protein interactions: A hotspot-centric view
Layton, C. J. (2010) · DukeSpace (Duke University)
Molecular serum portraits - A step towards personalized medicine
Carlsson, A. (2010) · Lund University Publications (Lund University)
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Friedman, M. (2008) · KTH Publication Database DiVA (KTH Royal Institute of Technology)
Ng, D. T. W. (2013) · Scholarly Commons (University of Pennsylvania)
StaRProtein, A Web Server for Prediction of the Stability of Repeat Proteins
Xu, Y., Zhou, X., & Huang, M. (2015) · PLoS ONE · doi:10.1371/journal.pone.0119417
Chemical Synthesis of Affibody Molecules for Protein Detection and Molecular Imaging
Ekblad, T. (2008) · KTH Publication Database DiVA (KTH Royal Institute of Technology)
Fluorescence-based ligand assays for protein detection using affibody affinity proteins
Renberg, B. (2006) · KTH Publication Database DiVA (KTH Royal Institute of Technology)
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Heinz, D. W., Weiss, M. S., & Wendt, K. U. (2005) · ChemBioChem · doi:10.1002/cbic.200500459
Affibody molecules for proteomic and therapeutic applications
Grönwall, C. (2008) · KTH Publication Database DiVA (KTH Royal Institute of Technology)
Metadata
- 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
- Venue
- Nature Biotechnology
- Published
- 2004-04-18
- Volume
- 22
- Issue
- 5
- Pages
- 575-582
- ISSN
- 0733-222X (ISSN-L)
- 1087-0156
- 1546-1696
- 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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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