ArticleChembiochem : a European journal of chemical biology2014
Cell surface display yields evolvable, clickable antibody fragments.
Article in Chembiochem : a European journal of chemical biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 23 citations in OpenAlex.
- Design, Construction, and Validation of a Yeast-Displayed Chemically Expanded Antibody Library.ACS synthetic biology · 2025Article
- Reaching New Heights in Genetic Code Manipulation with High Throughput Screening.Chemical reviews · 2024Review
- Design, Construction, and Validation of a Yeast-Displayed Chemically Expanded Antibody Library.bioRxiv : the preprint server for biology · 2024Article
- Protein Engineering and High-Throughput Screening by Yeast Surface Display: Survey of Current Methods.Small science · 2023Article
- High-Throughput Aminoacyl-tRNA Synthetase Engineering for Genetic Code Expansion in Yeast.ACS synthetic biology · 2022Article
- An Optimized Synthesis of Fmoc-l-Homopropargylglycine-OH.The Journal of organic chemistry · 2022Article
- Incorporating, Quantifying, and Leveraging Noncanonical Amino Acids in Yeast.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Chemical Diversification of Simple Synthetic Antibodies.ACS chemical biology · 2021Article
- Directed Evolution Using Stabilized Bacterial Peptide Display.Journal of the American Chemical Society · 2020Article
- Future prospects for noncanonical amino acids in biological therapeutics.Current opinion in biotechnology · 2019Review
- A Robust and Quantitative Reporter System To Evaluate Noncanonical Amino Acid Incorporation in Yeast.ACS synthetic biology · 2018Article
- A platform for constructing, evaluating, and screening bioconjugates on the yeast surface.Protein engineering, design & selection : PEDS · 2016Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 2 countries.
Funding
Abstract
Non-canonical amino acids (ncAAs) provide powerful tools for engineering the chemical and physical properties of proteins. However, introducing ncAAs into proteins can affect protein properties in unpredictable ways, thus necessitating screening efforts to identify mutants with desirable properties. In this work, we describe an Escherichia coli cell surface display platform for the directed evolution of clickable antibody fragments. This platform enabled isolation of antibody fragments with improved digoxigenin binding and modest affinity maturation in several different ncAA contexts. Azide-functionalized fragments exhibited improved binding kinetics relative to their methionine counterparts, facile chemical modification through azide-alkyne cycloaddition, and retention of binding properties after modification. The results described here suggest new possibilities for protein engineering, including modulation of molecular recognition events by ncAAs and direct screening of libraries of chemically modified proteins.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.