ArticleNature biotechnology2010
Spatially addressed combinatorial protein libraries for recombinant antibody discovery and optimization.
Article in Nature biotechnology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- An array of 60,000 antibodies for proteome-scale antibody generation and target discovery.Science advances · 2020Article
- Antibody Therapeutics in Oncology.Immunotherapy (Los Angeles, Calif.) · 2016Article
- Fc-Small Molecule Antibody Mimetics.Bioconjugate chemistry · 2015Article
- Matched Peptides: Tuning Matched Molecular Pair Analysis for Biopharmaceutical Applications.Journal of chemical information and modeling · 2015Article
- Structural and genetic diversity in antibody repertoires from diverse species.Current opinion in structural biology · 2015Review
- In vitro Fab display: a cell-free system for IgG discovery.Protein engineering, design & selection : PEDS · 2014Article
- Reshaping antibody diversity.Cell · 2013Article
- Simultaneous measurement of 10,000 protein-ligand affinity constants using microarray-based kinetic constant assays.Assay and drug development technologies · 2012Article
- Microarray-based method for screening of immunogenic proteins from bacteria.Journal of nanobiotechnology · 2012Article
- Bacterial display and screening of posttranslationally thioether-stabilized peptides.Applied and environmental microbiology · 2011Article
- Biotechnological applications of recombinant single-domain antibody fragments.Microbial cell factories · 2011Review
- Making antibodies from scratch.Nature biotechnology · 2010Article
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8 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Antibody discovery typically uses hybridoma- or display-based selection approaches, which lack the advantages of directly screening spatially addressed compound libraries as in small-molecule discovery. Here we apply the latter strategy to antibody discovery, using a library of ∼10,000 human germline antibody Fabs created by de novo DNA synthesis and automated protein expression and purification. In multiplexed screening assays, we obtained specific hits against seven of nine antigens. Using sequence-activity relationships and iterative mutagenesis, we optimized the binding affinities of two hits to the low nanomolar range. The matured Fabs showed full and partial antagonism activities in cell-based assays. Thus, protein drug leads can be discovered using surprisingly small libraries of proteins with known sequences, questioning the requirement for billions of members in an antibody discovery library. This methodology also provides sequence, expression and specificity information at the first step of the discovery process, and could enable novel antibody discovery in functional screens.
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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.