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A dataset comprised of binding interactions for 104,972 antibodies against a SARS-CoV-2 peptide
The dataset presented here contains quantitative binding scores of scFv-format antibodies against a SARS-CoV-2 target peptide collected via an AlphaSeq assay that can be used in the development and benchmarking of machine learning models. Starting from three seed sequences identified from a phage di...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9606274/ https://www.ncbi.nlm.nih.gov/pubmed/36289234 http://dx.doi.org/10.1038/s41597-022-01779-4 |
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author | Engelhart, Emily Emerson, Ryan Shing, Leslie Lennartz, Chelsea Guion, Daniel Kelley, Mary Lin, Charles Lopez, Randolph Younger, David Walsh, Matthew E. |
author_facet | Engelhart, Emily Emerson, Ryan Shing, Leslie Lennartz, Chelsea Guion, Daniel Kelley, Mary Lin, Charles Lopez, Randolph Younger, David Walsh, Matthew E. |
author_sort | Engelhart, Emily |
collection | PubMed |
description | The dataset presented here contains quantitative binding scores of scFv-format antibodies against a SARS-CoV-2 target peptide collected via an AlphaSeq assay that can be used in the development and benchmarking of machine learning models. Starting from three seed sequences identified from a phage display campaign using a human naïve library, four sets of 29,900 antibodies were designed in silico by creating all k = 1 mutations and random k = 2 and k = 3 mutations throughout the complementary-determining regions (CDRs). Of the 119,600 designs, 104,972 were successfully built in to the AlphaSeq library and target binding was subsequently measured with 71,384 designs resulting in a predicted affinity value for at least one of the triplicate measurements. Data include antibodies with predicted affinity measurements ranging from 37 pM to 22 mM. To our knowledge, this dataset is the largest, publicly available dataset that contains antibody sequences, antigen sequence and quantitative measurements of binding scores and provides an opportunity to serve as a benchmark to evaluate antibody-specific representation models for machine learning. |
format | Online Article Text |
id | pubmed-9606274 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-96062742022-10-28 A dataset comprised of binding interactions for 104,972 antibodies against a SARS-CoV-2 peptide Engelhart, Emily Emerson, Ryan Shing, Leslie Lennartz, Chelsea Guion, Daniel Kelley, Mary Lin, Charles Lopez, Randolph Younger, David Walsh, Matthew E. Sci Data Data Descriptor The dataset presented here contains quantitative binding scores of scFv-format antibodies against a SARS-CoV-2 target peptide collected via an AlphaSeq assay that can be used in the development and benchmarking of machine learning models. Starting from three seed sequences identified from a phage display campaign using a human naïve library, four sets of 29,900 antibodies were designed in silico by creating all k = 1 mutations and random k = 2 and k = 3 mutations throughout the complementary-determining regions (CDRs). Of the 119,600 designs, 104,972 were successfully built in to the AlphaSeq library and target binding was subsequently measured with 71,384 designs resulting in a predicted affinity value for at least one of the triplicate measurements. Data include antibodies with predicted affinity measurements ranging from 37 pM to 22 mM. To our knowledge, this dataset is the largest, publicly available dataset that contains antibody sequences, antigen sequence and quantitative measurements of binding scores and provides an opportunity to serve as a benchmark to evaluate antibody-specific representation models for machine learning. Nature Publishing Group UK 2022-10-26 /pmc/articles/PMC9606274/ /pubmed/36289234 http://dx.doi.org/10.1038/s41597-022-01779-4 Text en © The Author(s) 2022 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Data Descriptor Engelhart, Emily Emerson, Ryan Shing, Leslie Lennartz, Chelsea Guion, Daniel Kelley, Mary Lin, Charles Lopez, Randolph Younger, David Walsh, Matthew E. A dataset comprised of binding interactions for 104,972 antibodies against a SARS-CoV-2 peptide |
title | A dataset comprised of binding interactions for 104,972 antibodies against a SARS-CoV-2 peptide |
title_full | A dataset comprised of binding interactions for 104,972 antibodies against a SARS-CoV-2 peptide |
title_fullStr | A dataset comprised of binding interactions for 104,972 antibodies against a SARS-CoV-2 peptide |
title_full_unstemmed | A dataset comprised of binding interactions for 104,972 antibodies against a SARS-CoV-2 peptide |
title_short | A dataset comprised of binding interactions for 104,972 antibodies against a SARS-CoV-2 peptide |
title_sort | dataset comprised of binding interactions for 104,972 antibodies against a sars-cov-2 peptide |
topic | Data Descriptor |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9606274/ https://www.ncbi.nlm.nih.gov/pubmed/36289234 http://dx.doi.org/10.1038/s41597-022-01779-4 |
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