Ultra-large chemical libraries for the discovery of high-affinity peptide binders
Synthetic peptide libraries can access broad chemical space, but generally examine only ~ 106 compounds. Here, the authors show that in-solution affinity selection, interfaced with nLC-MS/MS sequencing, can identify binders from fully randomized synthetic libraries of 108 members.
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2020-06-01
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Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/s41467-020-16920-3 |
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doaj-a74b9352b36b4fe7805bb71af9a0b66c2021-06-27T11:14:57ZengNature Publishing GroupNature Communications2041-17232020-06-0111111110.1038/s41467-020-16920-3Ultra-large chemical libraries for the discovery of high-affinity peptide bindersAnthony J. Quartararo0Zachary P. Gates1Bente A. Somsen2Nina Hartrampf3Xiyun Ye4Arisa Shimada5Yasuhiro Kajihara6Christian Ottmann7Bradley L. Pentelute8Department of Chemistry, Massachusetts Institute of TechnologyDepartment of Chemistry, Massachusetts Institute of TechnologyLaboratory of Chemical Biology, Department of Biomedical Engineering and Institute for Complex Molecular Systems, Eindhoven University of TechnologyDepartment of Chemistry, Massachusetts Institute of TechnologyDepartment of Chemistry, Massachusetts Institute of TechnologyDepartment of Chemistry, Graduate School of Science, Osaka UniversityDepartment of Chemistry, Graduate School of Science, Osaka UniversityLaboratory of Chemical Biology, Department of Biomedical Engineering and Institute for Complex Molecular Systems, Eindhoven University of TechnologyDepartment of Chemistry, Massachusetts Institute of TechnologySynthetic peptide libraries can access broad chemical space, but generally examine only ~ 106 compounds. Here, the authors show that in-solution affinity selection, interfaced with nLC-MS/MS sequencing, can identify binders from fully randomized synthetic libraries of 108 members.https://doi.org/10.1038/s41467-020-16920-3 |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Anthony J. Quartararo Zachary P. Gates Bente A. Somsen Nina Hartrampf Xiyun Ye Arisa Shimada Yasuhiro Kajihara Christian Ottmann Bradley L. Pentelute |
spellingShingle |
Anthony J. Quartararo Zachary P. Gates Bente A. Somsen Nina Hartrampf Xiyun Ye Arisa Shimada Yasuhiro Kajihara Christian Ottmann Bradley L. Pentelute Ultra-large chemical libraries for the discovery of high-affinity peptide binders Nature Communications |
author_facet |
Anthony J. Quartararo Zachary P. Gates Bente A. Somsen Nina Hartrampf Xiyun Ye Arisa Shimada Yasuhiro Kajihara Christian Ottmann Bradley L. Pentelute |
author_sort |
Anthony J. Quartararo |
title |
Ultra-large chemical libraries for the discovery of high-affinity peptide binders |
title_short |
Ultra-large chemical libraries for the discovery of high-affinity peptide binders |
title_full |
Ultra-large chemical libraries for the discovery of high-affinity peptide binders |
title_fullStr |
Ultra-large chemical libraries for the discovery of high-affinity peptide binders |
title_full_unstemmed |
Ultra-large chemical libraries for the discovery of high-affinity peptide binders |
title_sort |
ultra-large chemical libraries for the discovery of high-affinity peptide binders |
publisher |
Nature Publishing Group |
series |
Nature Communications |
issn |
2041-1723 |
publishDate |
2020-06-01 |
description |
Synthetic peptide libraries can access broad chemical space, but generally examine only ~ 106 compounds. Here, the authors show that in-solution affinity selection, interfaced with nLC-MS/MS sequencing, can identify binders from fully randomized synthetic libraries of 108 members. |
url |
https://doi.org/10.1038/s41467-020-16920-3 |
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