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.

Bibliographic Details
Main Authors: Anthony J. Quartararo, Zachary P. Gates, Bente A. Somsen, Nina Hartrampf, Xiyun Ye, Arisa Shimada, Yasuhiro Kajihara, Christian Ottmann, Bradley L. Pentelute
Format: Article
Language:English
Published: Nature Publishing Group 2020-06-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-020-16920-3
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spelling 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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