Targeting undruggable carbohydrate recognition sites through focused fragment library design
Carbohydrate–protein interactions are key for cell–cell and host–pathogen recognition, but their hydrophilic nature makes the development of drug-like inhibitors a challenge. Here, screening of fragment libraries identifies metal-binding pharmacophores as novel scaffolds for the inhibition of Ca2+-d...
Main Authors: | , , , , , , , , , , , |
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Format: | Article |
Language: | English |
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Nature Portfolio
2022-05-01
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Series: | Communications Chemistry |
Online Access: | https://doi.org/10.1038/s42004-022-00679-3 |
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author | Elena Shanina Sakonwan Kuhaudomlarp Eike Siebs Felix F. Fuchsberger Maxime Denis Priscila da Silva Figueiredo Celestino Gomes Mads H. Clausen Peter H. Seeberger Didier Rognan Alexander Titz Anne Imberty Christoph Rademacher |
author_facet | Elena Shanina Sakonwan Kuhaudomlarp Eike Siebs Felix F. Fuchsberger Maxime Denis Priscila da Silva Figueiredo Celestino Gomes Mads H. Clausen Peter H. Seeberger Didier Rognan Alexander Titz Anne Imberty Christoph Rademacher |
author_sort | Elena Shanina |
collection | DOAJ |
description | Carbohydrate–protein interactions are key for cell–cell and host–pathogen recognition, but their hydrophilic nature makes the development of drug-like inhibitors a challenge. Here, screening of fragment libraries identifies metal-binding pharmacophores as novel scaffolds for the inhibition of Ca2+-dependent carbohydrate–protein interactions. |
first_indexed | 2024-12-12T13:00:28Z |
format | Article |
id | doaj.art-4b306191f31141ed861dba296acb045e |
institution | Directory Open Access Journal |
issn | 2399-3669 |
language | English |
last_indexed | 2024-12-12T13:00:28Z |
publishDate | 2022-05-01 |
publisher | Nature Portfolio |
record_format | Article |
series | Communications Chemistry |
spelling | doaj.art-4b306191f31141ed861dba296acb045e2022-12-22T00:23:48ZengNature PortfolioCommunications Chemistry2399-36692022-05-015111110.1038/s42004-022-00679-3Targeting undruggable carbohydrate recognition sites through focused fragment library designElena Shanina0Sakonwan Kuhaudomlarp1Eike Siebs2Felix F. Fuchsberger3Maxime Denis4Priscila da Silva Figueiredo Celestino Gomes5Mads H. Clausen6Peter H. Seeberger7Didier Rognan8Alexander Titz9Anne Imberty10Christoph Rademacher11Max Planck Institute of Colloids and Interfaces, Department of Biomolecular Systems, Am Mühlenberg 1University Grenoble Alpes, CNRS, CERMAVChemical Biology of Carbohydrates (CBCH), Helmholtz Institute for Pharmaceutical Research Saarland (HIPS), Helmholtz Centre for Infection ResearchMax Planck Institute of Colloids and Interfaces, Department of Biomolecular Systems, Am Mühlenberg 1University of Vienna, Department of Pharmaceutical Sciences, Althanstrasse 14Laboratoire d’Innovation Thérapeutique, UMR 7200 CNRS-Université de StrasbourgTechnical University of Denmark, Center for Nanomedicine and Theranostics, Department of Chemistry, Kemitorvet 207Max Planck Institute of Colloids and Interfaces, Department of Biomolecular Systems, Am Mühlenberg 1Laboratoire d’Innovation Thérapeutique, UMR 7200 CNRS-Université de StrasbourgChemical Biology of Carbohydrates (CBCH), Helmholtz Institute for Pharmaceutical Research Saarland (HIPS), Helmholtz Centre for Infection ResearchUniversity Grenoble Alpes, CNRS, CERMAVMax Planck Institute of Colloids and Interfaces, Department of Biomolecular Systems, Am Mühlenberg 1Carbohydrate–protein interactions are key for cell–cell and host–pathogen recognition, but their hydrophilic nature makes the development of drug-like inhibitors a challenge. Here, screening of fragment libraries identifies metal-binding pharmacophores as novel scaffolds for the inhibition of Ca2+-dependent carbohydrate–protein interactions.https://doi.org/10.1038/s42004-022-00679-3 |
spellingShingle | Elena Shanina Sakonwan Kuhaudomlarp Eike Siebs Felix F. Fuchsberger Maxime Denis Priscila da Silva Figueiredo Celestino Gomes Mads H. Clausen Peter H. Seeberger Didier Rognan Alexander Titz Anne Imberty Christoph Rademacher Targeting undruggable carbohydrate recognition sites through focused fragment library design Communications Chemistry |
title | Targeting undruggable carbohydrate recognition sites through focused fragment library design |
title_full | Targeting undruggable carbohydrate recognition sites through focused fragment library design |
title_fullStr | Targeting undruggable carbohydrate recognition sites through focused fragment library design |
title_full_unstemmed | Targeting undruggable carbohydrate recognition sites through focused fragment library design |
title_short | Targeting undruggable carbohydrate recognition sites through focused fragment library design |
title_sort | targeting undruggable carbohydrate recognition sites through focused fragment library design |
url | https://doi.org/10.1038/s42004-022-00679-3 |
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