Stoichiometric and irreversible cysteine-selective protein modification using carbonylacrylic reagents

Current cysteine bioconjugation strategies for protein-drug conjugates synthesis often yield heterogeneous and poorly stable products. Here, the authors use carbonylacrylic derivatives to selectively modify cysteine residues and synthesize biologically functional antibody conjugates highly stable in...

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Main Authors: Barbara Bernardim, Pedro M.S.D. Cal, Maria J. Matos, Bruno L. Oliveira, Nuria Martínez-Sáez, Inês S. Albuquerque, Elizabeth Perkins, Francisco Corzana, Antonio C.B. Burtoloso, Gonzalo Jiménez-Osés, Gonçalo J. L. Bernardes
Format: Article
Language:English
Published: Nature Portfolio 2016-10-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/ncomms13128
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author Barbara Bernardim
Pedro M.S.D. Cal
Maria J. Matos
Bruno L. Oliveira
Nuria Martínez-Sáez
Inês S. Albuquerque
Elizabeth Perkins
Francisco Corzana
Antonio C.B. Burtoloso
Gonzalo Jiménez-Osés
Gonçalo J. L. Bernardes
author_facet Barbara Bernardim
Pedro M.S.D. Cal
Maria J. Matos
Bruno L. Oliveira
Nuria Martínez-Sáez
Inês S. Albuquerque
Elizabeth Perkins
Francisco Corzana
Antonio C.B. Burtoloso
Gonzalo Jiménez-Osés
Gonçalo J. L. Bernardes
author_sort Barbara Bernardim
collection DOAJ
description Current cysteine bioconjugation strategies for protein-drug conjugates synthesis often yield heterogeneous and poorly stable products. Here, the authors use carbonylacrylic derivatives to selectively modify cysteine residues and synthesize biologically functional antibody conjugates highly stable in plasma.
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spelling doaj.art-c0d7ebdccc9c4ce596735356cd570e4c2022-12-21T19:09:19ZengNature PortfolioNature Communications2041-17232016-10-01711910.1038/ncomms13128Stoichiometric and irreversible cysteine-selective protein modification using carbonylacrylic reagentsBarbara Bernardim0Pedro M.S.D. Cal1Maria J. Matos2Bruno L. Oliveira3Nuria Martínez-Sáez4Inês S. Albuquerque5Elizabeth Perkins6Francisco Corzana7Antonio C.B. Burtoloso8Gonzalo Jiménez-Osés9Gonçalo J. L. Bernardes10Department of Chemistry, University of CambridgeDepartment of Chemistry, University of CambridgeDepartment of Chemistry, University of CambridgeDepartment of Chemistry, University of CambridgeDepartment of Chemistry, University of CambridgeInstituto de Medicina Molecular, Faculdade de Medicina, Universidade de LisboaAlbumedix Ltd, Castle CourtDepartment of Chemistry, University of CambridgeInstituto de Química de São Carlos, Universidade de São PauloDepartamento de Química, Universidad de La Rioja, Centro de Investigacioón en Síntesis QuímicaDepartment of Chemistry, University of CambridgeCurrent cysteine bioconjugation strategies for protein-drug conjugates synthesis often yield heterogeneous and poorly stable products. Here, the authors use carbonylacrylic derivatives to selectively modify cysteine residues and synthesize biologically functional antibody conjugates highly stable in plasma.https://doi.org/10.1038/ncomms13128
spellingShingle Barbara Bernardim
Pedro M.S.D. Cal
Maria J. Matos
Bruno L. Oliveira
Nuria Martínez-Sáez
Inês S. Albuquerque
Elizabeth Perkins
Francisco Corzana
Antonio C.B. Burtoloso
Gonzalo Jiménez-Osés
Gonçalo J. L. Bernardes
Stoichiometric and irreversible cysteine-selective protein modification using carbonylacrylic reagents
Nature Communications
title Stoichiometric and irreversible cysteine-selective protein modification using carbonylacrylic reagents
title_full Stoichiometric and irreversible cysteine-selective protein modification using carbonylacrylic reagents
title_fullStr Stoichiometric and irreversible cysteine-selective protein modification using carbonylacrylic reagents
title_full_unstemmed Stoichiometric and irreversible cysteine-selective protein modification using carbonylacrylic reagents
title_short Stoichiometric and irreversible cysteine-selective protein modification using carbonylacrylic reagents
title_sort stoichiometric and irreversible cysteine selective protein modification using carbonylacrylic reagents
url https://doi.org/10.1038/ncomms13128
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