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Dichloro Butenediamides as irreversible site‐selective protein conjugation reagent
Angewandte Chemie International Edition, 2021-10, Vol.60 (44), p.23750-23755
Laserna, Victor
Abegg, Daniel
Afonso, Cláudia F.
Martin, Esther M.
Adibekian, Alexander
Ravn, Peter
Corzana, Francisco
Bernardes, Gonçalo
International ed. in English, 2021
Volltextzugriff (PDF)
Details
Autor(en) / Beteiligte
Laserna, Victor
Abegg, Daniel
Afonso, Cláudia F.
Martin, Esther M.
Adibekian, Alexander
Ravn, Peter
Corzana, Francisco
Bernardes, Gonçalo
Titel
Dichloro Butenediamides as irreversible site‐selective protein conjugation reagent
Ist Teil von
Angewandte Chemie International Edition, 2021-10, Vol.60 (44), p.23750-23755
Auflage
International ed. in English
Ort / Verlag
Germany: John Wiley & Sons, Inc
Erscheinungsjahr
2021
Quelle
MEDLINE
Beschreibungen/Notizen
© 2021 The Authors. Angewandte Chemie International Edition published by Wiley-VCH GmbH. This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. We describe maleic-acid derivatives as robust cysteine-selective reagents for protein labelling with comparable kinetics and superior stability relative to maleimides. Diamide and amido-ester derivatives proved to be efficient protein-labelling species with a common mechanism in which a spontaneous cyclization occurs upon addition to cysteine. Introduction of chlorine atoms in their structures triggers ring hydrolysis or further conjugation with adjacent residues, which results in conjugates that are completely resistant to retro-Michael reactions in the presence of biological thiols and human plasma. By controlling the microenvironment of the reactive site, we can control selectivity towards the hydrolytic pathway, forming homogeneous conjugates. The method is applicable to several scaffolds and enables conjugation of different payloads. The synthetic accessibility of these reagents and the mild conditions required for fast and complete conjugation together with the superior stability of the conjugates make this strategy an important alternative to maleimides in bioconjugation. This project has received funding from the European Union's Horizon 2020 research and innovation programme under the Marie Skłodowska-Curie grant agreement N° 836698 and under grant agreement N° 852985. Funding from the Scripps Research Institute (A.A.), FCT Portugal (PhD scholarship PD/BD/135512/2018 to C.F.A. and FCT Stimulus CEECIND/00453/2018 to G.J.L.B.) and Agencia Estatal Investigación of Spain (AEI; Grant RTI2018-099592-B-C21 to F.C.) is also acknowledged.
Sprache
Englisch
Identifikatoren
ISSN: 1433-7851
eISSN: 1521-3773
DOI: 10.1002/anie.202108791
Titel-ID: cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_8596790
Format
–
Schlagworte
Atomic structure
,
Bioconjugation
,
Blood plasma
,
Chlorine
,
Conjugates
,
Conjugation
,
Cysteine
,
Diamide - chemistry
,
Humans
,
Irreversibility
,
Labeling
,
Maleimides
,
Michael addition
,
Microenvironments
,
Models, Molecular
,
Molecular Structure
,
Payloads
,
Proteins
,
Proteins - chemistry
,
Reagents
,
Selectivity
,
Stability
,
Thiols
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