Cover Feature: Investigating a Boronate‐Affinity‐Guided Acylation Reaction for Labelling Native Antibodies (Chem. Eur. J. 17/2022)

A boronic acid based biorthogonal probe in combination with an acyl donor has been introduced that enables site‐specific incorporation of azide group at the Ser and Tyr residues of nonengineered full‐length antibody. Further derivatization of this functional site was accomplished through click react...

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Published inChemistry : a European journal Vol. 28; no. 17
Main Authors Adak, Avijit K., Huang, Kuan‐Ting, Liao, Chien‐Yu, Lee, Yuan‐Jung, Kuo, Wen‐Hua, Huo, Yi‐Ren, Li, Pei‐Jhen, Chen, Yi‐Ju, Chen, Bo‐Shiun, Chen, Yu‐Ju, Chu Hwang, Kuo, Wayne Chang, Wun‐Shang, Lin, Chun‐Cheng
Format Journal Article
LanguageEnglish
Published 22.03.2022
Subjects
antibodies
antibody-drug conjugates
boronate affinity
boronic acid
protein modifications
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Summary:A boronic acid based biorthogonal probe in combination with an acyl donor has been introduced that enables site‐specific incorporation of azide group at the Ser and Tyr residues of nonengineered full‐length antibody. Further derivatization of this functional site was accomplished through click reaction, yielding well‐defined immunoconjugates. The generality of this boronate‐affinity method has been demonstrated on a number of monoclonal antibodies, all with different binding specificities. More information can be found in the Research Article by W.‐S. Wayne Chang, C.‐C. Lin et al. (DOI: 10.1002/chem.202104178).
Bibliography:These authors contributed equally to this work.
ISSN:0947-6539
1521-3765
DOI:10.1002/chem.202200536