Academic Journal

Protein Ligation and Labeling Enabled by a C‐Terminal Tetracysteine Tag

التفاصيل البيبلوغرافية
العنوان: Protein Ligation and Labeling Enabled by a C‐Terminal Tetracysteine Tag
المؤلفون: Mo, Zeyuan, Lin, Shaomin, Chen, Wentao, He, Chunmao
المساهمون: National Natural Science Foundation of China, Fundamental Research Funds for the Central Universities
المصدر: Angewandte Chemie International Edition ; volume 61, issue 15 ; ISSN 1433-7851 1521-3773
بيانات النشر: Wiley
سنة النشر: 2022
المجموعة: Wiley Online Library (Open Access Articles via Crossref)
الوصف: The hydrazinolysis of S‐cyanylated peptide provides an alternative way to afford protein α‐hydrazide, a key reagent used in native chemical ligation (NCL), without the aid of any inteins or enzymes. The currently used non‐selective S‐cyanylation, however, allows no other cysteine in the protein besides the one at the cleavage site. Herein, we report a regioselective S‐cyanylation and hydrazinolysis strategy achieved via the fusion of a tetracysteine tag to the C‐terminal of the protein of interest. We term it tetracysteine enabled protein ligation (TCEPL). While highly selective, the strategy is applicable for proteins expressed as inclusion bodies, and this was showcased by the efficient semi‐synthesis of an iron‐sulfur protein rubredoxin and the catalytic and hinge domains of matrix metalloprotease‐14 (MMP‐14) containing 207 amino acid residues. Furthermore, the TCEPL strategy was exploited for protein C‐terminal labeling with amino reagents bearing a variety of functional groups, demonstrating its versatility and generality.
نوع الوثيقة: article in journal/newspaper
اللغة: English
DOI: 10.1002/anie.202115377
الاتاحة: http://dx.doi.org/10.1002/anie.202115377
https://onlinelibrary.wiley.com/doi/pdf/10.1002/anie.202115377
https://onlinelibrary.wiley.com/doi/full-xml/10.1002/anie.202115377
Rights: http://onlinelibrary.wiley.com/termsAndConditions#vor
رقم الانضمام: edsbas.3BF8513A
قاعدة البيانات: BASE