دورية أكاديمية
أعرض في EDS

Reductive site-selective atypical C , Z -type/N2-C2 cleavage allows C-terminal protein amidation.

التفاصيل البيبلوغرافية
العنوان: Reductive site-selective atypical C , Z -type/N2-C2 cleavage allows C-terminal protein amidation.
المؤلفون: Mollner TA; Department of Chemistry, Chemistry Research Laboratory, University of Oxford, Oxford, UK., Giltrap AM; The Rosalind Franklin Institute, Oxfordshire, UK., Zeng Y; The Rosalind Franklin Institute, Oxfordshire, UK., Demyanenko Y; The Rosalind Franklin Institute, Oxfordshire, UK., Buchanan C; Department of Chemistry, Chemistry Research Laboratory, University of Oxford, Oxford, UK., Oehlrich D; Global Medicinal Chemistry, Janssen Research & Development, Beerse, Belgium., Baldwin AJ; Department of Chemistry, Chemistry Research Laboratory, University of Oxford, Oxford, UK.; The Rosalind Franklin Institute, Oxfordshire, UK., Anthony DC; Department of Pharmacology, University of Oxford, Oxford, UK., Mohammed S; Department of Chemistry, Chemistry Research Laboratory, University of Oxford, Oxford, UK.; The Rosalind Franklin Institute, Oxfordshire, UK.; Department of Biochemistry, University of Oxford, Oxford, UK., Davis BG; Department of Chemistry, Chemistry Research Laboratory, University of Oxford, Oxford, UK.; The Rosalind Franklin Institute, Oxfordshire, UK.; Department of Pharmacology, University of Oxford, Oxford, UK.
المصدر: Science advances [Sci Adv] 2022 Apr 08; Vol. 8 (14), pp. eabl8675. Date of Electronic Publication: 2022 Apr 08.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: American Association for the Advancement of Science Country of Publication: United States NLM ID: 101653440 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 2375-2548 (Electronic) Linking ISSN: 23752548 NLM ISO Abbreviation: Sci Adv Subsets: PubMed not MEDLINE; MEDLINE
أسماء مطبوعة: Original Publication: Washington, DC : American Association for the Advancement of Science, [2015]-
مستخلص: Biomolecule environments can enhance chemistries with the potential to mediate and modulate self-modification (e.g., self-cleavage). While these enhanced modes are found in certain biomolecules (e.g., RNA ribozymes), it is more rare in proteins. Targeted proteolytic cleavage is vital to physiology, biotechnology, and even emerging therapy. Yet, purely chemically induced methods for the site-selective cleavage of proteins remain scarce. Here, as a proof of principle, we designed and tested a system intended to combine protein-enhanced chemistry with tag modification to enable synthetic reductive protein chemistries promoted by diboron. This reductively driven, single-electron chemistry now enables an operationally simple, site-selective cleavage protocol for proteins directed to readily accessible dehydroalanine (Dha) residues as tags under aqueous conditions and in cell lysates. In this way, a mild, efficient, enzyme-free method now allows not only precise chemical proteolysis but also simultaneous use in the removal of affinity tags and/or protein-terminus editing to create altered N- and C-termini such as protein amidation (─CONH 2 ).
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تواريخ الأحداث: Date Created: 20220408 Latest Revision: 20230403
رمز التحديث: 20231215
مُعرف محوري في PubMed: PMC8993120
DOI: 10.1126/sciadv.abl8675
PMID: 35394836
قاعدة البيانات: MEDLINE
الوصف
تدمد:2375-2548
DOI:10.1126/sciadv.abl8675