دورية أكاديمية

Chemoenzymatic Synthesis of 4,5-Dihydroxyisoleucine Fragment of α-Amanitin.

التفاصيل البيبلوغرافية
العنوان: Chemoenzymatic Synthesis of 4,5-Dihydroxyisoleucine Fragment of α-Amanitin.
المؤلفون: Chao TH; Department of Chemistry, BioScience Research Collaborative, Rice University, Houston, Texas 77005, United States., Renata H; Department of Chemistry, BioScience Research Collaborative, Rice University, Houston, Texas 77005, United States.
المصدر: Organic letters [Org Lett] 2024 Apr 19; Vol. 26 (15), pp. 3263-3266. Date of Electronic Publication: 2024 Apr 10.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: American Chemical Society Country of Publication: United States NLM ID: 100890393 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1523-7052 (Electronic) Linking ISSN: 15237052 NLM ISO Abbreviation: Org Lett Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Washington, DC : American Chemical Society, c1999-
مواضيع طبية MeSH: Alpha-Amanitin*/chemistry , Amanitins*/pharmacology, Isoleucine ; RNA Polymerase II/chemistry ; RNA Polymerase II/genetics ; RNA Polymerase II/metabolism
مستخلص: The ability of α-amanitin to potently inhibit RNA polymerase II (RNAP II) has elicited further research into its use as a novel payload for antibody-drug conjugates. Despite this promise, the de novo synthesis of α-amanitin is still a major challenge as it possesses an unusual bicyclic octapeptide structure that contains several oxidized amino acids, most notably 4,5-dihydroxy-l-isoleucine. Here, we report a concise chemoenzymatic synthesis of this key amino acid residue, which features two regioselective and diastereoselective enzymatic C-H oxidations on l-isoleucine.
المشرفين على المادة: 0 (Alpha-Amanitin)
0 (Amanitins)
04Y7590D77 (Isoleucine)
EC 2.7.7.- (RNA Polymerase II)
تواريخ الأحداث: Date Created: 20240410 Date Completed: 20240422 Latest Revision: 20240422
رمز التحديث: 20240422
DOI: 10.1021/acs.orglett.4c00901
PMID: 38598422
قاعدة البيانات: MEDLINE
الوصف
تدمد:1523-7052
DOI:10.1021/acs.orglett.4c00901