دورية أكاديمية
Hexafluoroisopropanol as a Bioconjugation Medium of Ultrafast, Tryptophan-Selective Catalysis.
| العنوان: | Hexafluoroisopropanol as a Bioconjugation Medium of Ultrafast, Tryptophan-Selective Catalysis. |
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| المؤلفون: | Nuruzzaman M; Department of Chemistry, North Carolina State University, Raleigh, North Carolina 27695, United States., Colella BM; Department of Chemistry, North Carolina State University, Raleigh, North Carolina 27695, United States., Uzoewulu CP; Department of Chemistry, North Carolina State University, Raleigh, North Carolina 27695, United States., Meo AE; Department of Chemistry, North Carolina State University, Raleigh, North Carolina 27695, United States., Gross EJ; Department of Chemistry, North Carolina State University, Raleigh, North Carolina 27695, United States., Ishizawa S; Department of Chemistry, North Carolina State University, Raleigh, North Carolina 27695, United States., Sana S; Department of Radiology and Biomedical Research Imaging Center, and UNC Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill, Raleigh, North Carolina 27599, United States., Zhang H; Department of Radiology and Biomedical Research Imaging Center, and UNC Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill, Raleigh, North Carolina 27599, United States., Hoff ME; Department of Chemistry, North Carolina State University, Raleigh, North Carolina 27695, United States., Medlock BTW; Department of Chemistry, North Carolina State University, Raleigh, North Carolina 27695, United States., Joyner EC; Department of Chemistry, North Carolina State University, Raleigh, North Carolina 27695, United States., Sato S; Frontier Research Institute for Interdisciplinary Sciences, Tohoku University, Sendai 980-8578, Japan., Ison EA; Department of Chemistry, North Carolina State University, Raleigh, North Carolina 27695, United States., Li Z; Department of Radiology and Biomedical Research Imaging Center, and UNC Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill, Raleigh, North Carolina 27599, United States., Ohata J; Department of Chemistry, North Carolina State University, Raleigh, North Carolina 27695, United States. |
| المصدر: | Journal of the American Chemical Society [J Am Chem Soc] 2024 Mar 13; Vol. 146 (10), pp. 6773-6783. Date of Electronic Publication: 2024 Feb 29. |
| نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't; Research Support, N.I.H., Extramural |
| اللغة: | English |
| بيانات الدورية: | Publisher: American Chemical Society Country of Publication: United States NLM ID: 7503056 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1520-5126 (Electronic) Linking ISSN: 00027863 NLM ISO Abbreviation: J Am Chem Soc Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: Washington, DC : American Chemical Society Original Publication: Easton, Pa. [etc.] |
| مواضيع طبية MeSH: | Tryptophan* , Proteins*/chemistry , Hydrocarbons, Fluorinated* , Propanols*, Peptides ; Catalysis |
| مستخلص: | The past decade has seen a remarkable growth in the number of bioconjugation techniques in chemistry, biology, material science, and biomedical fields. A core design element in bioconjugation technology is a chemical reaction that can form a covalent bond between the protein of interest and the labeling reagent. Achieving chemoselective protein bioconjugation in aqueous media is challenging, especially for generally less reactive amino acid residues, such as tryptophan. We present here the development of tryptophan-selective bioconjugation methods through ultrafast Lewis acid-catalyzed reactions in hexafluoroisopropanol (HFIP). Structure-reactivity relationship studies have revealed a combination of thiophene and ethanol moieties to give a suitable labeling reagent for this bioconjugation process, which enables modification of peptides and proteins in an extremely rapid reaction unencumbered by noticeable side reactions. The capability of the labeling method also facilitated radiofluorination application as well as antibody functionalization. Enhancement of an α-helix by HFIP leads to its compatibility with a certain protein, and this report also demonstrates a further stabilization strategy achieved by the addition of an ionic liquid to the HFIP medium. The nonaqueous bioconjugation approaches allow access to numerous chemical reactions that are unavailable in traditional aqueous processes and will further advance the chemistry of proteins. |
| معلومات مُعتمدة: | R01 EB029451 United States EB NIBIB NIH HHS |
| المشرفين على المادة: | 8DUH1N11BX (Tryptophan) 3D632GYQ50 (hexafluoroisopropanol) 0 (Proteins) 0 (Peptides) 0 (Hydrocarbons, Fluorinated) 0 (Propanols) |
| تواريخ الأحداث: | Date Created: 20240229 Date Completed: 20240314 Latest Revision: 20240710 |
| رمز التحديث: | 20240710 |
| DOI: | 10.1021/jacs.3c13447 |
| PMID: | 38421958 |
| قاعدة البيانات: | MEDLINE |
Find this issue from the American Chemical Society | تدمد: | 1520-5126 |
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| DOI: | 10.1021/jacs.3c13447 |