Academic Journal
Hexafluoroisopropanol as a Bioconjugation Medium of Ultrafast, Tryptophan-Selective Catalysis
| العنوان: | Hexafluoroisopropanol as a Bioconjugation Medium of Ultrafast, Tryptophan-Selective Catalysis |
|---|---|
| المؤلفون: | Mohammad Nuruzzaman, Brandon M. Colella, Chiamaka P. Uzoewulu, Alissa E. Meo, Elizabeth J. Gross, Seiya Ishizawa, Sravani Sana, He Zhang, Meredith E. Hoff, Bryce T. W. Medlock, Emily C. Joyner, Shinichi Sato, Elon A. Ison, Zibo Li, Jun Ohata |
| سنة النشر: | 2024 |
| مصطلحات موضوعية: | Biophysics, Biochemistry, Microbiology, Genetics, Biotechnology, Immunology, Developmental Biology, Inorganic Chemistry, Infectious Diseases, Computational Biology, Chemical Sciences not elsewhere classified, Information Systems not elsewhere classified, stabilization strategy achieved, report also demonstrates, core design element, noticeable side reactions, traditional aqueous processes, numerous chemical reactions, ultrafast lewis acid, suitable labeling reagent, selective bioconjugation methods, labeling reagent, catalyzed reactions, selective catalysis, chemical reaction, aqueous media, bioconjugation technology, bioconjugation techniques, bioconjugation process, bioconjugation medium |
| الوصف: | 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. |
| نوع الوثيقة: | article in journal/newspaper |
| اللغة: | unknown |
| Relation: | https://figshare.com/articles/journal_contribution/Hexafluoroisopropanol_as_a_Bioconjugation_Medium_of_Ultrafast_Tryptophan-Selective_Catalysis/25318130 |
| DOI: | 10.1021/jacs.3c13447.s001 |
| الاتاحة: | https://doi.org/10.1021/jacs.3c13447.s001 https://figshare.com/articles/journal_contribution/Hexafluoroisopropanol_as_a_Bioconjugation_Medium_of_Ultrafast_Tryptophan-Selective_Catalysis/25318130 |
| Rights: | CC BY-NC 4.0 |
| رقم الانضمام: | edsbas.8E52C445 |
| قاعدة البيانات: | BASE |
| DOI: | 10.1021/jacs.3c13447.s001 |
|---|