Esterification Delivers a Functional Enzyme into a Human Cell
| Autor: | Valerie T. Ressler, Kalie A. Mix, Ronald T. Raines |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
0301 basic medicine
Proteolysis media_common.quotation_subject Chemical biology 01 natural sciences Biochemistry Article 03 medical and health sciences chemistry.chemical_compound Ribonucleases medicine Humans Ribonuclease Internalization media_common chemistry.chemical_classification Esterification biology medicine.diagnostic_test 010405 organic chemistry Chemistry Esterases General Medicine 0104 chemical sciences Cytosol 030104 developmental biology Enzyme Biocatalysis biology.protein Molecular Medicine Diazo |
| Zdroj: | ACS Chemical Biology. 14:599-602 |
| ISSN: | 1554-8937 1554-8929 |
| DOI: | 10.1021/acschembio.9b00033 |
| Popis: | A major hurdle in chemical biology is the delivery of native proteins into the cytosol of mammalian cells. Herein, we report that esterification of the carboxyl groups of an enzyme with a diazo compound enables not only its passage into the cytosol, but also the retention of its catalytic activity there. This scenario is demonstrated with human ribonuclease 1, which manifests ribonucleolytic activity that can be cytotoxic. After internalization, the nascent esters are hydrolyzed in situ by endogenous esterases, making the process traceless. This strategy provides unprecedented opportunities for the delivery of functional enzymes into human cells. |
| Databáze: | OpenAIRE |
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